bio 2.0.3 → 2.0.5
This diff represents the content of publicly available package versions that have been released to one of the supported registries. The information contained in this diff is provided for informational purposes only and reflects changes between package versions as they appear in their respective public registries.
- checksums.yaml +4 -4
- data/.github/workflows/ruby.yml +38 -0
- data/.gitignore +32 -0
- data/ChangeLog +366 -0
- data/Gemfile +3 -0
- data/LEGAL +11 -0
- data/README.rdoc +1 -1
- data/RELEASE_NOTES.rdoc +50 -0
- data/appveyor.yml +14 -13
- data/bioruby.gemspec +9 -10
- data/lib/bio/appl/blast/genomenet.rb +2 -1
- data/lib/bio/appl/pts1.rb +1 -1
- data/lib/bio/db/embl/uniprotkb.rb +184 -26
- data/lib/bio/version.rb +1 -1
- data/test/data/uniprot/P03589.uniprot +127 -0
- data/test/data/uniprot/P28907.uniprot +551 -0
- data/test/data/uniprot/P49144.uniprot +232 -0
- data/test/functional/bio/test_command.rb +2 -0
- data/test/network/bio/db/kegg/test_genes_hsa7422.rb +26 -12
- data/test/unit/bio/db/embl/test_uniprotkb_P03589.rb +378 -0
- data/test/unit/bio/db/embl/test_uniprotkb_P28907.rb +325 -0
- data/test/unit/bio/db/embl/test_uniprotkb_P49144.rb +359 -0
- metadata +14 -15
- data/.travis.yml +0 -71
- data/gemfiles/Gemfile.travis-jruby1.8 +0 -6
- data/gemfiles/Gemfile.travis-jruby1.9 +0 -5
- data/gemfiles/Gemfile.travis-rbx +0 -10
- data/gemfiles/Gemfile.travis-ruby1.8 +0 -6
- data/gemfiles/Gemfile.travis-ruby1.9 +0 -5
- data/gemfiles/Gemfile.windows +0 -6
- data/gemfiles/modify-Gemfile.rb +0 -28
- data/gemfiles/prepare-gemspec.rb +0 -29
@@ -0,0 +1,232 @@
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ID 5HT1B_RABIT Reviewed; 390 AA.
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AC P49144;
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DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
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DT 01-FEB-1996, sequence version 1.
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DT 22-FEB-2023, entry version 127.
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DE RecName: Full=5-hydroxytryptamine receptor 1B;
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DE Short=5-HT-1B;
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DE Short=5-HT1B;
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DE AltName: Full=Serotonin 1D beta receptor;
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DE Short=5-HT-1D-beta;
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DE AltName: Full=Serotonin receptor 1B;
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GN Name=HTR1B;
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OS Oryctolagus cuniculus (Rabbit).
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OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
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OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
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OX NCBI_TaxID=9986;
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RN [1]
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RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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RC TISSUE=Liver;
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RX PubMed=8543023; DOI=10.1016/0014-5793(95)01308-3;
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RA Harwood G.S., Lockyer M., Giles H., Fairweather N.;
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RT "Cloning and characterisation of the rabbit 5-HT1D alpha and 5-HT1D beta
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RT receptors.";
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RL FEBS Lett. 377:73-76(1995).
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RN [2]
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RP NUCLEOTIDE SEQUENCE.
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RC STRAIN=New Zealand white; TISSUE=Saphenous vein;
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RA Wurch T., Cathala C., Palmer C., Valentin J.P., John G., Colpaert F.C.,
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RA Pauwels P.J.;
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RT "Molecular cloning and identification of a rabbit saphenous vein 5-HT 1DB
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RT receptor gene.";
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RL Neurosci. Res. Commun. 18:155-162(1996).
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RN [3]
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RP NUCLEOTIDE SEQUENCE.
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RC STRAIN=New Zealand white;
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RX PubMed=8878052; DOI=10.1007/bf00171053;
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RA Bard J.A., Kucharewicz S.A., Zgombick J.M., Weinshank R.L., Branchek T.A.,
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RA Cohen M.L.;
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RT "Differences in ligand binding profiles between cloned rabbit and human 5-
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RT HT1D alpha and 5-HT1D beta receptors: ketanserin and methiothepin
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RT distinguish rabbit 5-HT1D receptor subtypes.";
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RL Naunyn Schmiedebergs Arch. Pharmacol. 354:237-244(1996).
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CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
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CC (serotonin). Also functions as a receptor for various alkaloids and
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CC psychoactive substances. Ligand binding causes a conformation change
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CC that triggers signaling via guanine nucleotide-binding proteins (G
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CC proteins) and modulates the activity of down-stream effectors, such as
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CC adenylate cyclase. Signaling inhibits adenylate cyclase activity.
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CC Arrestin family members inhibit signaling via G proteins and mediate
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CC activation of alternative signaling pathways. Regulates the release of
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CC 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and
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CC thereby affects neural activity, nociceptive processing, pain
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CC perception, mood and behavior. Besides, plays a role in
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CC vasoconstriction of cerebral arteries.
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CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
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CC {ECO:0000250}.
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CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
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CC transmembrane helices. {ECO:0000250}.
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CC -!- PTM: Phosphorylated. {ECO:0000250}.
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CC -!- PTM: Palmitoylated. {ECO:0000250}.
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CC -!- MISCELLANEOUS: A residue in the 7th transmembrane region ('Thr-355' in
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CC human, 'Asn-351' in mouse and rat) is important for species-specific
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CC sensitivity to various agonists. {ECO:0000250}.
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CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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CC ---------------------------------------------------------------------------
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CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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CC ---------------------------------------------------------------------------
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DR EMBL; Z50163; CAA90531.1; -; Genomic_DNA.
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DR EMBL; X89731; CAA61883.1; -; mRNA.
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DR EMBL; U60826; AAB58467.1; -; Genomic_DNA.
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DR PIR; S58126; S58126.
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DR PIR; S68422; S68422.
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DR RefSeq; NP_001076259.1; NM_001082790.1.
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DR AlphaFoldDB; P49144; -.
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DR SMR; P49144; -.
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DR STRING; 9986.ENSOCUP00000016295; -.
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DR BindingDB; P49144; -.
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DR ChEMBL; CHEMBL5717; -.
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DR GlyCosmos; P49144; 2 sites, No reported glycans.
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DR GeneID; 100009594; -.
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84
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DR KEGG; ocu:100009594; -.
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DR CTD; 3351; -.
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DR eggNOG; KOG3656; Eukaryota.
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DR InParanoid; P49144; -.
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DR OrthoDB; 2999405at2759; -.
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DR TreeFam; TF316350; -.
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DR PRO; PR:P49144; -.
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DR Proteomes; UP000001811; Unplaced.
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DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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DR GO; GO:0045202; C:synapse; IEA:GOC.
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DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISS:UniProtKB.
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DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
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DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
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DR GO; GO:0046849; P:bone remodeling; IEA:InterPro.
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DR GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
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DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
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DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
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DR GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB.
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DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
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DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
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DR CDD; cd15333; 7tmA_5-HT1B_1D; 1.
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DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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DR InterPro; IPR002147; 5HT1B_rcpt.
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DR InterPro; IPR002231; 5HT_rcpt.
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DR InterPro; IPR000276; GPCR_Rhodpsn.
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DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
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DR PANTHER; PTHR24248:SF66; OCTOPAMINE RECEPTOR BETA-3R; 1.
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DR Pfam; PF00001; 7tm_1; 1.
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DR PRINTS; PR00513; 5HT1BRECEPTR.
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DR PRINTS; PR01101; 5HTRECEPTOR.
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DR PRINTS; PR00237; GPCRRHODOPSN.
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DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
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DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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PE 2: Evidence at transcript level;
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KW Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
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KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
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KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
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FT CHAIN 1..390
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FT /note="5-hydroxytryptamine receptor 1B"
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FT /id="PRO_0000068920"
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FT TOPO_DOM 1..49
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FT /note="Extracellular"
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FT /evidence="ECO:0000250"
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FT TRANSMEM 50..75
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FT /note="Helical; Name=1"
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FT /evidence="ECO:0000250"
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FT TOPO_DOM 76..84
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FT /note="Cytoplasmic"
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FT /evidence="ECO:0000250"
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FT TRANSMEM 85..110
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FT /note="Helical; Name=2"
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FT /evidence="ECO:0000250"
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FT TOPO_DOM 111..123
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FT /note="Extracellular"
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FT /evidence="ECO:0000250"
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FT TRANSMEM 124..145
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FT /note="Helical; Name=3"
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FT /evidence="ECO:0000250"
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FT TOPO_DOM 146..165
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FT /note="Cytoplasmic"
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FT /evidence="ECO:0000250"
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FT TRANSMEM 166..187
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FT /note="Helical; Name=4"
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FT /evidence="ECO:0000250"
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FT TOPO_DOM 188..205
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FT /note="Extracellular"
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FT /evidence="ECO:0000250"
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FT TRANSMEM 206..228
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FT /note="Helical; Name=5"
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FT /evidence="ECO:0000250"
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FT TOPO_DOM 229..315
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FT /note="Cytoplasmic"
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FT /evidence="ECO:0000250"
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FT TRANSMEM 316..336
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FT /note="Helical; Name=6"
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FT /evidence="ECO:0000250"
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FT TOPO_DOM 337..349
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FT /note="Extracellular"
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FT /evidence="ECO:0000250"
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FT TRANSMEM 350..371
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FT /note="Helical; Name=7"
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FT /evidence="ECO:0000250"
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FT TOPO_DOM 372..390
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FT /note="Cytoplasmic"
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FT /evidence="ECO:0000250"
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FT REGION 260..282
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FT /note="Disordered"
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FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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FT MOTIF 146..148
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FT /note="DRY motif; important for ligand-induced conformation
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FT changes and signaling"
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FT /evidence="ECO:0000250"
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FT MOTIF 365..369
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FT /note="NPxxY motif; important for ligand-induced
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FT conformation changes and signaling"
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FT /evidence="ECO:0000250"
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FT BINDING 129
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FT /ligand="ergotamine"
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FT /ligand_id="ChEBI:CHEBI:190463"
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FT /ligand_note="agonist"
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FT /evidence="ECO:0000250|UniProtKB:P28222"
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FT BINDING 134
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FT /ligand="ergotamine"
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FT /ligand_id="ChEBI:CHEBI:190463"
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FT /ligand_note="agonist"
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FT /evidence="ECO:0000250|UniProtKB:P28222"
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FT BINDING 201
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FT /ligand="ergotamine"
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FT /ligand_id="ChEBI:CHEBI:190463"
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FT /ligand_note="agonist"
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FT /evidence="ECO:0000250|UniProtKB:P28222"
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FT SITE 355
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FT /note="Important for species-specific agonist sensitivity"
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FT /evidence="ECO:0000250"
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FT LIPID 388
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FT /note="S-palmitoyl cysteine"
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FT /evidence="ECO:0000255"
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FT CARBOHYD 24
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FT /note="N-linked (GlcNAc...) asparagine"
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FT /evidence="ECO:0000255"
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FT CARBOHYD 32
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FT /note="N-linked (GlcNAc...) asparagine"
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FT /evidence="ECO:0000255"
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FT DISULFID 122..199
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FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
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FT CONFLICT 5
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FT /note="G -> S (in Ref. 1 and 3)"
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FT /evidence="ECO:0000305"
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FT CONFLICT 7
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FT /note="Q -> R (in Ref. 1 and 3)"
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FT /evidence="ECO:0000305"
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FT CONFLICT 14
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FT /note="Missing (in Ref. 1 and 3)"
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FT /evidence="ECO:0000305"
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FT CONFLICT 171
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FT /note="R -> A (in Ref. 1 and 3)"
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FT /evidence="ECO:0000305"
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SQ SEQUENCE 390 AA; 43496 MW; C22EBC077C6C897D CRC64;
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MEEPGAQCAP PLAAGSQIAV PQANLSAAHS HNCSAEGYIY QDSIALPWKV LLVLLLALFT
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LATTLSNAFV VATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV
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VCDLWLSSDI TCCTASIMHL CVIALDRYWA ITDAVEYSAK RTPKRAAIMI RLVWVFSICI
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SLPPFFWRQA KAEEEVSECL VNTDHVLYTV YSTVGAFYLP TLLLIALYGR IYVEARSRIL
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KQTPNRTGKR LTRAQLITDS PGSTTSVTSI NSRAPDVPSE SGSPVYVNQV KVRVSDALLE
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KKKLMAARER KATKTLGIIL GVFIVCWLPF FIISLVMPIC KDACWFHQAI FDFFTWLGYV
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NSLINPIIYT MSNEDFKQAF HKLIRFKCTS
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//
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@@ -187,8 +187,10 @@ module Bio
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return
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end
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assert_equal('', str.to_s.strip)
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assert_equal('', err.to_s.strip)
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str, err = Bio::Command.query_command_open3(ary, @data)
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assert_equal(@sorted, str.to_s.strip.split(/\s+/))
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assert_equal('', err.to_s.strip)
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end
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end #class FuncTestCommandQuery
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@@ -38,7 +38,8 @@ module Bio
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"H01457 Diabetic retinopathy",
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"H01459 Diabetic neuropathy",
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"H01529 Avascular necrosis of femoral head",
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"H01709 Glucocorticoid-induced osteonecrosis"
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"H01709 Glucocorticoid-induced osteonecrosis",
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"H02559 Microvascular complications of diabetes"]
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assert_equal(expected, @obj.diseases_as_strings)
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end
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@@ -48,41 +49,54 @@ module Bio
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"H01457"=>"Diabetic retinopathy",
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"H01459"=>"Diabetic neuropathy",
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"H01529"=>"Avascular necrosis of femoral head",
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"H01709"=>"Glucocorticoid-induced osteonecrosis"
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"H01709"=>"Glucocorticoid-induced osteonecrosis",
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"H02559"=>"Microvascular complications of diabetes"}
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assert_equal(expected, @obj.diseases_as_hash)
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end
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def test_drug_targets_as_strings
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expected = ["Abicipar pegol: D11517",
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"Aflibercept: D09574",
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"Aflibercept beta: D10819",
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"Bevacizumab: D06409",
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"Aflibercept: D09574<JP/US>",
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"Aflibercept beta: D10819<JP>",
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"Bevacizumab: D06409<JP/US>",
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"Bevasiranib sodium: D08874",
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"Brolucizumab: D11083",
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-
"
|
63
|
+
"Brolucizumab: D11083<JP/US>",
|
64
|
+
"Dilpacimab: D11642",
|
65
|
+
"Emvododstat: D11890",
|
66
|
+
"Faricimab: D11516<JP/US>",
|
63
67
|
"Navicixizumab: D11126",
|
64
68
|
"Pegaptanib: D05386",
|
65
|
-
"Ranibizumab: D05697",
|
69
|
+
"Ranibizumab: D05697<JP/US>",
|
70
|
+
"Tarcocimab: D12507",
|
71
|
+
"Tarcocimab tedromer: D12508",
|
66
72
|
"Vanucizumab: D11244"]
|
67
73
|
assert_equal(expected, @obj.drug_targets_as_strings)
|
68
74
|
end
|
69
75
|
|
70
76
|
def test_networks_as_strings
|
71
|
-
expected = ["
|
72
|
-
"nt06124 Chemokine signaling (virus)",
|
77
|
+
expected = ["nt06124 Chemokine signaling (viruses)",
|
73
78
|
"nt06164 Kaposi sarcoma-associated herpesvirus (KSHV)",
|
74
|
-
"nt06214 PI3K signaling",
|
75
79
|
"nt06219 JAK-STAT signaling",
|
76
80
|
"nt06224 CXCR signaling",
|
77
81
|
"nt06225 HIF-1 signaling",
|
82
|
+
"nt06227 Nuclear receptor signaling",
|
78
83
|
"nt06262 Pancreatic cancer",
|
79
84
|
"nt06264 Renal cell carcinoma",
|
85
|
+
"nt06360 Cushing syndrome",
|
86
|
+
"nt06526 MAPK signaling",
|
87
|
+
"nt06528 Calcium signaling",
|
88
|
+
"nt06530 PI3K signaling",
|
80
89
|
"N00079 HIF-1 signaling pathway",
|
81
90
|
"N00080 Loss of VHL to HIF-1 signaling pathway",
|
82
91
|
"N00081 Mutation-inactivated VHL to HIF-1 signaling pathway",
|
83
92
|
"N00095 ERBB2-overexpression to EGF-Jak-STAT signaling pathway",
|
84
93
|
"N00157 KSHV vGPCR to GNB/G-ERK signaling pathway",
|
85
|
-
"
|
94
|
+
"N00317 AhR signaling pathway",
|
95
|
+
"N01412 Metals to HTF-1 signaling pathway",
|
96
|
+
"N01592 GF-RTK-RAS-ERK signaling pathway",
|
97
|
+
"N01641 RTK-PLCG-ITPR signaling pathway",
|
98
|
+
"N01656 GF-RTK-PI3K signaling pathway",
|
99
|
+
"N01658 GF-RTK-RAS-PI3K signaling pathway"]
|
86
100
|
assert_equal(expected, @obj.networks_as_strings)
|
87
101
|
end
|
88
102
|
|