5HT7R_HUMAN
ID 5HT7R_HUMAN Reviewed; 479 AA.
AC P34969; B5BUP6; P78336; P78372; P78516; Q5VX01; Q5VX02; Q5VX03;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=5-hydroxytryptamine receptor 7;
DE Short=5-HT-7;
DE Short=5-HT7;
DE AltName: Full=5-HT-X;
DE AltName: Full=Serotonin receptor 7;
GN Name=HTR7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=9084407; DOI=10.1046/j.1471-4159.1997.68041372.x;
RA Heidmann D.E.A., Metcalf M.A., Kohen R., Hamblin M.W.;
RT "Four 5-hydroxytryptamine7 (5-HT7) receptor isoforms in human and rat
RT produced by alternative splicing: species differences due to altered
RT intron-exon organization.";
RL J. Neurochem. 68:1372-1381(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Fetal brain, and Placenta;
RX PubMed=8226867; DOI=10.1016/s0021-9258(19)49479-9;
RA Bard J.A., Zgombick J.M., Adham N., Vaysse P., Branchek T.A.,
RA Weinshank R.L.;
RT "Cloning of a novel human serotonin receptor (5-HT7) positively linked to
RT adenylate cyclase.";
RL J. Biol. Chem. 268:23422-23426(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Brain;
RA King M.M., Aronstam R.S., Sharma S.V.;
RT "Isolation of cDNA coding for 5-hydroxytryptamine receptor 7, transcript
RT variant b (HTR7B).";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP GLYCOSYLATION AT ASN-5 AND ASN-66.
RX PubMed=22448645; DOI=10.1111/j.1742-4658.2012.08581.x;
RA Gellynck E., Andressen K.W., Lintermans B., Haegeman G., Levy F.O.,
RA Vanhoenacker P., Van Craenenbroeck K.;
RT "Biochemical and pharmacological study of N-linked glycosylation of the
RT human serotonin 5-HT(7)a receptor.";
RL FEBS J. 279:1994-2003(2012).
RN [10]
RP VARIANTS LYS-92 AND LEU-279.
RX PubMed=9154233;
RA Erdmann J., Nothen M.M., Shimron-Abarbanell D., Rietschel M., Albus M.,
RA Borrmann M., Maier W., Franzek E., Korner J., Weigelt B., Fimmers R.,
RA Propping P.;
RT "The human serotonin 7 (5-HT7) receptor gene: genomic organization and
RT systematic mutation screening in schizophrenia and bipolar affective
RT disorder.";
RL Mol. Psychiatry 1:392-397(1996).
CC -!- FUNCTION: This is one of the several different receptors for 5-
CC hydroxytryptamine (serotonin), a biogenic hormone that functions as a
CC neurotransmitter, a hormone, and a mitogen. The activity of this
CC receptor is mediated by G proteins that stimulate adenylate cyclase.
CC -!- INTERACTION:
CC P34969; P43243: MATR3; NbExp=2; IntAct=EBI-2625020, EBI-352602;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Isoform A and isoform B appear to be expressed at higher
CC levels.;
CC Name=D;
CC IsoId=P34969-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P34969-2; Sequence=VSP_001857;
CC Name=B;
CC IsoId=P34969-3; Sequence=VSP_001856;
CC -!- TISSUE SPECIFICITY: Isoform A is the predominant isoform in spleen,
CC caudate and hippocampus. Isoform B is expressed at lower levels.
CC Isoform D is a minor isoform in terms of expression.
CC {ECO:0000269|PubMed:9084407}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U68487; AAB48393.1; -; mRNA.
DR EMBL; U68488; AAB48394.1; -; mRNA.
DR EMBL; U68492; AAF07218.1; -; Genomic_DNA.
DR EMBL; U68493; AAF07217.1; -; Genomic_DNA.
DR EMBL; U68492; AAF07217.1; JOINED; Genomic_DNA.
DR EMBL; U68493; AAB48397.2; -; Genomic_DNA.
DR EMBL; U68492; AAB48397.2; JOINED; Genomic_DNA.
DR EMBL; L21195; AAC37538.1; -; mRNA.
DR EMBL; AY493988; AAR87480.1; -; mRNA.
DR EMBL; AK292606; BAF85295.1; -; mRNA.
DR EMBL; AB451482; BAG70296.1; -; mRNA.
DR EMBL; AL360011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW50118.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50119.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50120.1; -; Genomic_DNA.
DR EMBL; BC047526; AAH47526.1; -; mRNA.
DR CCDS; CCDS7408.1; -. [P34969-1]
DR CCDS; CCDS7409.1; -. [P34969-2]
DR CCDS; CCDS7410.1; -. [P34969-3]
DR PIR; A48881; A48881.
DR RefSeq; NP_000863.1; NM_000872.4. [P34969-2]
DR RefSeq; NP_062873.1; NM_019859.3. [P34969-1]
DR RefSeq; NP_062874.1; NM_019860.3. [P34969-3]
DR AlphaFoldDB; P34969; -.
DR SMR; P34969; -.
DR BioGRID; 109595; 5.
DR IntAct; P34969; 76.
DR STRING; 9606.ENSP00000337949; -.
DR BindingDB; P34969; -.
DR ChEMBL; CHEMBL3155; -.
DR DrugBank; DB06288; Amisulpride.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB00543; Amoxapine.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB14185; Aripiprazole lauroxil.
DR DrugBank; DB06216; Asenapine.
DR DrugBank; DB01200; Bromocriptine.
DR DrugBank; DB00248; Cabergoline.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB00924; Cyclobenzaprine.
DR DrugBank; DB00434; Cyproheptadine.
DR DrugBank; DB11273; Dihydroergocornine.
DR DrugBank; DB13345; Dihydroergocristine.
DR DrugBank; DB00988; Dopamine.
DR DrugBank; DB00751; Epinastine.
DR DrugBank; DB01049; Ergoloid mesylate.
DR DrugBank; DB12141; Gilteritinib.
DR DrugBank; DB00502; Haloperidol.
DR DrugBank; DB04946; Iloperidone.
DR DrugBank; DB00458; Imipramine.
DR DrugBank; DB00589; Lisuride.
DR DrugBank; DB04948; Lofexidine.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB08815; Lurasidone.
DR DrugBank; DB00934; Maprotiline.
DR DrugBank; DB00247; Methysergide.
DR DrugBank; DB06148; Mianserin.
DR DrugBank; DB01267; Paliperidone.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB01224; Quetiapine.
DR DrugBank; DB00734; Risperidone.
DR DrugBank; DB13988; SB-269970.
DR DrugBank; DB09304; Setiptiline.
DR DrugBank; DB13025; Tiapride.
DR DrugBank; DB09068; Vortioxetine.
DR DrugBank; DB00246; Ziprasidone.
DR DrugBank; DB00315; Zolmitriptan.
DR DrugBank; DB09225; Zotepine.
DR DrugCentral; P34969; -.
DR GuidetoPHARMACOLOGY; 12; -.
DR GlyGen; P34969; 2 sites.
DR iPTMnet; P34969; -.
DR PhosphoSitePlus; P34969; -.
DR BioMuta; HTR7; -.
DR DMDM; 8488960; -.
DR MassIVE; P34969; -.
DR PaxDb; P34969; -.
DR PeptideAtlas; P34969; -.
DR PRIDE; P34969; -.
DR ProteomicsDB; 54961; -. [P34969-1]
DR ProteomicsDB; 54962; -. [P34969-2]
DR ProteomicsDB; 54963; -. [P34969-3]
DR Antibodypedia; 16324; 436 antibodies from 36 providers.
DR DNASU; 3363; -.
DR Ensembl; ENST00000277874.10; ENSP00000277874.6; ENSG00000148680.16. [P34969-2]
DR Ensembl; ENST00000336152.8; ENSP00000337949.3; ENSG00000148680.16. [P34969-1]
DR Ensembl; ENST00000371719.2; ENSP00000360784.2; ENSG00000148680.16. [P34969-3]
DR GeneID; 3363; -.
DR KEGG; hsa:3363; -.
DR MANE-Select; ENST00000336152.8; ENSP00000337949.3; NM_019859.4; NP_062873.1.
DR UCSC; uc001kgz.4; human. [P34969-1]
DR CTD; 3363; -.
DR DisGeNET; 3363; -.
DR GeneCards; HTR7; -.
DR HGNC; HGNC:5302; HTR7.
DR HPA; ENSG00000148680; Group enriched (brain, parathyroid gland, testis).
DR MIM; 182137; gene.
DR neXtProt; NX_P34969; -.
DR OpenTargets; ENSG00000148680; -.
DR PharmGKB; PA29561; -.
DR VEuPathDB; HostDB:ENSG00000148680; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_6_1; -.
DR InParanoid; P34969; -.
DR OMA; GFPRPEK; -.
DR OrthoDB; 1327781at2759; -.
DR PhylomeDB; P34969; -.
DR TreeFam; TF331895; -.
DR PathwayCommons; P34969; -.
DR Reactome; R-HSA-390666; Serotonin receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR Reactome; R-HSA-9706019; RHOBTB3 ATPase cycle. [P34969-2]
DR SignaLink; P34969; -.
DR SIGNOR; P34969; -.
DR BioGRID-ORCS; 3363; 11 hits in 1066 CRISPR screens.
DR GeneWiki; 5-HT7_receptor; -.
DR GenomeRNAi; 3363; -.
DR Pharos; P34969; Tclin.
DR PRO; PR:P34969; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P34969; protein.
DR Bgee; ENSG00000148680; Expressed in sperm and 136 other tissues.
DR Genevisible; P34969; HS.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; TAS:ProtInc.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR InterPro; IPR001069; 5HT_7_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00652; 5HT7RECEPTR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..479
FT /note="5-hydroxytryptamine receptor 7"
FT /id="PRO_0000068979"
FT TOPO_DOM 1..83
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 84..104
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 105..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 118..138
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 139..157
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 158..178
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 179..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 202..222
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 223..236
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 237..257
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 258..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 326..346
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 347..367
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 368..388
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 389..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 401
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22448645"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22448645"
FT DISULFID 155..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 433..479
FT /note="RACTRRVLLRPEKRPPVSVWVLQSPDHHNWLADKMLTTVEKKVMIHD -> Q
FT NADYCRKKGHDS (in isoform A)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8226867"
FT /id="VSP_001857"
FT VAR_SEQ 433..479
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:19054851, ECO:0000303|Ref.3"
FT /id="VSP_001856"
FT VARIANT 92
FT /note="T -> K (in dbSNP:rs1379762209)"
FT /evidence="ECO:0000269|PubMed:9154233"
FT /id="VAR_012995"
FT VARIANT 279
FT /note="P -> L (in dbSNP:rs114969659)"
FT /evidence="ECO:0000269|PubMed:9154233"
FT /id="VAR_012996"
FT VARIANT 448
FT /note="P -> Q (in dbSNP:rs33954285)"
FT /id="VAR_049365"
SQ SEQUENCE 479 AA; 53555 MW; 1F62E985EADE1F23 CRC64;
MMDVNSSGRP DLYGHLRSFL LPEVGRGLPD LSPDGGADPV AGSWAPHLLS EVTASPAPTW
DAPPDNASGC GEQINYGRVE KVVIGSILTL ITLLTIAGNC LVVISVCFVK KLRQPSNYLI
VSLALADLSV AVAVMPFVSV TDLIGGKWIF GHFFCNVFIA MDVMCCTASI MTLCVISIDR
YLGITRPLTY PVRQNGKCMA KMILSVWLLS ASITLPPLFG WAQNVNDDKV CLISQDFGYT
IYSTAVAFYI PMSVMLFMYY QIYKAARKSA AKHKFPGFPR VEPDSVIALN GIVKLQKEVE
ECANLSRLLK HERKNISIFK REQKAATTLG IIVGAFTVCW LPFFLLSTAR PFICGTSCSC
IPLWVERTFL WLGYANSLIN PFIYAFFNRD LRTTYRSLLQ CQYRNINRKL SAAGMHEALK
LAERPERPEF VLRACTRRVL LRPEKRPPVS VWVLQSPDHH NWLADKMLTT VEKKVMIHD
