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Vasoactive intestinal polypeptide receptor 1 (VIP-R-1) (Pituitary adenylate cyclase-activating polypeptide type II receptor) (PACAP type II receptor) (PACAP-R-2) (PACAP-R2) (VPAC1)

 VIPR1_HUMAN             Reviewed;         457 AA.
P32241; A5JUT9; B3KPV1; B4DEB5; B4DGI4; F5H1F5; G3V0I1; Q15871;
Q6P2M6;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
30-AUG-2017, entry version 166.
RecName: Full=Vasoactive intestinal polypeptide receptor 1;
Short=VIP-R-1;
AltName: Full=Pituitary adenylate cyclase-activating polypeptide type II receptor;
Short=PACAP type II receptor;
Short=PACAP-R-2;
Short=PACAP-R2;
AltName: Full=VPAC1;
Flags: Precursor;
Name=VIPR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM SHORT).
TISSUE=Intestine;
PubMed=8390245; DOI=10.1006/bbrc.1993.1658;
Sreedharan S.P., Patel D.R., Huang J.-X., Goetzl E.J.;
"Cloning and functional expression of a human neuroendocrine
vasoactive intestinal peptide receptor.";
Biochem. Biophys. Res. Commun. 193:546-553(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), AND ALTERNATIVE
SPLICING.
TISSUE=Intestine;
PubMed=8179610; DOI=10.1006/bbrc.1994.1517;
Couvineau A., Rouyer-Fessard C., Darmoul D., Maoret J.J., Carrero I.,
Ogier-Denis E., Laburthe M.;
"Human intestinal VIP receptor: cloning and functional expression of
two cDNA encoding proteins with different N-terminal domains.";
Biochem. Biophys. Res. Commun. 200:769-776(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
"Genome-wide discovery and analysis of human seven transmembrane helix
receptor genes.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Lung;
Martin A.L., Kaighin V.A., Aronstam R.S.;
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SHORT; 3; 4 AND 5).
TISSUE=Brain, Cerebellum, Lung, and Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT), AND VARIANT
MET-341.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 33-457.
TISSUE=Liver;
PubMed=7917790; DOI=10.1016/0898-6568(94)90037-X;
Gagnon A.W., Aiyar N., Elshourbagy N.A.;
"Molecular cloning and functional characterization of a human liver
vasoactive intestinal peptide receptor.";
Cell. Signal. 6:321-333(1994).
[10]
INTERACTION WITH VIP.
PubMed=7818527; DOI=10.1006/bbrc.1995.1034;
Couvineau A., Gaudin P., Maoret J.J., Rouyer-Fessard C., Nicole P.,
Laburthe M.;
"Highly conserved aspartate 68, tryptophan 73 and glycine 109 in the
N-terminal extracellular domain of the human VIP receptor are
essential for its ability to bind VIP.";
Biochem. Biophys. Res. Commun. 206:246-252(1995).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=8926282; DOI=10.1007/BF01540969;
Xia M., Sreedharan S.P., Goetzl E.J.;
"Predominant expression of type II vasoactive intestinal peptide
receptors by human T lymphoblastoma cells: transduction of both Ca2+
and cyclic AMP signals.";
J. Clin. Immunol. 16:21-30(1996).
[12]
DISULFIDE BOND.
PubMed=9928020; DOI=10.1111/j.1749-6632.1998.tb11186.x;
Knudsen S.M., Tams J.W., Wulff B.S., Fahrenkrug J.;
"Importance of conserved cysteines in the extracellular loops of human
PACAP/VIP1 receptor for ligand binding and stimulation of cAMP
production.";
Ann. N. Y. Acad. Sci. 865:259-265(1998).
[13]
X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 400-408 IN COMPLEX WITH MHC.
PubMed=14734527; DOI=10.1084/jem.20031690;
Hulsmeyer M., Fiorillo M.T., Bettosini F., Sorrentino R., Saenger W.,
Ziegler A., Uchanska-Ziegler B.;
"Dual, HLA-B27 subtype-dependent conformation of a self-peptide.";
J. Exp. Med. 199:271-281(2004).
[14]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 400-408 IN COMPLEX WITH MHC.
PubMed=18650441; DOI=10.1074/jbc.M802818200;
Beltrami A., Rossmann M., Fiorillo M.T., Paladini F., Sorrentino R.,
Saenger W., Kumar P., Ziegler A., Uchanska-Ziegler B.;
"Citrullination-dependent differential presentation of a self-peptide
by HLA-B27 subtypes.";
J. Biol. Chem. 283:27189-27199(2008).
-!- FUNCTION: This is a receptor for VIP. The activity of this
receptor is mediated by G proteins which activate adenylyl
cyclase. The affinity is VIP = PACAP-27 > PACAP-38.
{ECO:0000269|PubMed:8926282}.
-!- INTERACTION:
P01282:VIP; NbExp=2; IntAct=EBI-3917984, EBI-6656819;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=Short; Synonyms=hIVR8;
IsoId=P32241-1; Sequence=Displayed;
Name=Long; Synonyms=hIVR5;
IsoId=P32241-2; Sequence=VSP_002010;
Name=3;
IsoId=P32241-3; Sequence=VSP_045143;
Name=4;
IsoId=P32241-4; Sequence=VSP_047271, VSP_047273;
Name=5;
IsoId=P32241-5; Sequence=VSP_047272;
-!- TISSUE SPECIFICITY: In lung, HT-29 colonic epithelial cells, Raji
B-lymphoblasts. Lesser extent in brain, heart, kidney, liver and
placenta. Not expressed in CD4+ or CD8+ T-cells. Expressed in the
T-cell lines HARRIS, HuT 78, Jurkat and SUP-T1, but not in the T-
cell lines Peer, MOLT-4, HSB and YT. {ECO:0000269|PubMed:8926282}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; L13288; AAA36805.1; -; mRNA.
EMBL; U11087; AAB60362.1; -; Genomic_DNA.
EMBL; U11079; AAB60362.1; JOINED; Genomic_DNA.
EMBL; U11080; AAB60362.1; JOINED; Genomic_DNA.
EMBL; U11081; AAB60362.1; JOINED; Genomic_DNA.
EMBL; U11083; AAB60362.1; JOINED; Genomic_DNA.
EMBL; U11084; AAB60362.1; JOINED; Genomic_DNA.
EMBL; U11085; AAB60362.1; JOINED; Genomic_DNA.
EMBL; U11086; AAB60362.1; JOINED; Genomic_DNA.
EMBL; X75299; CAA53046.1; -; mRNA.
EMBL; X77777; CAA54814.1; -; mRNA.
EMBL; AB065669; BAC05895.1; -; Genomic_DNA.
EMBL; EF577396; ABQ52416.1; -; mRNA.
EMBL; AK314334; BAG36980.1; -; mRNA.
EMBL; AK293548; BAG57026.1; -; mRNA.
EMBL; AK294609; BAG57795.1; -; mRNA.
EMBL; AK056819; BAG51813.1; -; mRNA.
EMBL; AC092047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64649.1; -; Genomic_DNA.
EMBL; CH471055; EAW64650.1; -; Genomic_DNA.
EMBL; BC064424; AAH64424.1; -; mRNA.
EMBL; L20295; AAA36802.1; -; mRNA.
CCDS; CCDS2698.1; -. [P32241-1]
CCDS; CCDS58827.1; -. [P32241-4]
CCDS; CCDS58828.1; -. [P32241-5]
CCDS; CCDS58829.1; -. [P32241-3]
PIR; JC2194; JC2194.
PIR; JC2195; JC2195.
RefSeq; NP_001238811.1; NM_001251882.1. [P32241-5]
RefSeq; NP_001238812.1; NM_001251883.1. [P32241-3]
RefSeq; NP_001238813.1; NM_001251884.1. [P32241-4]
RefSeq; NP_001238814.1; NM_001251885.1.
RefSeq; NP_004615.2; NM_004624.3. [P32241-1]
RefSeq; XP_005265495.1; XM_005265438.3. [P32241-5]
RefSeq; XP_011532381.1; XM_011534079.1. [P32241-5]
UniGene; Hs.348500; -.
PDB; 1OF2; X-ray; 2.20 A; C=400-408.
PDB; 1OGT; X-ray; 1.47 A; C=400-408.
PDB; 3B3I; X-ray; 1.86 A; C=400-408.
PDB; 3B6S; X-ray; 1.80 A; C=400-408.
PDB; 3DTX; X-ray; 2.10 A; C=400-408.
PDB; 3HCV; X-ray; 1.95 A; C=400-408.
PDB; 5DEF; X-ray; 1.60 A; C=400-408.
PDB; 5DEG; X-ray; 1.83 A; C=400-408.
PDB; 5IB1; X-ray; 1.91 A; C=400-408.
PDB; 5IB2; X-ray; 1.44 A; C=400-408.
PDB; 5IB3; X-ray; 1.91 A; C=400-408.
PDB; 5IB4; X-ray; 1.95 A; C=400-408.
PDB; 5IB5; X-ray; 2.49 A; C/F=400-408.
PDBsum; 1OF2; -.
PDBsum; 1OGT; -.
PDBsum; 3B3I; -.
PDBsum; 3B6S; -.
PDBsum; 3DTX; -.
PDBsum; 3HCV; -.
PDBsum; 5DEF; -.
PDBsum; 5DEG; -.
PDBsum; 5IB1; -.
PDBsum; 5IB2; -.
PDBsum; 5IB3; -.
PDBsum; 5IB4; -.
PDBsum; 5IB5; -.
ProteinModelPortal; P32241; -.
SMR; P32241; -.
BioGrid; 113274; 33.
IntAct; P32241; 4.
MINT; MINT-1217405; -.
STRING; 9606.ENSP00000327246; -.
BindingDB; P32241; -.
ChEMBL; CHEMBL5144; -.
GuidetoPHARMACOLOGY; 371; -.
TCDB; 9.A.14.4.9; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P32241; -.
PhosphoSitePlus; P32241; -.
BioMuta; VIPR1; -.
DMDM; 418253; -.
PaxDb; P32241; -.
PeptideAtlas; P32241; -.
PRIDE; P32241; -.
DNASU; 7433; -.
Ensembl; ENST00000325123; ENSP00000327246; ENSG00000114812. [P32241-1]
Ensembl; ENST00000433647; ENSP00000394950; ENSG00000114812. [P32241-5]
Ensembl; ENST00000438259; ENSP00000415371; ENSG00000114812. [P32241-3]
Ensembl; ENST00000543411; ENSP00000445701; ENSG00000114812. [P32241-4]
GeneID; 7433; -.
KEGG; hsa:7433; -.
UCSC; uc003clf.3; human. [P32241-1]
CTD; 7433; -.
DisGeNET; 7433; -.
GeneCards; VIPR1; -.
HGNC; HGNC:12694; VIPR1.
HPA; HPA026777; -.
MIM; 192321; gene.
neXtProt; NX_P32241; -.
OpenTargets; ENSG00000114812; -.
PharmGKB; PA37313; -.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00760000118800; -.
HOGENOM; HOG000008249; -.
HOVERGEN; HBG008318; -.
InParanoid; P32241; -.
KO; K04589; -.
OMA; FWWIIKT; -.
OrthoDB; EOG091G0NF8; -.
PhylomeDB; P32241; -.
TreeFam; TF315710; -.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-420092; Glucagon-type ligand receptors.
SIGNOR; P32241; -.
ChiTaRS; VIPR1; human.
EvolutionaryTrace; P32241; -.
GeneWiki; VIPR1; -.
GenomeRNAi; 7433; -.
PRO; PR:P32241; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114812; -.
CleanEx; HS_VIPR1; -.
ExpressionAtlas; P32241; baseline and differential.
Genevisible; P32241; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0007586; P:digestion; TAS:ProtInc.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
InterPro; IPR001571; GPCR_2_VIP_rcpt.
InterPro; IPR001771; GPCR_2_VIP_rcpt_1.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR00249; GPCRSECRETIN.
PRINTS; PR00491; VASOACTVEIPR.
PRINTS; PR01154; VIP1RECEPTOR.
SMART; SM00008; HormR; 1.
SUPFAM; SSF111418; SSF111418; 1.
PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Polymorphism; Receptor; Reference proteome; Signal; Transducer;
Transmembrane; Transmembrane helix.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 457 Vasoactive intestinal polypeptide
receptor 1.
/FTId=PRO_0000012855.
TOPO_DOM 31 142 Extracellular. {ECO:0000255}.
TRANSMEM 143 167 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 168 174 Cytoplasmic. {ECO:0000255}.
TRANSMEM 175 194 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 195 216 Extracellular. {ECO:0000255}.
TRANSMEM 217 240 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 241 254 Cytoplasmic. {ECO:0000255}.
TRANSMEM 255 276 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 277 292 Extracellular. {ECO:0000255}.
TRANSMEM 293 316 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 317 341 Cytoplasmic. {ECO:0000255}.
TRANSMEM 342 361 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 362 373 Extracellular. {ECO:0000255}.
TRANSMEM 374 393 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 394 457 Cytoplasmic. {ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 72 {ECO:0000250}.
DISULFID 63 105 {ECO:0000250}.
DISULFID 86 122 {ECO:0000250}.
DISULFID 215 285 {ECO:0000269|PubMed:9928020}.
VAR_SEQ 1 263 MRPPSPLPARWLCVLAGALAWALGPAGGQAARLQEECDYVQ
MIEVQHKQCLEEAQLENETIGCSKMWDNLTCWPATPRGQVV
VLACPLIFKLFSSIQGRNVSRSCTDEGWTHLEPGPYPIACG
LDDKAASLDEQQTMFYGSVKTGYTIGYGLSLATLLVATAIL
SLFRKLHCTRNYIHMHLFISFILRAAAVFIKDLALFDSGES
DQCSEGSVGCKAAMVFFQYCVMANFFWLLVEGLYLYTLLAV
SFFSERKYFWGYILIGW -> MTRQRVWMRWAVRQPWSFSN
IVSWLTSSGCWWRASTCTPCLPSPSSLSGSTSG (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045143.
VAR_SEQ 1 61 MRPPSPLPARWLCVLAGALAWALGPAGGQAARLQEECDYVQ
MIEVQHKQCLEEAQLENETI -> MRAGRRPRLGPWAG
(in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047271.
VAR_SEQ 1 41 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047272.
VAR_SEQ 1 32 MRPPSPLPARWLCVLAGALAWALGPAGGQAAR -> MPPPP
LLSLRRLGGGWSAVTRLVVAAAGARSRGGRGGSRGAGGGGR
GGVARRRRLELRAARSLLGSS (in isoform Long).
{ECO:0000303|PubMed:8179610}.
/FTId=VSP_002010.
VAR_SEQ 134 134 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047273.
VARIANT 341 341 R -> M (in dbSNP:rs17855906).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_055041.
VARIANT 445 445 R -> L (in dbSNP:rs3733055).
/FTId=VAR_020021.
CONFLICT 80 80 Q -> R (in Ref. 5; BAG57795).
{ECO:0000305}.
CONFLICT 284 284 G -> GLLR (in Ref. 2; CAA54814/CAA53046).
{ECO:0000305}.
CONFLICT 320 320 L -> F (in Ref. 5; BAG51813).
{ECO:0000305}.
CONFLICT 369 369 K -> R (in Ref. 5; BAG57795).
{ECO:0000305}.
SEQUENCE 457 AA; 51547 MW; DAA40CF5BEC47D7D CRC64;
MRPPSPLPAR WLCVLAGALA WALGPAGGQA ARLQEECDYV QMIEVQHKQC LEEAQLENET
IGCSKMWDNL TCWPATPRGQ VVVLACPLIF KLFSSIQGRN VSRSCTDEGW THLEPGPYPI
ACGLDDKAAS LDEQQTMFYG SVKTGYTIGY GLSLATLLVA TAILSLFRKL HCTRNYIHMH
LFISFILRAA AVFIKDLALF DSGESDQCSE GSVGCKAAMV FFQYCVMANF FWLLVEGLYL
YTLLAVSFFS ERKYFWGYIL IGWGVPSTFT MVWTIARIHF EDYGCWDTIN SSLWWIIKGP
ILTSILVNFI LFICIIRILL QKLRPPDIRK SDSSPYSRLA RSTLLLIPLF GVHYIMFAFF
PDNFKPEVKM VFELVVGSFQ GFVVAILYCF LNGEVQAELR RKWRRWHLQG VLGWNPKYRH
PSGGSNGATC STQVSMLTRV SPGARRSSSF QAEVSLV


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