VIPR2_HUMAN
ID VIPR2_HUMAN Reviewed; 438 AA.
AC P41587; Q13053; Q15870; Q53Y09; Q6ZN22; Q9UCW0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Vasoactive intestinal polypeptide receptor 2;
DE Short=VIP-R-2;
DE AltName: Full=Helodermin-preferring VIP receptor;
DE AltName: Full=Pituitary adenylate cyclase-activating polypeptide type III receptor;
DE Short=PACAP type III receptor;
DE Short=PACAP-R-3;
DE Short=PACAP-R3;
DE AltName: Full=VPAC2;
DE Flags: Precursor;
GN Name=VIPR2; Synonyms=VIP2R;
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] (ISOFORM 1).
RX PubMed=7811244; DOI=10.1006/bbrc.1994.2852;
RA Svoboda M., Tastenoy M., van Rampelbergh J., Goossens J.-F., Neef P.,
RA Waelbroeck M., Robberecht P.;
RT "Molecular cloning and functional characterization of a human VIP receptor
RT from SUP-T1 lymphoblasts.";
RL Biochem. Biophys. Res. Commun. 205:1617-1624(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8938447; DOI=10.1006/geno.1996.0569;
RA Mackay M., Fantes J., Scherer S., Boyle S., West K., Tsui L.-C.,
RA Belloni E., Lutz E., van Heyningen V., Harmar A.J.;
RT "Chromosomal localization in mouse and human of the vasoactive intestinal
RT peptide receptor type 2 gene: a possible contributor to the
RT holoprosencephaly 3 phenotype.";
RL Genomics 37:345-353(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
RX PubMed=8933357; DOI=10.1046/j.1365-2826.1996.05191.x;
RA Wei Y., Mojsov S.;
RT "Tissue specific expression of different human receptor types for pituitary
RT adenylate cyclase activating polypeptide and vasoactive intestinal
RT polypeptide: implications for their role in human physiology.";
RL J. Neuroendocrinol. 8:811-817(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=10481065; DOI=10.1016/s0014-5793(99)01135-7;
RA Lutz E.M., Shen S., Mackay M., West K., Harmar A.J.;
RT "Structure of the human VIP2R gene for vasoactive intestinal peptide type 2
RT receptor.";
RL FEBS Lett. 458:197-203(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [9]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-318 (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=T-cell;
RX PubMed=8926282; DOI=10.1007/bf01540969;
RA Xia M., Sreedharan S.P., Goetzl E.J.;
RT "Predominant expression of type II vasoactive intestinal peptide receptors
RT by human T lymphoblastoma cells: transduction of both Ca2+ and cyclic AMP
RT signals.";
RL J. Clin. Immunol. 16:21-30(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-118, AND DISULFIDE BONDS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the extracellular domain of human vasoactive
RT intestinal polypeptide receptor 2.";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- FUNCTION: This is a receptor for VIP as well as PACAP-38 and -27, the
CC activity of this receptor is mediated by G proteins which activate
CC adenylyl cyclase. Can be coupled to phospholipase C.
CC {ECO:0000269|PubMed:8926282}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P41587-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41587-2; Sequence=VSP_056684, VSP_056685;
CC -!- TISSUE SPECIFICITY: Expressed in CD4+ T-cells, but not in CD8+ T-cells.
CC Expressed in the T-cell lines Jurkat, Peer, MOLT-4, HSB, YT and SUP-T1,
CC but not in the T-cell lines HARRIS and HuT 78.
CC {ECO:0000269|PubMed:8926282}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; L36566; AAC37569.1; -; mRNA.
DR EMBL; L40764; AAC41756.1; -; Genomic_DNA.
DR EMBL; U18810; AAC50872.1; -; mRNA.
DR EMBL; X95097; CAA64474.1; -; mRNA.
DR EMBL; Y18423; CAB41899.1; -; Genomic_DNA.
DR EMBL; Y18424; CAB41899.1; JOINED; Genomic_DNA.
DR EMBL; Y18425; CAB41899.1; JOINED; Genomic_DNA.
DR EMBL; Y18426; CAB41899.1; JOINED; Genomic_DNA.
DR EMBL; Y18427; CAB41899.1; JOINED; Genomic_DNA.
DR EMBL; Y18428; CAB41899.1; JOINED; Genomic_DNA.
DR EMBL; Y18429; CAB41899.1; JOINED; Genomic_DNA.
DR EMBL; Y18430; CAB41899.1; JOINED; Genomic_DNA.
DR EMBL; Y18431; CAB41899.1; JOINED; Genomic_DNA.
DR EMBL; BT007118; AAP35782.1; -; mRNA.
DR EMBL; AK131406; BAD18553.1; -; mRNA.
DR EMBL; AC004863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF027390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236954; EAL23936.1; -; Genomic_DNA.
DR EMBL; CH471149; EAX04596.1; -; Genomic_DNA.
DR EMBL; BC010569; AAH10569.1; -; mRNA.
DR CCDS; CCDS5950.1; -. [P41587-1]
DR CCDS; CCDS78295.1; -. [P41587-2]
DR PIR; G02822; G02822.
DR RefSeq; NP_001291451.1; NM_001304522.1.
DR RefSeq; NP_001295188.1; NM_001308259.1. [P41587-2]
DR RefSeq; NP_003373.2; NM_003382.4. [P41587-1]
DR PDB; 2X57; X-ray; 2.10 A; A/B/C=26-118.
DR PDBsum; 2X57; -.
DR AlphaFoldDB; P41587; -.
DR SMR; P41587; -.
DR BioGRID; 113275; 205.
DR IntAct; P41587; 96.
DR MINT; P41587; -.
DR STRING; 9606.ENSP00000262178; -.
DR BindingDB; P41587; -.
DR ChEMBL; CHEMBL4532; -.
DR GuidetoPHARMACOLOGY; 372; -.
DR GlyGen; P41587; 3 sites.
DR iPTMnet; P41587; -.
DR PhosphoSitePlus; P41587; -.
DR BioMuta; VIPR2; -.
DR DMDM; 2506490; -.
DR MassIVE; P41587; -.
DR PaxDb; P41587; -.
DR PeptideAtlas; P41587; -.
DR PRIDE; P41587; -.
DR ProteomicsDB; 55470; -. [P41587-1]
DR ProteomicsDB; 67967; -.
DR Antibodypedia; 18979; 329 antibodies from 35 providers.
DR DNASU; 7434; -.
DR Ensembl; ENST00000262178.7; ENSP00000262178.2; ENSG00000106018.14. [P41587-1]
DR Ensembl; ENST00000377633.7; ENSP00000366860.3; ENSG00000106018.14. [P41587-2]
DR GeneID; 7434; -.
DR KEGG; hsa:7434; -.
DR MANE-Select; ENST00000262178.7; ENSP00000262178.2; NM_003382.5; NP_003373.2.
DR UCSC; uc064jts.1; human. [P41587-1]
DR CTD; 7434; -.
DR DisGeNET; 7434; -.
DR GeneCards; VIPR2; -.
DR HGNC; HGNC:12695; VIPR2.
DR HPA; ENSG00000106018; Low tissue specificity.
DR MalaCards; VIPR2; -.
DR MIM; 601970; gene.
DR neXtProt; NX_P41587; -.
DR OpenTargets; ENSG00000106018; -.
DR PharmGKB; PA37314; -.
DR VEuPathDB; HostDB:ENSG00000106018; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000158089; -.
DR HOGENOM; CLU_002753_4_4_1; -.
DR InParanoid; P41587; -.
DR OMA; KACTGVW; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P41587; -.
DR TreeFam; TF315710; -.
DR PathwayCommons; P41587; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P41587; -.
DR BioGRID-ORCS; 7434; 14 hits in 1071 CRISPR screens.
DR ChiTaRS; VIPR2; human.
DR GeneWiki; VIPR2; -.
DR GenomeRNAi; 7434; -.
DR Pharos; P41587; Tchem.
DR PRO; PR:P41587; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P41587; protein.
DR Bgee; ENSG00000106018; Expressed in mucosa of stomach and 129 other tissues.
DR ExpressionAtlas; P41587; baseline and differential.
DR Genevisible; P41587; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; IBA:GO_Central.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR001571; GPCR_2_VIP_rcpt.
DR InterPro; IPR002284; GPCR_2_VIP_rcpt_2.
DR PANTHER; PTHR45620:SF22; PTHR45620:SF22; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR00491; VASOACTVEIPR.
DR PRINTS; PR01155; VIP2RECEPTOR.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..438
FT /note="Vasoactive intestinal polypeptide receptor 2"
FT /id="PRO_0000012860"
FT TOPO_DOM 24..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..151
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..178
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..227
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..262
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..303
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..348
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..380
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..61
FT /evidence="ECO:0000269|Ref.12"
FT DISULFID 52..93
FT /evidence="ECO:0000269|Ref.12"
FT DISULFID 75..109
FT /evidence="ECO:0000269|Ref.12"
FT DISULFID 202..271
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..103
FT /note="MRTLLPPALLTCWLLAPVNSIHPECRFHLEIQEEETKCAELLRSQTEKHKAC
FT SGVWDNITCWRPANVGETVTVPCPKVFSNFYSKAGNISKNCTSDGWSETFP -> MPLW
FT EAPSDHPANPPATLQGHTSLPGCQEEPARDPQSGLPQITSESSSFSEGSLPSWSSGPAG
FT AKLNASHEGIGSSSDGNGDSKAATERVVSAMDTVRRKHPE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056684"
FT VAR_SEQ 104..119
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056685"
FT VARIANT 39
FT /note="A -> T (in dbSNP:rs1062609)"
FT /id="VAR_011811"
FT VARIANT 412
FT /note="R -> H (in dbSNP:rs1042620)"
FT /id="VAR_011812"
FT CONFLICT 424
FT /note="G -> A (in Ref. 1; AAC37569/AAC41756 and 3;
FT AAC50872)"
FT /evidence="ECO:0000305"
FT HELIX 26..44
FT /evidence="ECO:0007829|PDB:2X57"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2X57"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2X57"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2X57"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2X57"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:2X57"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2X57"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:2X57"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:2X57"
SQ SEQUENCE 438 AA; 49479 MW; 265A43A70BE09699 CRC64;
MRTLLPPALL TCWLLAPVNS IHPECRFHLE IQEEETKCAE LLRSQTEKHK ACSGVWDNIT
CWRPANVGET VTVPCPKVFS NFYSKAGNIS KNCTSDGWSE TFPDFVDACG YSDPEDESKI
TFYILVKAIY TLGYSVSLMS LATGSIILCL FRKLHCTRNY IHLNLFLSFI LRAISVLVKD
DVLYSSSGTL HCPDQPSSWV GCKLSLVFLQ YCIMANFFWL LVEGLYLHTL LVAMLPPRRC
FLAYLLIGWG LPTVCIGAWT AARLYLEDTG CWDTNDHSVP WWVIRIPILI SIIVNFVLFI
SIIRILLQKL TSPDVGGNDQ SQYKRLAKST LLLIPLFGVH YMVFAVFPIS ISSKYQILFE
LCLGSFQGLV VAVLYCFLNS EVQCELKRKW RSRCPTPSAS RDYRVCGSSF SRNGSEGALQ
FHRGSRAQSF LQTETSVI
