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CD151_HUMAN
ID   CD151_HUMAN             Reviewed;         253 AA.
AC   P48509; A8KAK8; E9PI15; Q14826; Q86U54; Q96TE3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 3.
DT   03-AUG-2022, entry version 196.
DE   RecName: Full=CD151 antigen;
DE   AltName: Full=GP27;
DE   AltName: Full=Membrane glycoprotein SFA-1;
DE   AltName: Full=Platelet-endothelial tetraspan antigen 3;
DE            Short=PETA-3;
DE   AltName: Full=Tetraspanin-24;
DE            Short=Tspan-24;
DE   AltName: CD_antigen=CD151;
GN   Name=CD151; Synonyms=TSPAN24;
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 [MRNA].
RC   TISSUE=Platelet;
RX   PubMed=7632941;
RA   Fitter S., Tetaz T.J., Berndt M.C., Ashman L.K.;
RT   "Molecular cloning of cDNA encoding a novel platelet-endothelial cell
RT   tetra-span antigen, PETA-3.";
RL   Blood 86:1348-1355(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-132 AND SER-137.
RX   PubMed=8627808; DOI=10.1128/jvi.70.5.3258-3263.1996;
RA   Hasegawa H., Utsunomiya Y., Kishimoto K., Yanagisawa K., Fujita S.;
RT   "SFA-1, a novel cellular gene induced by human T-cell leukemia virus type
RT   1, is a member of the transmembrane 4 superfamily.";
RL   J. Virol. 70:3258-3263(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-132 AND SER-137.
RX   PubMed=11181065; DOI=10.1006/bbrc.2001.4384;
RA   Whittock N.V., McLean W.H.I.;
RT   "Genomic organization, amplification, fine mapping, and intragenic
RT   polymorphisms of the human hemidesmosomal tetraspanin CD151 gene.";
RL   Biochem. Biophys. Res. Commun. 281:425-430(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-120.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [10]
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   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, and Kidney;
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   [12]
RP   PALMITOYLATION AT CYS-11; CYS-15; CYS-242 AND CYS-243, AND INTERACTION WITH
RP   CD9; CD181 AND INTEGRINS ITGA3:ITGB1; ITGA5:ITGB1; ITGA3:ITGB1 AND
RP   ITGA6:ITGB4.
RX   PubMed=11907260; DOI=10.1091/mbc.01-05-0275;
RA   Yang X., Claas C., Kraeft S.K., Chen L.B., Wang Z., Kreidberg J.A.,
RA   Hemler M.E.;
RT   "Palmitoylation of tetraspanin proteins: modulation of CD151 lateral
RT   interactions, subcellular distribution, and integrin-dependent cell
RT   morphology.";
RL   Mol. Biol. Cell 13:767-781(2002).
RN   [13]
RP   FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN RAPH BLOOD GROUP SYSTEM,
RP   INVOLVEMENT IN NPEBD, AND VARIANT HIS-178.
RX   PubMed=15265795; DOI=10.1182/blood-2004-04-1512;
RA   Karamatic Crew V., Burton N., Kagan A., Green C.A., Levene C., Flinter F.,
RA   Brady R.L., Daniels G., Anstee D.J.;
RT   "CD151, the first member of the tetraspanin (TM4) superfamily detected on
RT   erythrocytes, is essential for the correct assembly of human basement
RT   membranes in kidney and skin.";
RL   Blood 104:2217-2223(2004).
RN   [14]
RP   PALMITOYLATION.
RX   PubMed=18508921; DOI=10.1091/mbc.e07-11-1164;
RA   Sharma C., Yang X.H., Hemler M.E.;
RT   "DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9
RT   and CD151.";
RL   Mol. Biol. Cell 19:3415-3425(2008).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   FUNCTION (MICROBIAL INFECTION).
RX   PubMed=24553111; DOI=10.3390/v6020893;
RA   Scheffer K.D., Berditchevski F., Florin L.;
RT   "The tetraspanin CD151 in papillomavirus infection.";
RL   Viruses 6:893-908(2014).
RN   [18]
RP   INTERACTION WITH INTEGRIN ITGAV:ITGB3.
RX   PubMed=27993971; DOI=10.1042/bcj20160998;
RA   Yu J., Lee C.Y., Changou C.A., Cedano-Prieto D.M., Takada Y.K., Takada Y.;
RT   "The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding
RT   site of integrin alphavbeta3.";
RL   Biochem. J. 474:589-596(2017).
CC   -!- FUNCTION: Essential for the proper assembly of the glomerular and
CC       tubular basement membranes in kidney. {ECO:0000269|PubMed:15265795}.
CC   -!- FUNCTION: (Microbial infection) Plays a role in human papillomavirus
CC       16/HPV-16 endocytosis upon binding to cell surface receptor.
CC       {ECO:0000269|PubMed:24553111}.
CC   -!- SUBUNIT: Interacts with integrins ITGA3:ITGB1, ITGA5:ITGB1, ITGA3:ITGB1
CC       and ITGA6:ITGB4 and with CD9 and CD181 (PubMed:11907260). Interacts
CC       (via the second extracellular domain) with integrin ITGAV:ITGB3
CC       (PubMed:27993971). {ECO:0000269|PubMed:11907260,
CC       ECO:0000269|PubMed:27993971}.
CC   -!- INTERACTION:
CC       P48509; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-10210332, EBI-11343438;
CC       P48509; Q8IYS0: GRAMD1C; NbExp=11; IntAct=EBI-10210332, EBI-7054335;
CC       P48509; P26006: ITGA3; NbExp=6; IntAct=EBI-10210332, EBI-2550768;
CC       P48509; P26715: KLRC1; NbExp=3; IntAct=EBI-10210332, EBI-9018187;
CC       P48509; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-10210332, EBI-7238458;
CC       P48509; Q8WUV1: TSPAN18; NbExp=3; IntAct=EBI-10210332, EBI-17670824;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in a variety of tissues including
CC       vascular endothelium and epidermis. Expressed on erythroid cells, with
CC       a higher level of expression in erythroid precursors than on mature
CC       erythrocytes. {ECO:0000269|PubMed:15265795}.
CC   -!- INDUCTION: By HTLV-1.
CC   -!- PTM: Palmitoylated. Palmitoylation by ZDHHC2 regulates CD151
CC       expression, association with other tetraspanin family proteins and
CC       function in cell adhesion. {ECO:0000269|PubMed:18508921}.
CC   -!- POLYMORPHISM: CD151 defines the MER2=RAPH1 antigen of the RAPH blood
CC       group system. 92% of Caucasians are MER2-positive and 8% are apparently
CC       MER2-negative. {ECO:0000269|PubMed:15265795}.
CC   -!- DISEASE: Nephropathy with pretibial epidermolysis bullosa and deafness
CC       (NPEBD) [MIM:609057]: A disorder characterized by the association of
CC       hereditary nephritis, epidermolysis bullosa, deafness, and beta-
CC       thalassemia minor. {ECO:0000269|PubMed:15265795}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC       database;
CC       URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=raph";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/cd151/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CD151ID967ch11p15.html";
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DR   EMBL; U14650; AAA87064.1; -; mRNA.
DR   EMBL; D29963; BAA06229.1; -; mRNA.
DR   EMBL; AF315942; AAK14179.1; -; Genomic_DNA.
DR   EMBL; BT007397; AAP36061.1; -; mRNA.
DR   EMBL; BT020132; AAV38934.1; -; mRNA.
DR   EMBL; CR456826; CAG33107.1; -; mRNA.
DR   EMBL; CR542098; CAG46895.1; -; mRNA.
DR   EMBL; AK293073; BAF85762.1; -; mRNA.
DR   EMBL; DQ074789; AAY68211.1; -; Genomic_DNA.
DR   EMBL; AP006621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP006623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471158; EAX02400.1; -; Genomic_DNA.
DR   EMBL; BC001374; AAH01374.1; -; mRNA.
DR   EMBL; BC013302; AAH13302.1; -; mRNA.
DR   CCDS; CCDS7719.1; -.
DR   RefSeq; NP_001034579.1; NM_001039490.1.
DR   RefSeq; NP_004348.2; NM_004357.4.
DR   RefSeq; NP_620598.1; NM_139029.1.
DR   RefSeq; NP_620599.1; NM_139030.3.
DR   AlphaFoldDB; P48509; -.
DR   SMR; P48509; -.
DR   BioGRID; 107415; 59.
DR   CORUM; P48509; -.
DR   IntAct; P48509; 21.
DR   MINT; P48509; -.
DR   STRING; 9606.ENSP00000380565; -.
DR   TCDB; 8.A.40.1.15; the tetraspanin (tetraspanin) family.
DR   GlyGen; P48509; 2 sites.
DR   iPTMnet; P48509; -.
DR   PhosphoSitePlus; P48509; -.
DR   SwissPalm; P48509; -.
DR   BioMuta; CD151; -.
DR   DMDM; 85687560; -.
DR   EPD; P48509; -.
DR   jPOST; P48509; -.
DR   MassIVE; P48509; -.
DR   MaxQB; P48509; -.
DR   PaxDb; P48509; -.
DR   PeptideAtlas; P48509; -.
DR   PRIDE; P48509; -.
DR   ProteomicsDB; 55898; -.
DR   ABCD; P48509; 6 sequenced antibodies.
DR   Antibodypedia; 2778; 651 antibodies from 38 providers.
DR   DNASU; 977; -.
DR   Ensembl; ENST00000322008.9; ENSP00000324101.4; ENSG00000177697.19.
DR   Ensembl; ENST00000397420.9; ENSP00000380565.3; ENSG00000177697.19.
DR   Ensembl; ENST00000397421.5; ENSP00000380566.1; ENSG00000177697.19.
DR   Ensembl; ENST00000530726.5; ENSP00000432385.1; ENSG00000177697.19.
DR   GeneID; 977; -.
DR   KEGG; hsa:977; -.
DR   MANE-Select; ENST00000397420.9; ENSP00000380565.3; NM_004357.5; NP_004348.2.
DR   UCSC; uc001lry.4; human.
DR   CTD; 977; -.
DR   DisGeNET; 977; -.
DR   GeneCards; CD151; -.
DR   HGNC; HGNC:1630; CD151.
DR   HPA; ENSG00000177697; Low tissue specificity.
DR   MalaCards; CD151; -.
DR   MIM; 179620; phenotype.
DR   MIM; 602243; gene.
DR   MIM; 609057; phenotype.
DR   neXtProt; NX_P48509; -.
DR   OpenTargets; ENSG00000177697; -.
DR   Orphanet; 300333; Nephrotic syndrome-epidermolysis bullosa-sensorineural deafness syndrome.
DR   PharmGKB; PA26189; -.
DR   VEuPathDB; HostDB:ENSG00000177697; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   GeneTree; ENSGT00940000157760; -.
DR   HOGENOM; CLU_055524_5_0_1; -.
DR   InParanoid; P48509; -.
DR   OMA; WADSLWI; -.
DR   OrthoDB; 1051357at2759; -.
DR   PhylomeDB; P48509; -.
DR   TreeFam; TF352892; -.
DR   PathwayCommons; P48509; -.
DR   Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-HSA-446107; Type I hemidesmosome assembly.
DR   SignaLink; P48509; -.
DR   SIGNOR; P48509; -.
DR   BioGRID-ORCS; 977; 27 hits in 1081 CRISPR screens.
DR   ChiTaRS; CD151; human.
DR   GeneWiki; CD151; -.
DR   GenomeRNAi; 977; -.
DR   Pharos; P48509; Tbio.
DR   PRO; PR:P48509; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P48509; protein.
DR   Bgee; ENSG00000177697; Expressed in descending thoracic aorta and 185 other tissues.
DR   ExpressionAtlas; P48509; baseline and differential.
DR   Genevisible; P48509; HS.
DR   GO; GO:0005604; C:basement membrane; IDA:CACAO.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:MGI.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IDA:MGI.
DR   GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR   GO; GO:0044319; P:wound healing, spreading of cells; IDA:MGI.
DR   Gene3D; 1.10.1450.10; -; 1.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR000301; Tetraspanin_animals.
DR   InterPro; IPR018503; Tetraspanin_CS.
DR   InterPro; IPR008952; Tetraspanin_EC2_sf.
DR   PANTHER; PTHR19282; PTHR19282; 1.
DR   Pfam; PF00335; Tetraspanin; 1.
DR   PIRSF; PIRSF002419; Tetraspanin; 1.
DR   SUPFAM; SSF48652; SSF48652; 1.
DR   PROSITE; PS00421; TM4_1; 1.
PE   1: Evidence at protein level;
KW   Blood group antigen; Deafness; Epidermolysis bullosa; Glycoprotein;
KW   Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..253
FT                   /note="CD151 antigen"
FT                   /id="PRO_0000219230"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..57
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..221
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..253
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           11
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:11907260"
FT   LIPID           15
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:11907260"
FT   LIPID           242
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:11907260"
FT   LIPID           243
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:11907260"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         120
FT                   /note="T -> M (in dbSNP:rs34215390)"
FT                   /evidence="ECO:0000269|Ref.8"
FT                   /id="VAR_025098"
FT   VARIANT         132
FT                   /note="K -> R"
FT                   /evidence="ECO:0000269|PubMed:11181065,
FT                   ECO:0000269|PubMed:8627808"
FT                   /id="VAR_012490"
FT   VARIANT         137
FT                   /note="P -> S (in dbSNP:rs1431926999)"
FT                   /evidence="ECO:0000269|PubMed:11181065,
FT                   ECO:0000269|PubMed:8627808"
FT                   /id="VAR_012491"
FT   VARIANT         178
FT                   /note="R -> H (in dbSNP:rs779114765)"
FT                   /evidence="ECO:0000269|PubMed:15265795"
FT                   /id="VAR_021153"
SQ   SEQUENCE   253 AA;  28295 MW;  0C8FE4CF2C3C286D CRC64;
     MGEFNEKKTT CGTVCLKYLL FTYNCCFWLA GLAVMAVGIW TLALKSDYIS LLASGTYLAT
     AYILVVAGTV VMVTGVLGCC ATFKERRNLL RLYFILLLII FLLEIIAGIL AYAYYQQLNT
     ELKENLKDTM TKRYHQPGHE AVTSAVDQLQ QEFHCCGSNN SQDWRDSEWI RSQEAGGRVV
     PDSCCKTVVA LCGQRDHASN IYKVEGGCIT KLETFIQEHL RVIGAVGIGI ACVQVFGMIF
     TCCLYRSLKL EHY
 
 
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