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 02-SEP-2026, entry version 215. 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; DOI=10.1182/blood.v86.4.1348.bloodjournal8641348; 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 EBS7, 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 FUNCTION. RX PubMed=17045834; DOI=10.1016/j.biocel.2006.09.001; RA Zheng Z.Z., Liu Z.X.; RT "Activation of the phosphatidylinositol 3-kinase/protein kinase Akt pathway RT mediates CD151-induced endothelial cell proliferation and cell migration."; RL Int. J. Biochem. Cell Biol. 39:340-348(2007). RN [15] RP UBIQUITINATION BY RNF128, AND MUTAGENESIS OF LYS-7; LYS-8 AND LYS-17. RX PubMed=18713730; DOI=10.1074/jbc.m805092200; RA Lineberry N., Su L., Soares L., Fathman C.G.; RT "The single subunit transmembrane E3 ligase gene related to anergy in RT lymphocytes (GRAIL) captures and then ubiquitinates transmembrane proteins RT across the cell membrane."; RL J. Biol. Chem. 283:28497-28505(2008). RN [16] RP FUNCTION, MUTAGENESIS OF ASN-159, AND INTERACTION WITH INTEGRIN ITGA3. RX PubMed=18852263; DOI=10.1074/jbc.m806394200; RA Baldwin G., Novitskaya V., Sadej R., Pochec E., Litynska A., Hartmann C., RA Williams J., Ashman L., Eble J.A., Berditchevski F.; RT "Tetraspanin CD151 regulates glycosylation of (alpha)3(beta)1 integrin."; RL J. Biol. Chem. 283:35445-35454(2008). RN [17] 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 [18] 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 [19] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAC1 AND CDC42. RX PubMed=22843693; DOI=10.1074/jbc.m111.314443; RA Hong I.K., Jeoung D.I., Ha K.S., Kim Y.M., Lee H.; RT "Tetraspanin CD151 stimulates adhesion-dependent activation of Ras, Rac, RT and Cdc42 by facilitating molecular association between beta1 integrins and RT small GTPases."; RL J. Biol. Chem. 287:32027-32039(2012). RN [20] 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 [21] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24723389; DOI=10.1002/eji.201344235; RA Rocha-Perugini V., Gonzalez-Granado J.M., Tejera E., Lopez-Martin S., RA Yanez-Mo M., Sanchez-Madrid F.; RT "Tetraspanins CD9 and CD151 at the immune synapse support T-cell integrin RT signaling."; RL Eur. J. Immunol. 44:1967-1975(2014). RN [22] 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 [23] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=27147745; DOI=10.1128/jvi.00145-16; RA Hochdorfer D., Florin L., Sinzger C., Lieber D.; RT "Tetraspanin CD151 Promotes Initial Events in Human Cytomegalovirus RT Infection."; RL J. Virol. 90:6430-6442(2016). RN [24] 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). RN [25] RP FUNCTION, AND INTERACTION WITH INTEGRINS ITGA3:ITGB1 AND ITGA6:ITGB4. RX PubMed=31488507; DOI=10.1242/jcs.235366; RA Te Molder L., Juksar J., Harkes R., Wang W., Kreft M., Sonnenberg A.; RT "Tetraspanin CD151 and integrin alpha3beta1 contribute to the stabilization RT of integrin alpha6beta4-containing cell-matrix adhesions."; RL J. Cell Sci. 132:0-0(2019). RN [26] RP TISSUE SPECIFICITY, AND INDUCTION BY TCR ACTIVATION. RX PubMed=32978478; DOI=10.1038/s41598-020-72719-8; RA Perez M.D., Seu L., Lowman K.E., Moylan D.C., Tidwell C., Samuel S., RA Duverger A., Wagner F.H., Carlin E., Sharma V., Pope B., Raman C., RA Erdmann N., Locke J., Hu H., Sabbaj S., Kutsch O.; RT "The tetraspanin CD151 marks a unique population of activated human T RT cells."; RL Sci. Rep. 10:15748-15748(2020). RN [27] RP FUNCTION, AND INTERACTION WITH F11R. RX PubMed=35067832; DOI=10.1007/s00018-022-04140-5; RA Thoelmann S., Seebach J., Otani T., Florin L., Schnittler H., Gerke V., RA Furuse M., Ebnet K.; RT "JAM-A interacts with alpha3beta1 integrin and tetraspanins CD151 and CD9 RT to regulate collective cell migration of polarized epithelial cells."; RL Cell. Mol. Life Sci. 79:88-88(2022). CC -!- FUNCTION: Structural component of specialized membrane microdomains CC known as tetraspanin-enriched microdomains (TERMs), which act as CC platforms for receptor clustering and signaling. Plays a role in CC various cellular and molecular mechanism through its association with CC both integrin and non-integrin proteins. These interactions facilitate CC critical cellular functions, including cell-to-cell communication, CC wound healing, platelet aggregation, trafficking, cell motility, and CC angiogenesis (PubMed:17045834, PubMed:24723389, PubMed:31488507). Via CC interaction with JAM-A/F11R and integrin ITGA3:ITGB1, promotes the CC recruitment of signaling molecules such as RAC1, CDC42 and RhoGTPases CC to facilitate the polarization of epithelial cells and the CC reorganization of the actin cytoskeleton, which are critical steps in CC cell migration process (PubMed:22843693, PubMed:35067832). Regulates CC the glycosylation pattern of ITGA3:ITGB1 thereby modulating its CC activity (PubMed:18852263). Plays an essential role in the maintenance CC of central laminin-binding integrin ITGA6:ITGB4-containing adhesion CC complexes (PubMed:31488507). Essential for the proper assembly of the CC glomerular and tubular basement membranes in kidney (PubMed:15265795). CC Contributes to T-cell activation by modulating integrin signaling CC leading to activation of downstream targets PTK2 and MAPK1/MAPK3 CC (PubMed:24723389). {ECO:0000269|PubMed:15265795, CC ECO:0000269|PubMed:17045834, ECO:0000269|PubMed:18852263, CC ECO:0000269|PubMed:22843693, ECO:0000269|PubMed:24723389, CC ECO:0000269|PubMed:31488507, ECO:0000269|PubMed:35067832}. 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 -!- FUNCTION: (Microbial infection) Plays a role in human cytomegalovirus CC entry into host cell by contributing to entry receptor binding, CC membrane fusion, or release of the capsid. CC {ECO:0000269|PubMed:27147745}. CC -!- SUBUNIT: Interacts with integrins ITGA3:ITGB1, ITGA5:ITGB1, ITGA3:ITGB1 CC and ITGA6:ITGB4 and with CD9 and CD181 (PubMed:11907260, CC PubMed:31488507). Interacts (via the second extracellular domain) with CC integrin ITGAV:ITGB3 (PubMed:27993971). Interacts with ITGA3; this CC interaction modulates ITGA3 glycosylation pattern (PubMed:18852263). CC Interacts with F11R (PubMed:35067832). Interacts with RAC1 and CDC42; CC these interactions mediate physical association of RAC1 and CDC42 with CC integrin adhesion receptor complexes (PubMed:22843693). CC {ECO:0000269|PubMed:11907260, ECO:0000269|PubMed:18852263, CC ECO:0000269|PubMed:22843693, ECO:0000269|PubMed:27993971, CC ECO:0000269|PubMed:31488507, ECO:0000269|PubMed:35067832}. 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=7; IntAct=EBI-10210332, EBI-2550768; CC P48509; P23229: ITGA6; NbExp=5; IntAct=EBI-10210332, EBI-2436548; CC P48509; P16144: ITGB4; NbExp=3; IntAct=EBI-10210332, EBI-948678; 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: Cell membrane {ECO:0000269|PubMed:22843693, CC ECO:0000269|PubMed:24723389}; Multi-pass membrane protein. CC Note=Relocalizes to the immune synapse in T-cells upon activation. CC {ECO:0000269|PubMed:24723389}. 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 (PubMed:15265795). Acts as a sensitive T-cell activation CC marker (PubMed:32978478). {ECO:0000269|PubMed:15265795, CC ECO:0000269|PubMed:32978478}. CC -!- INDUCTION: On both CD4 and CD8 T-cells following TCR/CD3 activation. CC {ECO:0000269|PubMed:32978478}. 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 -!- PTM: Ubiquitinated by RNF128 on lysine residues present in the CC tetraspanin amino terminus via 'Lys-48'-linked ubiquitin leading to CC proteasomal degradation. {ECO:0000269|PubMed:18713730}. 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: Epidermolysis bullosa simplex 7, with nephropathy and deafness CC (EBS7) [MIM:609057]: A form of epidermolysis bullosa, a genodermatosis CC characterized by recurrent blistering, fragility of the skin and CC mucosal epithelia, and erosions caused by minor mechanical trauma. EBS7 CC is an autosomal recessive disorder characterized by the association of CC skin blistering, hereditary nephritis, sensorineural deafness, and CC beta-thalassemia minor. Skin blistering is present at birth, CC particularly in the tibial area but also scattered on other parts of CC the body. {ECO:0000269|PubMed:15265795}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/967/CD151"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001039490.2. DR RefSeq; NP_004348.2; NM_004357.5. DR RefSeq; NP_620598.1; NM_139029.2. DR RefSeq; NP_620599.1; NM_139030.4. DR RefSeq; XP_024304548.1; XM_024448780.2. DR RefSeq; XP_054226609.1; XM_054370634.1. DR AlphaFoldDB; P48509; -. DR SMR; P48509; -. DR BioGRID; 107415; 77. DR CORUM; P48509; -. DR FunCoup; P48509; 248. DR IntAct; P48509; 52. DR MINT; P48509; -. DR NDEx; IQUERY-CP-CD151; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000324101; -. DR TCDB; 8.A.40.1.15; the tetraspanin (tetraspanin) family. DR GlyCosmos; P48509; 1 site, No reported glycans. DR GlyGen; P48509; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; P48509; -. DR PhosphoSitePlus; P48509; -. DR SwissPalm; P48509; -. DR BioMuta; CD151; -. DR DMDM; 85687560; -. DR jPOST; P48509; -. DR MassIVE; P48509; -. DR PaxDb; 9606-ENSP00000324101; -. DR PeptideAtlas; P48509; -. DR ProteomicsDB; 55898; -. DR Pumba; P48509; -. DR ABCD; P48509; 6 sequenced antibodies. DR Antibodypedia; 2778; 704 antibodies from 40 providers. DR DNASU; 977; -. DR Ensembl; ENST00000322008.9; ENSP00000324101.4; ENSG00000177697.20. DR Ensembl; ENST00000397420.9; ENSP00000380565.3; ENSG00000177697.20. DR Ensembl; ENST00000397421.5; ENSP00000380566.1; ENSG00000177697.20. DR Ensembl; ENST00000530726.5; ENSP00000432385.1; ENSG00000177697.20. DR Ensembl; ENST00000890766.1; ENSP00000560825.1; ENSG00000177697.20. DR Ensembl; ENST00000890768.1; ENSP00000560827.1; ENSG00000177697.20. DR Ensembl; ENST00000890769.1; ENSP00000560828.1; ENSG00000177697.20. DR Ensembl; ENST00000890774.1; ENSP00000560833.1; ENSG00000177697.20. DR Ensembl; ENST00000890777.1; ENSP00000560836.1; ENSG00000177697.20. DR Ensembl; ENST00000890778.1; ENSP00000560837.1; ENSG00000177697.20. DR Ensembl; ENST00000890779.1; ENSP00000560838.1; ENSG00000177697.20. DR Ensembl; ENST00000890782.1; ENSP00000560841.1; ENSG00000177697.20. DR Ensembl; ENST00000890783.1; ENSP00000560842.1; ENSG00000177697.20. DR Ensembl; ENST00000890785.1; ENSP00000560844.1; ENSG00000177697.20. DR Ensembl; ENST00000890786.1; ENSP00000560845.1; ENSG00000177697.20. DR Ensembl; ENST00000890787.1; ENSP00000560846.1; ENSG00000177697.20. DR Ensembl; ENST00000919377.1; ENSP00000589436.1; ENSG00000177697.20. DR Ensembl; ENST00000919378.1; ENSP00000589437.1; ENSG00000177697.20. DR Ensembl; ENST00000919383.1; ENSP00000589442.1; ENSG00000177697.20. DR Ensembl; ENST00000946304.1; ENSP00000616363.1; ENSG00000177697.20. DR Ensembl; ENST00000946309.1; ENSP00000616368.1; ENSG00000177697.20. DR Ensembl; ENST00000946310.1; ENSP00000616369.1; ENSG00000177697.20. DR Ensembl; ENST00000946311.1; ENSP00000616370.1; ENSG00000177697.20. 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 AGR; HGNC:1630; -. DR ClinPGx; PA26189; -. DR CTD; 977; -. DR DisGeNET; 977; -. DR GeneCards; CD151; -. DR GeneReviews; CD151; -. DR HGNC; HGNC:1630; CD151. DR HPA; ENSG00000177697; Tissue enhanced (blood). DR MalaCards; CD151; -. DR MIM; 179620; phenotype. DR MIM; 602243; gene. DR MIM; 609057; phenotype. DR OpenTargets; ENSG00000177697; -. DR Orphanet; 300333; Nephrotic syndrome-epidermolysis bullosa-sensorineural deafness syndrome. DR VEuPathDB; HostDB:ENSG00000177697; -. DR eggNOG; KOG3882; Eukaryota. DR GeneTree; ENSGT00940000157760; -. DR HOGENOM; CLU_055524_5_0_1; -. DR InParanoid; P48509; -. DR OMA; DSCCKTR; -. DR OrthoDB; 438211at2759; -. DR PAN-GO; P48509; 2 GO annotations based on evolutionary models. DR PhylomeDB; P48509; -. 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 Agora; ENSG00000177697; -. DR BioGRID-ORCS; 977; 29 hits in 1162 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 187 other cell types or tissues. DR ExpressionAtlas; P48509; baseline and differential. 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:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. 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:0044319; P:wound healing, spreading of cells; IDA:MGI. DR CDD; cd03155; CD151_like_LEL; 1. DR FunFam; 1.10.1450.10:FF:000005; Tetraspanin; 1. DR Gene3D; 1.10.1450.10; Tetraspanin; 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:SF487; CD151 ANTIGEN; 1. DR PANTHER; PTHR19282; TETRASPANIN; 1. DR Pfam; PF00335; Tetraspanin; 1. DR PIRSF; PIRSF002419; Tetraspanin; 1. DR PRINTS; PR00259; TMFOUR. DR SUPFAM; SSF48652; Tetraspanin; 1. DR PROSITE; PS00421; TM4_1; 1. PE 1: Evidence at protein level; KW Blood group antigen; Cell membrane; Deafness; Epidermolysis bullosa; KW Glycoprotein; Host-virus interaction; Lipoprotein; Membrane; Palmitate; KW Proteomics identification; Reference proteome; Transmembrane; KW Transmembrane helix; Ubl conjugation. 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" FT MUTAGEN 7 FT /note="K->R: Complete loss of RNF128-mediated FT ubiquitination; when associated with R-8 and R-17." FT /evidence="ECO:0000269|PubMed:18713730" FT MUTAGEN 8 FT /note="K->R: Complete loss of RNF128-mediated FT ubiquitination; when associated with R-7 and R-17." FT /evidence="ECO:0000269|PubMed:18713730" FT MUTAGEN 17 FT /note="K->R: Complete loss of RNF128-mediated FT ubiquitination; when associated with R-7 and R-8." FT /evidence="ECO:0000269|PubMed:18713730" FT MUTAGEN 159 FT /note="N->Q: Unable to modulate the glycosylation pattern FT of integrin ITGA3 subunit." FT /evidence="ECO:0000269|PubMed:18852263" 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 //