CD151_MOUSE
ID CD151_MOUSE Reviewed; 253 AA.
AC O35566; O89118;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 158.
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: CD_antigen=CD151;
GN Name=Cd151; Synonyms=Peta3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9294006; DOI=10.1016/s0167-4781(97)00095-x;
RA Hasegawa H., Watanabe H., Nomura T., Utsunomiya Y., Yanagisawa K.,
RA Fujita S.;
RT "Molecular cloning and expression of mouse homologue of SFA-1/PETA-3
RT (CD151), a member of the transmembrane 4 superfamily.";
RL Biochim. Biophys. Acta 1353:125-130(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv;
RX PubMed=9602068; DOI=10.1016/s0167-4781(98)00034-7;
RA Fitter S., Seldin M.F., Ashman L.K.;
RT "Characterisation of the mouse homologue of CD151 (PETA-3/SFA-1); genomic
RT structure, chromosomal localisation and identification of 2 novel splice
RT forms.";
RL Biochim. Biophys. Acta 1398:75-85(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Essential for the proper assembly of the glomerular and
CC tubular basement membranes in kidney. {ECO:0000250|UniProtKB:P48509}.
CC -!- SUBUNIT: Interacts with integrins ITGA3:ITGB1, ITGA5:ITGB1, ITGA3:ITGB1
CC and ITGA6:ITGB4 and with CD9 and CD181. Interacts (via the second
CC extracellular domain) with integrin ITGAV:ITGB3.
CC {ECO:0000250|UniProtKB:P48509}.
CC -!- INTERACTION:
CC O35566; Q62470: Itga3; NbExp=2; IntAct=EBI-8369654, EBI-8398907;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- PTM: Palmitoylated. Palmitoylation by ZDHHC2 regulates CD151
CC expression, association with other tetraspanin family proteins and
CC function in cell adhesion. {ECO:0000250|UniProtKB:P48509}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR EMBL; D89290; BAA22447.1; -; mRNA.
DR EMBL; AF033620; AAC25952.1; -; Genomic_DNA.
DR EMBL; U89772; AAC25976.1; -; mRNA.
DR CCDS; CCDS22017.1; -.
DR RefSeq; NP_001104519.1; NM_001111049.1.
DR RefSeq; NP_001104520.1; NM_001111050.1.
DR RefSeq; NP_033972.2; NM_009842.3.
DR AlphaFoldDB; O35566; -.
DR SMR; O35566; -.
DR BioGRID; 198574; 1.
DR IntAct; O35566; 2.
DR STRING; 10090.ENSMUSP00000101622; -.
DR GlyGen; O35566; 1 site.
DR iPTMnet; O35566; -.
DR PhosphoSitePlus; O35566; -.
DR SwissPalm; O35566; -.
DR MaxQB; O35566; -.
DR PaxDb; O35566; -.
DR PeptideAtlas; O35566; -.
DR PRIDE; O35566; -.
DR ProteomicsDB; 281259; -.
DR Antibodypedia; 2778; 651 antibodies from 38 providers.
DR DNASU; 12476; -.
DR Ensembl; ENSMUST00000058746; ENSMUSP00000061636; ENSMUSG00000025510.
DR Ensembl; ENSMUST00000106000; ENSMUSP00000101622; ENSMUSG00000025510.
DR Ensembl; ENSMUST00000177840; ENSMUSP00000136331; ENSMUSG00000025510.
DR GeneID; 12476; -.
DR KEGG; mmu:12476; -.
DR UCSC; uc009kll.2; mouse.
DR CTD; 977; -.
DR MGI; MGI:1096360; Cd151.
DR VEuPathDB; HostDB:ENSMUSG00000025510; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157760; -.
DR HOGENOM; CLU_055524_5_0_1; -.
DR InParanoid; O35566; -.
DR OMA; WADSLWI; -.
DR OrthoDB; 1051357at2759; -.
DR PhylomeDB; O35566; -.
DR TreeFam; TF352892; -.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR BioGRID-ORCS; 12476; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Cd151; mouse.
DR PRO; PR:O35566; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35566; protein.
DR Bgee; ENSMUSG00000025510; Expressed in endothelial cell of lymphatic vessel and 256 other tissues.
DR ExpressionAtlas; O35566; baseline and differential.
DR Genevisible; O35566; MM.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISO: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 Glycoprotein; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..253
FT /note="CD151 antigen"
FT /id="PRO_0000219232"
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:0000250|UniProtKB:P48509"
FT LIPID 15
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P48509"
FT LIPID 242
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P48509"
FT LIPID 243
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P48509"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 237
FT /note="G -> S (in Ref. 1; BAA22447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 28246 MW; AEBEEBCE2D765F1B CRC64;
MGEFNEKKAT CGTVCLKYLL FTYNCCFWLA GLAVMAVGIW TLALKSDYIS LLASSTYLAT
AYILVVAGVV VMVTGVLGCC ATFKERRNLL RLYFILLLII FLLEIIAGIL AYVYYQQLNT
ELKENLKDTM VKRYHQSGHE GVSSAVDKLQ QEFHCCGSNN SQDWQDSEWI RSGEADSRVV
PDSCCKTMVA GCGKRDHASN IYKVEGGCIT KLETFIQEHL RVIGAVGIGI ACVQVFGMIF
TCCLYRSLKL EHY
