ID   CD151_MACMU             Reviewed;         253 AA.
AC   P61171; Q9MYM2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=CD151 antigen;
DE   AltName: Full=Platelet-endothelial tetraspan antigen 3;
DE            Short=PETA-3;
DE   AltName: CD_antigen=CD151;
GN   Name=CD151;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shanmukhappa K., Kapil S.;
RT   "CD151/PETA-3, a tetraspanin molecule, interacts with the 3' untranslated
RT   region and partial nucleoprotein gene of porcine reproductive and
RT   respiratory syndrome virus RNA.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; AF275665; AAF90151.1; -; mRNA.
DR   RefSeq; NP_001027994.1; NM_001032822.1.
DR   AlphaFoldDB; P61171; -.
DR   SMR; P61171; -.
DR   STRING; 9544.ENSMMUP00000027151; -.
DR   PRIDE; P61171; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   InParanoid; P61171; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..253
FT                   /note="CD151 antigen"
FT                   /id="PRO_0000219231"
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"
SQ   SEQUENCE   253 AA;  28438 MW;  CAD2780B63F644A4 CRC64;
     MGEFNEKKTT CGTVCLKYLL FTYNCCFWLA GLAVMAVGIW TLALKSDYIS LLASGTYLAT
     AYILVVAGAV VMVTGVLGCC ATFKERRNLL RLYFILLLII FLLEIIAGVL AYVYYQQLNT
     ELKENLKDTM AKRYHQPGHE AVTSAVDQLQ QEFHCCGSNN SQDWRDSEWI RLREARGRVV
     PDSCCKTVVA GCGQRDHAFN IYKVEGGFIT KLETFIQEHL RVIGAVGTGI ACVQVFGMIF
     TCCLYRSLKL EHY