ID   CD151_BOVIN             Reviewed;         253 AA.
AC   Q3ZBH3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=CD151 antigen;
DE   AltName: CD_antigen=CD151;
GN   Name=CD151;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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; BC103294; AAI03295.1; -; mRNA.
DR   RefSeq; NP_001030424.1; NM_001035347.1.
DR   RefSeq; XP_005227410.1; XM_005227353.1.
DR   RefSeq; XP_005227411.1; XM_005227354.2.
DR   RefSeq; XP_005227412.1; XM_005227355.3.
DR   RefSeq; XP_005227413.1; XM_005227356.2.
DR   RefSeq; XP_005227414.1; XM_005227357.3.
DR   RefSeq; XP_005227415.1; XM_005227358.2.
DR   RefSeq; XP_005227416.1; XM_005227359.3.
DR   RefSeq; XP_010819544.1; XM_010821242.1.
DR   AlphaFoldDB; Q3ZBH3; -.
DR   SMR; Q3ZBH3; -.
DR   STRING; 9913.ENSBTAP00000051660; -.
DR   PaxDb; Q3ZBH3; -.
DR   PRIDE; Q3ZBH3; -.
DR   GeneID; 523328; -.
DR   KEGG; bta:523328; -.
DR   CTD; 977; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   HOGENOM; CLU_055524_5_0_1; -.
DR   InParanoid; Q3ZBH3; -.
DR   Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
DR   Gene3D; 1.10.1450.10; -; 1.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR000301; Tetraspanin_animals.
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.
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_0000284961"
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;  27987 MW;  A5AD08CF3DB2A308 CRC64;
     MGEFGEKSTT CGTVCLKYLL FTFNCCFWLA GLAVMAVGIW TLALKSDYIS LLASGTYLAT
     AYILVVAGIV VMVTGALGCC ATFKERRNLL RLYFGLLLII FLLEIIAGAL AYIYYQQLNA
     ELKENLKDTM TRRYHQPGHE GVTSAVDKLQ QEFHCCGSNN SRDWQDSEWI HSGEAGGRVV
     PDSCCKTVVP GCGRRDHASN IYKVEGGCIT KLETFIQEHL RIIGAVGLGI ACVQVFGMLF
     TCCLYKSLKL EHY