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CD151_RAT
ID   CD151_RAT               Reviewed;         253 AA.
AC   Q9QZA6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   03-AUG-2022, entry version 141.
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; Synonyms=Peta3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RX   PubMed=11682256; DOI=10.1016/s0893-133x(01)00269-x;
RA   Hua L.V., Green M., Wong A., Warsh J.J., Li P.P.;
RT   "Tetraspan protein CD151: a common target of mood stabilizing drugs?";
RL   Neuropsychopharmacology 25:729-736(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [3]
RP   PROTEIN SEQUENCE OF 9-17 AND 134-148, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
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; AF192547; AAF05763.2; -; mRNA.
DR   EMBL; BC072515; AAH72515.1; -; mRNA.
DR   RefSeq; NP_071968.1; NM_022523.1.
DR   RefSeq; XP_003749065.1; XM_003749017.4.
DR   RefSeq; XP_006230638.1; XM_006230576.3.
DR   RefSeq; XP_006230660.1; XM_006230598.3.
DR   RefSeq; XP_017445147.1; XM_017589658.1.
DR   RefSeq; XP_017445148.1; XM_017589659.1.
DR   RefSeq; XP_017445742.1; XM_017590253.1.
DR   RefSeq; XP_017445743.1; XM_017590254.1.
DR   RefSeq; XP_017459719.1; XM_017604230.1.
DR   RefSeq; XP_017459724.1; XM_017604235.1.
DR   RefSeq; XP_017459725.1; XM_017604236.1.
DR   RefSeq; XP_017459726.1; XM_017604237.1.
DR   AlphaFoldDB; Q9QZA6; -.
DR   SMR; Q9QZA6; -.
DR   STRING; 10116.ENSRNOP00000066223; -.
DR   GlyGen; Q9QZA6; 1 site, 3 N-linked glycans (1 site).
DR   iPTMnet; Q9QZA6; -.
DR   PhosphoSitePlus; Q9QZA6; -.
DR   jPOST; Q9QZA6; -.
DR   PaxDb; Q9QZA6; -.
DR   PRIDE; Q9QZA6; -.
DR   Ensembl; ENSRNOT00000089241; ENSRNOP00000073673; ENSRNOG00000062573.
DR   GeneID; 64315; -.
DR   KEGG; rno:64315; -.
DR   UCSC; RGD:621290; rat.
DR   CTD; 977; -.
DR   RGD; 621290; Cd151.
DR   eggNOG; KOG3882; Eukaryota.
DR   GeneTree; ENSGT00940000157760; -.
DR   HOGENOM; CLU_055524_5_0_1; -.
DR   InParanoid; Q9QZA6; -.
DR   OMA; WADSLWI; -.
DR   OrthoDB; 1051357at2759; -.
DR   PhylomeDB; Q9QZA6; -.
DR   TreeFam; TF352892; -.
DR   Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-RNO-446107; Type I hemidesmosome assembly.
DR   PRO; PR:Q9QZA6; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019215; Expressed in ovary and 19 other tissues.
DR   Genevisible; Q9QZA6; RN.
DR   GO; GO:0005604; C:basement membrane; ISO:RGD.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IPI:RGD.
DR   GO; GO:0016477; P:cell migration; ISO:RGD.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR   GO; GO:0045807; P:positive regulation of endocytosis; ISO:RGD.
DR   GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR   GO; GO:0044319; P:wound healing, spreading of cells; ISO:RGD.
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   Direct protein sequencing; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..253
FT                   /note="CD151 antigen"
FT                   /id="PRO_0000219233"
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;  28355 MW;  51876AF31B4DCB2B CRC64;
     MGEFNEKKAT CGTVCLKYLL FTYNCCFWLA GLAVMAVGIW TLALKSDYIS LLASSTYLAT
     AYILVVAGVV VMVTGVLGCC ATFKERRNLL RLYFILLLII FLLEIIAGIL AYVYYQQLNT
     ELKENLKDTM IKRYHQSGHE GVTNAVDKLQ QEFHCCGSNN SRDWRDSEWI RSGEADSRVV
     PDSCCKTVVT GCGKREHASN IYKVEGGCIT KLESFIQEHL RVIGAVGIGI ACVQVFGMIF
     TCCLYRSLKL EHY
 
 
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