CD5_MOUSE
ID CD5_MOUSE Reviewed; 494 AA.
AC P13379;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=T-cell surface glycoprotein CD5;
DE AltName: Full=Lymphocyte antigen 1;
DE Short=Ly-1;
DE Short=Lyt-1;
DE AltName: CD_antigen=CD5;
DE Flags: Precursor;
GN Name=Cd5; Synonyms=Ly-1;
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].
RC TISSUE=T-cell;
RX PubMed=3025855; DOI=10.1073/pnas.84.1.204;
RA Huang H.-J.S., Jones N.H., Strominger J.L., Herzenberg L.A.;
RT "Molecular cloning of Ly-1, a membrane glycoprotein of mouse T lymphocytes
RT and a subset of B cells: molecular homology to its human counterpart Leu-
RT 1/T1 (CD5).";
RL Proc. Natl. Acad. Sci. U.S.A. 84:204-208(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC STRAIN=NIH Swiss;
RX PubMed=7536775;
RA Weichert T.R., Schwartz R.C.;
RT "Cloning of the murine CD5 promoter and its tissue-specific regulation.";
RL J. Immunol. 154:4603-4612(1995).
RN [3]
RP PHOSPHORYLATION BY LYN, AND INTERACTION WITH PTPN6/SHP-1.
RX PubMed=11007759; DOI=10.1093/intimm/12.10.1417;
RA Ochi H., Watanabe T.;
RT "Negative regulation of B cell receptor-mediated signaling in B-1 cells
RT through CD5 and Ly49 co-receptors via Lyn kinase activity.";
RL Int. Immunol. 12:1417-1423(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND SER-484, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: May act as a receptor in regulating T-cell proliferation.
CC -!- SUBUNIT: Interacts with CD72/LYB-2. Interacts with PTPN6/SHP-1.
CC {ECO:0000269|PubMed:11007759}.
CC -!- INTERACTION:
CC P13379; P22682: Cbl; NbExp=5; IntAct=EBI-12600513, EBI-640919;
CC P13379; Q3TTA7: Cblb; NbExp=4; IntAct=EBI-12600513, EBI-3649276;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- PTM: Phosphorylated on tyrosine residues by LYN; this creates binding
CC sites for PTPN6/SHP-1. {ECO:0000269|PubMed:11007759}.
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DR EMBL; M15177; AAA39453.1; -; mRNA.
DR EMBL; U09204; AAC52187.1; -; Genomic_DNA.
DR CCDS; CCDS29586.1; -.
DR PIR; A29079; A29079.
DR RefSeq; NP_031676.3; NM_007650.3.
DR AlphaFoldDB; P13379; -.
DR SMR; P13379; -.
DR IntAct; P13379; 5.
DR STRING; 10090.ENSMUSP00000025571; -.
DR GlyGen; P13379; 4 sites.
DR iPTMnet; P13379; -.
DR PhosphoSitePlus; P13379; -.
DR SwissPalm; P13379; -.
DR EPD; P13379; -.
DR jPOST; P13379; -.
DR PaxDb; P13379; -.
DR PeptideAtlas; P13379; -.
DR PRIDE; P13379; -.
DR ProteomicsDB; 283749; -.
DR Antibodypedia; 4206; 3821 antibodies from 54 providers.
DR DNASU; 12507; -.
DR Ensembl; ENSMUST00000025571; ENSMUSP00000025571; ENSMUSG00000024669.
DR GeneID; 12507; -.
DR KEGG; mmu:12507; -.
DR UCSC; uc008gqv.1; mouse.
DR CTD; 921; -.
DR MGI; MGI:88340; Cd5.
DR VEuPathDB; HostDB:ENSMUSG00000024669; -.
DR eggNOG; ENOG502RYTM; Eukaryota.
DR GeneTree; ENSGT00390000017536; -.
DR HOGENOM; CLU_047656_0_0_1; -.
DR InParanoid; P13379; -.
DR OMA; FHRNHTA; -.
DR OrthoDB; 1017770at2759; -.
DR PhylomeDB; P13379; -.
DR TreeFam; TF329295; -.
DR BioGRID-ORCS; 12507; 2 hits in 73 CRISPR screens.
DR PRO; PR:P13379; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P13379; protein.
DR Bgee; ENSMUSG00000024669; Expressed in thymus and 46 other tissues.
DR ExpressionAtlas; P13379; baseline and differential.
DR Genevisible; P13379; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0044214; C:spanning component of plasma membrane; ISO:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0031295; P:T cell costimulation; IDA:MGI.
DR Gene3D; 3.10.250.10; -; 2.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR003566; Tcell_CD5.
DR PANTHER; PTHR47309; PTHR47309; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00258; SPERACTRCPTR.
DR PRINTS; PR01409; TCELLCD5.
DR SMART; SM00202; SR; 2.
DR SUPFAM; SSF56487; SSF56487; 2.
DR PROSITE; PS50287; SRCR_2; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT CHAIN 24..494
FT /note="T-cell surface glycoprotein CD5"
FT /id="PRO_0000033223"
FT TOPO_DOM 25..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..133
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 159..268
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 276..367
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 439..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 452
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 59..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 80..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 106..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 201..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 244..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 285..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 301..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 316..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 341..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 494 AA; 53849 MW; 1EBBBBFE2488C162 CRC64;
MDSHEVLLAA TYLLGTLAAF CLGQSGRGGL DIQVMLSGSN SKCQGQVEIQ MENKWKTVCS
SSWRLSQDHS KNAQQASAVC KQLRCGDPLA LGPFPSLNRP QNQVFCQGSP WSISNCNNTS
SQDQCLPLSL ICLEPQRTTP PPTTTPPTTV PEPTAPPRLQ LVPGHEGLRC TGVVEFYNGS
WGGTILYKAK DRPLGLGNLI CKSLQCGSFL THLSGTEAAG TPAPAELRDP RPLPIRWEAP
NGSCVSLQQC FQKTTAQEGG QALTVICSDF QPKVQSRLVG GSSVCEGIAE VRQRSQWEAL
CDSSAARGRG RWEELCREQQ CGDLISFHTV DADKTSPGFL CAQEKLSQCY HLQKKKHCNK
RVFVTCQDPN PAGLAPGTVA SIILTLVLLV VLLAMCGPLV YKKLVKKFRQ KKQRQWIGPT
GVNQNMSFHR SHTATVRSQV ENPTASHVDN EYSQPPRNSH LSAYPALEGA LHRSSTQPDN
SSDSDYDLQV AQRL
