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   27-MAR-2024, entry version 172.
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   GlyCosmos; P13379; 4 sites, No reported glycans.
DR   GlyGen; P13379; 4 sites.
DR   iPTMnet; P13379; -.
DR   PhosphoSitePlus; P13379; -.
DR   SwissPalm; P13379; -.
DR   EPD; P13379; -.
DR   jPOST; P13379; -.
DR   PaxDb; 10090-ENSMUSP00000025571; -.
DR   PeptideAtlas; P13379; -.
DR   ProteomicsDB; 283749; -.
DR   Antibodypedia; 4206; 4420 antibodies from 55 providers.
DR   DNASU; 12507; -.
DR   Ensembl; ENSMUST00000025571.9; ENSMUSP00000025571.8; ENSMUSG00000024669.9.
DR   GeneID; 12507; -.
DR   KEGG; mmu:12507; -.
DR   UCSC; uc008gqv.1; mouse.
DR   AGR; MGI:88340; -.
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; VCSGFQP; -.
DR   OrthoDB; 5322862at2759; -.
DR   PhylomeDB; P13379; -.
DR   TreeFam; TF329295; -.
DR   BioGRID-ORCS; 12507; 2 hits in 78 CRISPR screens.
DR   PRO; PR:P13379; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P13379; Protein.
DR   Bgee; ENSMUSG00000024669; Expressed in thymus and 49 other cell types or tissues.
DR   ExpressionAtlas; P13379; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; SRCR-like domain; 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; T-CELL SURFACE GLYCOPROTEIN CD5; 1.
DR   PANTHER; PTHR47309:SF1; T-CELL SURFACE GLYCOPROTEIN CD5; 1.
DR   Pfam; PF00530; SRCR; 1.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   PRINTS; PR01409; TCELLCD5.
DR   SMART; SM00202; SR; 2.
DR   SUPFAM; SSF56487; SRCR-like; 2.
DR   PROSITE; PS50287; SRCR_2; 3.
DR   Genevisible; P13379; MM.
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
//