CD5_RAT
ID CD5_RAT Reviewed; 491 AA.
AC P51882; Q63098;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=T-cell surface glycoprotein CD5;
DE AltName: CD_antigen=CD5;
DE Flags: Precursor;
GN Name=Cd5;
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].
RA Murakami T., Matsuura A.;
RT "Structure and expression of the Rat Homologue of CD5.";
RL Sapporo Igaku Zasshi 61:13-26(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PVG;
RX PubMed=7510236; DOI=10.1002/eji.1830240314;
RA Vermeer L.A., Boer de N.K., Bucci C., Bos N.A., Kroese F.G.M., Alberti S.;
RT "MRC OX19 recognizes the rat CD5 surface glycoprotein, but does not provide
RT evidence for a population of CD5bright B cells.";
RL Eur. J. Immunol. 24:585-592(1994).
CC -!- FUNCTION: May act as a receptor in regulating T-cell proliferation.
CC -!- SUBUNIT: Interacts with CD72/LYB-2. Interacts with PTPN6/SHP-1 (By
CC similarity). {ECO:0000250}.
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:0000250}.
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DR EMBL; D10728; BAA01571.1; -; mRNA.
DR EMBL; X78985; CAA55586.1; -; mRNA.
DR PIR; S43536; S43536.
DR RefSeq; NP_062168.1; NM_019295.1.
DR AlphaFoldDB; P51882; -.
DR SMR; P51882; -.
DR STRING; 10116.ENSRNOP00000051697; -.
DR GlyGen; P51882; 3 sites.
DR iPTMnet; P51882; -.
DR PhosphoSitePlus; P51882; -.
DR PaxDb; P51882; -.
DR PRIDE; P51882; -.
DR GeneID; 54236; -.
DR KEGG; rno:54236; -.
DR UCSC; RGD:2309; rat.
DR CTD; 921; -.
DR RGD; 2309; Cd5.
DR VEuPathDB; HostDB:ENSRNOG00000020872; -.
DR eggNOG; ENOG502RYTM; Eukaryota.
DR InParanoid; P51882; -.
DR OrthoDB; 1017770at2759; -.
DR PhylomeDB; P51882; -.
DR PRO; PR:P51882; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020872; Expressed in thymus and 11 other tissues.
DR ExpressionAtlas; P51882; baseline and differential.
DR Genevisible; P51882; RN.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:RGD.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0009966; P:regulation of signal transduction; NAS:RGD.
DR GO; GO:0031295; P:T cell costimulation; ISO:RGD.
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; 1.
DR SUPFAM; SSF56487; SSF56487; 2.
DR PROSITE; PS50287; SRCR_2; 3.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..491
FT /note="T-cell surface glycoprotein CD5"
FT /id="PRO_0000033224"
FT TOPO_DOM 25..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..131
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 157..266
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 274..364
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 467..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 449
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 58..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 79..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 105..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 199..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 242..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 283..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 299..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 314..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 339..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CONFLICT 27
FT /note="R -> RDGPGKKEHEKGR (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 218..223
FT /note="GTPAPA -> ELQLCS (in Ref. 2; CAA55586)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..372
FT /note="GLA -> AW (in Ref. 2; CAA55586)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="V -> M (in Ref. 2; CAA55586)"
FT /evidence="ECO:0000305"
FT CONFLICT 457..458
FT /note="RL -> W (in Ref. 2; CAA55586)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="R -> K (in Ref. 2; CAA55586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 53440 MW; 88DD76F8E6891CDE CRC64;
MDSHEVLLAA TYLLGTLAAF CLGQSGRGFV GAQVMLSGSN SKCQGLVEVQ MNGMKTVCSS
SWRLSQDLWK NANEASTVCQ QLGCGNPLAL GHLTLWNRPK NQILCQGPPW SFSNCSTSSL
GQCLPLSLVC LEPQKTTPLP TTTLPTTMPE PTAPPRLQLV PGHEGLRCTG VVEFYNGSRG
GTILYKAKAR PVDLGNLICK SLQCGSFLTH LSRIETAGTP APAELRDPRP LPIRWEAQNG
SCTSLQQCFQ KTTVQEGSQA LAVVCSDFQP KVQSRLVGGS SVCEGIAEVR QRSQWAALCD
SSAARGPGRW EELCQEQQCG NLISFHVMDA DRTSPGVLCT QEKLSQCYQL QKKTHCKRVF
ITCKDPNPVG LAPGTVASII LTLVLLVVLM VMCGPLIYKK LVKKFRQKKQ RQWIGPTGVN
QSMSFHRSHT ATVRSQVENP AASHVDNEYS QPPRNSRLSA YPALEGALHR SSTQPDNSSD
SDYDLQVAQR L