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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
 
 
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