CD5_BOVIN
ID CD5_BOVIN Reviewed; 495 AA.
AC P19238; Q2HJA1;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=T-cell surface glycoprotein CD5;
DE AltName: CD_antigen=CD5;
DE Flags: Precursor;
GN Name=CD5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=1698281; DOI=10.1093/nar/18.17.5296;
RA Yu Q., Reichert M., Brousseau T., Cleuter Y., Burny A., Kettmann R.;
RT "Sequence of bovine CD5.";
RL Nucleic Acids Res. 18:5296-5296(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; X53061; CAA37231.1; -; mRNA.
DR EMBL; BC113237; AAI13238.1; -; mRNA.
DR PIR; S11270; S11270.
DR RefSeq; NP_776324.1; NM_173899.2.
DR AlphaFoldDB; P19238; -.
DR SMR; P19238; -.
DR STRING; 9913.ENSBTAP00000018258; -.
DR PaxDb; P19238; -.
DR PRIDE; P19238; -.
DR Ensembl; ENSBTAT00000018258; ENSBTAP00000018258; ENSBTAG00000013730.
DR GeneID; 280745; -.
DR KEGG; bta:280745; -.
DR CTD; 921; -.
DR VEuPathDB; HostDB:ENSBTAG00000013730; -.
DR VGNC; VGNC:27037; CD5.
DR eggNOG; ENOG502RYTM; Eukaryota.
DR GeneTree; ENSGT00390000017536; -.
DR HOGENOM; CLU_047656_0_0_1; -.
DR InParanoid; P19238; -.
DR OMA; FHRNHTA; -.
DR OrthoDB; 1017770at2759; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000013730; Expressed in mesenteric lymph node and 83 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IBA:GO_Central.
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; 2.
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 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:0000255"
FT CHAIN 24..495
FT /note="T-cell surface glycoprotein CD5"
FT /id="PRO_0000033221"
FT TOPO_DOM 24..372
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..134
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 160..266
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 274..368
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 475..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 453
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06127"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 80..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 108..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 202..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 242..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 283..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 301..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 316..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 342..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CONFLICT 312..313
FT /note="WE -> RV (in Ref. 1; CAA37231)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="A -> P (in Ref. 1; CAA37231)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 54367 MW; 8D72B01293132AE1 CRC64;
MGSQHLPLAA LYLLELLVTS CLGGLKVEVQ GLTMRLSGSG SRCQGRLEVS NGTEWYAVHS
QSWGQLSLYQ VAPRQFLKLC QELQCRDPLL LSSSRYFKEV QFQKLIICHG QLGSFSNCSL
NRGRQVDSLA LICLEPPRTT APPTTSPPTT TPEPTAPPRF QLVAEPGGLR CAGVVEFYSG
GLGGTIGIEP QNDIKDLGQL ICAALQCGSF LKPLPETEEA QTQKPEGQRP LPIRWEIQNP
KCTSLEQCFR KVQPWVGGQA LGLICSDFQP KVQSRLVGGS DVCEGSVEVR SGKGQKWDTL
CDDSWAKGTA RWEEVCREQQ CGNVSSYRGL DPSEKTLGGF YCPPGILSRC HKLEEKKSHC
KRVFVTCQNS SRAGLGAGAV MSIILALLLL AVLLVVCGPL AYKKVVKKFR QKKQRQWIGP
TGMNQNMSFH RNHTVTVRSQ VENATASHVE NEYSQPPRNS QISAYPALEG ALHRISTQPD
NSSDSDYELH GAQRL