Cd5
entrez
12507
canonical
uniprot
P13379
canonical
ensembl
ENSMUSG00000024669
resolver
ensp
ENSMUSP00000025571
resolver
ensp
ENSMUSP00000158313
resolver
enst
ENSMUST00000025571
resolver
genesymbol
Cd5
resolver
genesymbol_syn
Ly-1
resolver
uniprot
Q3UP78
resolver
uniprot_entry
CD5_MOUSE
resolver
uniprot_entry
Q3UP78_MOUSE
resolver
amino_acid_sequence
MDSHEVLLAATYLLGTLAAFCLGQSGRGGLDIQVMLSGSNSKCQGQVEIQMENKWKTVCSSSWRLSQDHSKNAQQASAVCKQLRCGDPLALGPFPSLNRPQNQVFCQGSPWSISNCNNTSSQDQCLPLSLICLEPQRTTPPPTTTPPTTVPEPTAPPRLQLVPGHEGLRCTGVVEFYNGSWGGTILYKAKDRPLGLGNLICKSLQCGSFLTHLSGTEAAGTPAPAELRDPRPLPIRWEAPNGSCVSLQQCFQKTTAQEGGQALTVICSDFQPKVQSRLVGGSSVCEGIAEVRQRSQWEALCDSSAARGRGRWEELCREQQCGDLISFHTVDADKTSPGFLCAQEKLSQCYHLQKKKHCNKRVFVTCQDPNPAGLAPGTVASIILTLVLLVVLLAMCGPLVYKKLVKKFRQKKQRQWIGPTGVNQNMSFHRSHTATVRSQVENPTASHVDNEYSQPPRNSHLSAYPALEGALHRSSTQPDNSSDSDYDLQVAQRL
uniprot
proteins
function
FUNCTION: Lymphoid-specific receptor expressed by all T-cells and in a subset of B-cells known as B1a cells. Plays a role in the regulation of TCR and BCR signaling, thymocyte selection, T-cell effector differentiation and immune tolerance (PubMed:35720357). Acts by interacting with several ligands expressed on B-cells such as CD5L or CD72 and thereby plays an important role in contact-mediated, T-dependent B-cell activation and in the maintenance of regulatory T and B-cell homeostasis (PubMed:24950378, PubMed:9064341, PubMed:9723705). Functions as a negative regulator of TCR signaling during thymocyte development by associating with several signaling proteins including LCK, CD3Z chain, PI3K or CBL (PubMed:11157848). Mechanistically, co-engagement of CD3 with CD5 enhances phosphorylated CBL recruitment leading to increased VAV1 phosphorylation and degradation (By similarity). Modulates B-cell biology through ERK1/2 activation in a Ca(2+)-dependent pathway via the non-selective Ca(2+) channel TRPC1, leading to IL-10 production (By similarity). {ECO:0000250|UniProtKB:P06127, ECO:0000269|PubMed:24950378, ECO:0000269|PubMed:35720357, ECO:0000269|PubMed:9064341, ECO:0000269|PubMed:9723705}.
uniprot
proteins
mass_dalton
53849
uniprot
proteins
mutagenesis
MUTAGEN 452; /note="Y->F: Complete loss of LCK binding."; /evidence="ECO:0000269|PubMed:11157848"; MUTAGEN 464; /note="Y->F: No loss of LCK binding."; /evidence="ECO:0000269|PubMed:11157848"; MUTAGEN 486; /note="Y->F: Complete loss of LCK binding."; /evidence="ECO:0000269|PubMed:11157848
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine, threonine and tyrosine residues following TCR stimulation (PubMed:11007759). Phosphorylated by LCK on Tyr-452 and Tyr-486 upon TCR engagement (PubMed:11157848). {ECO:0000269|PubMed:11007759, ECO:0000269|PubMed:11157848}.
uniprot
proteins
pubmed
11007759
uniprot
proteins
pubmed
11157848
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24950378
uniprot
proteins
pubmed
3025855
uniprot
proteins
pubmed
35720357
uniprot
proteins
pubmed
36002232
uniprot
proteins
pubmed
7536775
uniprot
proteins
pubmed
9064341
uniprot
proteins
pubmed
9723705
uniprot
proteins
sequence_length
494
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 372..401; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins