LAX1_BOVIN
ID LAX1_BOVIN Reviewed; 387 AA.
AC Q58CT8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Lymphocyte transmembrane adapter 1;
DE AltName: Full=Membrane-associated adapter protein LAX;
GN Name=LAX1; Synonyms=LAX;
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 [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Negatively regulates TCR (T-cell antigen receptor)-mediated
CC signaling in T-cells and BCR (B-cell antigen receptor)-mediated
CC signaling in B-cells. {ECO:0000250}.
CC -!- SUBUNIT: When phosphorylated, interacts with GRB2, PIK3R1 and GRAP2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III
CC membrane protein {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosines upon TCR or BCR activation; which
CC leads to the recruitment of GRB2, PIK3R1 and GRAP2. {ECO:0000250}.
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DR EMBL; BT021859; AAX46706.1; -; mRNA.
DR RefSeq; NP_001015674.1; NM_001015674.1.
DR RefSeq; XP_005216749.1; XM_005216692.2.
DR AlphaFoldDB; Q58CT8; -.
DR STRING; 9913.ENSBTAP00000016385; -.
DR PaxDb; Q58CT8; -.
DR PRIDE; Q58CT8; -.
DR Ensembl; ENSBTAT00000016385; ENSBTAP00000016385; ENSBTAG00000012349.
DR GeneID; 540424; -.
DR KEGG; bta:540424; -.
DR CTD; 54900; -.
DR VEuPathDB; HostDB:ENSBTAG00000012349; -.
DR VGNC; VGNC:30802; LAX1.
DR eggNOG; ENOG502SP30; Eukaryota.
DR GeneTree; ENSGT00390000014063; -.
DR HOGENOM; CLU_058345_0_0_1; -.
DR InParanoid; Q58CT8; -.
DR OMA; RDYINVP; -.
DR OrthoDB; 1008191at2759; -.
DR TreeFam; TF337411; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000012349; Expressed in abdominal lymph node and 83 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; 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:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0050851; P:antigen receptor-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042113; P:B cell activation; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046649; P:lymphocyte activation; IBA:GO_Central.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0050868; P:negative regulation of T cell activation; IBA:GO_Central.
DR InterPro; IPR031393; LAX.
DR PANTHER; PTHR24091; PTHR24091; 1.
DR Pfam; PF15681; LAX; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Immunity; Membrane; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..387
FT /note="Lymphocyte transmembrane adapter 1"
FT /id="PRO_0000083328"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 114..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT MOD_RES 270
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT MOD_RES 296
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT MOD_RES 375
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV1"
SQ SEQUENCE 387 AA; 41859 MW; 2A0136AC143958DB CRC64;
MDVTTSAWSE TTRRISEPST LQGTLGSLDK AEDHSSSIFS GFAALLAILL VVAVICVLWC
CGKRKKRQVP YLRVTIMPLL TLPRPRQRAK NIYDLLPRRQ EELGRHPSRS IRIVSTESLL
SRNSDSPSSE HVPSRAGDAL HMHRAHTHAM GYAVGIYDNA MRPQMCGNLA PSPHYVNVRA
SRGSPSTSSE DSRDYVNIPT AKEIAETLAS ASNPPRNLFI LPGTKELAPS EEIDEGCGNA
SDCTSLGSPG TENSDPLSDG EGSSQTSNDY VNMAELDLGT PQGKQLQGMF QCRRDYENVP
PGPSSNKQQE EEVTSSNTDH VEGRTDGPET HTPPAVQSGS FLALKDHVAC QSSAHSETGP
WEDAEETSSE DSHDYENVCA AEAGARG
