ID   LAX1_RAT                Reviewed;         406 AA.
AC   Q5FVQ5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Lymphocyte transmembrane adapter 1;
DE   AltName: Full=Membrane-associated adapter protein LAX;
GN   Name=Lax1; Synonyms=Lax;
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 [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC089837; AAH89837.1; -; mRNA.
DR   RefSeq; NP_001017491.1; NM_001017491.1.
DR   RefSeq; XP_017454368.1; XM_017598879.1.
DR   AlphaFoldDB; Q5FVQ5; -.
DR   STRING; 10116.ENSRNOP00000032707; -.
DR   iPTMnet; Q5FVQ5; -.
DR   PhosphoSitePlus; Q5FVQ5; -.
DR   PaxDb; Q5FVQ5; -.
DR   PRIDE; Q5FVQ5; -.
DR   Ensembl; ENSRNOT00000029533; ENSRNOP00000032707; ENSRNOG00000028250.
DR   GeneID; 498232; -.
DR   KEGG; rno:498232; -.
DR   UCSC; RGD:1563522; rat.
DR   CTD; 54900; -.
DR   RGD; 1563522; Lax1.
DR   eggNOG; ENOG502SP30; Eukaryota.
DR   GeneTree; ENSGT00390000014063; -.
DR   HOGENOM; CLU_058345_0_0_1; -.
DR   InParanoid; Q5FVQ5; -.
DR   OMA; RDYINVP; -.
DR   OrthoDB; 1008191at2759; -.
DR   PhylomeDB; Q5FVQ5; -.
DR   TreeFam; TF337411; -.
DR   PRO; PR:Q5FVQ5; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000028250; Expressed in spleen and 10 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0050851; P:antigen receptor-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0042113; P:B cell activation; ISO:RGD.
DR   GO; GO:0006955; P:immune response; ISO:RGD.
DR   GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR   GO; GO:0046649; P:lymphocyte activation; ISO:RGD.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:RGD.
DR   GO; GO:0050868; P:negative regulation of T cell activation; ISO:RGD.
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..406
FT                   /note="Lymphocyte transmembrane adapter 1"
FT                   /id="PRO_0000083331"
FT   TOPO_DOM        1..33
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..406
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         184
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT   MOD_RES         259
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT   MOD_RES         285
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT   MOD_RES         352
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWV1"
SQ   SEQUENCE   406 AA;  43936 MW;  5F3366C0697193C0 CRC64;
     MYTTPAPPEI TRRSSEPSTQ QGTLGSLEGE KGHLLFPGFV VLVTIFLVVI VTCILWSRKK
     QKKRRVPYLQ VTPSLALPPP RQRAKNIYDF LPRQQTELGR HQLSGFSTES LLSRASDSPE
     PEVPQASGSL QKHRASVHAV EYTVGVYDNG TVAQMCGPLA SSAHRVCDGT SRNNSISSKE
     SNDYVNIPTA EDTSETLTCT KSTPESHLGL PSGQRLEFAE GGHAGCGKAT DRTGVWAPGL
     QGSNSLSEGD DSSQSSNDYV NMTGLDLEDI QESRPRVAFQ CCRDYENVPP VVANGSQLQT
     VEEVTSSTTD RGEPAQRTLP SVYHMAFRPS AWSEDGAMIP GEEASNGDSS DYENVLVPEL
     EGKDWKQGPG TWHPSDERTP SDQAGKFCEA VYPAGSLATE TSGEEV