LAX1_MOUSE
ID LAX1_MOUSE Reviewed; 407 AA.
AC Q8BHB3; Q8BS18; Q8CGV1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Lymphocyte transmembrane adapter 1;
DE AltName: Full=Linker for activation of X cells;
DE AltName: Full=Membrane-associated adapter protein LAX;
GN Name=Lax1; Synonyms=Lax;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12359715; DOI=10.1074/jbc.m208946200;
RA Zhu M., Janssen E., Leung K., Zhang W.;
RT "Molecular cloning of a novel gene encoding a membrane-associated adaptor
RT protein (LAX) in lymphocyte signaling.";
RL J. Biol. Chem. 277:46151-46158(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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).
RN [4]
RP INDUCTION, TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15843560; DOI=10.4049/jimmunol.174.9.5612;
RA Zhu M., Granillo O., Wen R., Yang K., Dai X., Wang D., Zhang W.;
RT "Negative regulation of lymphocyte activation by the adaptor protein LAX.";
RL J. Immunol. 174:5612-5619(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:0000269|PubMed:15843560}.
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 -!- TISSUE SPECIFICITY: Expressed in T-cells and B-cells.
CC {ECO:0000269|PubMed:15843560}.
CC -!- INDUCTION: Up-regulated in T- and B-cells following TCR and BCR
CC engagement, respectively. {ECO:0000269|PubMed:15843560}.
CC -!- PTM: Phosphorylated on tyrosines upon TCR or BCR activation; which
CC leads to the recruitment of GRB2, PIK3R1 and GRAP2. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable, fertile and healthy, and show
CC normal lymphocyte development. However, their T- and B-cells are
CC hyperresponsive to stimulation via TCR or BCR.
CC {ECO:0000269|PubMed:15843560}.
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DR EMBL; AY090785; AAM09819.1; -; mRNA.
DR EMBL; AK040834; BAC30715.1; -; mRNA.
DR EMBL; AK088503; BAC40394.1; -; mRNA.
DR EMBL; BC042765; AAH42765.1; -; mRNA.
DR CCDS; CCDS35711.1; -.
DR RefSeq; NP_001153121.1; NM_001159649.1.
DR RefSeq; NP_766430.3; NM_172842.3.
DR RefSeq; XP_006529620.1; XM_006529557.3.
DR AlphaFoldDB; Q8BHB3; -.
DR IntAct; Q8BHB3; 1.
DR STRING; 10090.ENSMUSP00000131126; -.
DR iPTMnet; Q8BHB3; -.
DR PhosphoSitePlus; Q8BHB3; -.
DR EPD; Q8BHB3; -.
DR PaxDb; Q8BHB3; -.
DR PRIDE; Q8BHB3; -.
DR ProteomicsDB; 264978; -.
DR Antibodypedia; 1184; 253 antibodies from 29 providers.
DR DNASU; 240754; -.
DR Ensembl; ENSMUST00000169295; ENSMUSP00000131126; ENSMUSG00000051998.
DR GeneID; 240754; -.
DR KEGG; mmu:240754; -.
DR UCSC; uc007cqs.2; mouse.
DR CTD; 54900; -.
DR MGI; MGI:2443362; Lax1.
DR VEuPathDB; HostDB:ENSMUSG00000051998; -.
DR eggNOG; ENOG502SP30; Eukaryota.
DR GeneTree; ENSGT00390000014063; -.
DR HOGENOM; CLU_058345_0_0_1; -.
DR InParanoid; Q8BHB3; -.
DR OMA; RDYINVP; -.
DR OrthoDB; 1008191at2759; -.
DR PhylomeDB; Q8BHB3; -.
DR TreeFam; TF337411; -.
DR BioGRID-ORCS; 240754; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q8BHB3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BHB3; protein.
DR Bgee; ENSMUSG00000051998; Expressed in mesenteric lymph node and 41 other tissues.
DR ExpressionAtlas; Q8BHB3; baseline and differential.
DR Genevisible; Q8BHB3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0050851; P:antigen receptor-mediated signaling pathway; IMP:MGI.
DR GO; GO:0042113; P:B cell activation; ISO:MGI.
DR GO; GO:0006955; P:immune response; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0046649; P:lymphocyte activation; IMP:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0050868; P:negative regulation of T cell activation; ISO:MGI.
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..407
FT /note="Lymphocyte transmembrane adapter 1"
FT /id="PRO_0000083330"
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..407
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 331..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT MOD_RES 260
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT MOD_RES 286
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT MOD_RES 353
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV1"
FT CONFLICT 67
FT /note="P -> S (in Ref. 2; BAC40394 and 3; AAH42765)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="N -> D (in Ref. 2; BAC40394 and 3; AAH42765)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> V (in Ref. 2; BAC30715)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="R -> G (in Ref. 2; BAC40394 and 3; AAH42765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 44838 MW; 00C3F063A7CFC7BE CRC64;
MYSTPAPPEV TRRNSEPSTR QGTLGSLQGE KGQIIFPGFV VLLTIILVII AACILWSWKK
QKKRPVPYFQ VAPSLTLPPP RHRAKNIYDF LPRQQTELGR HQLSGFSTES LLSRASDSPE
PEAPQANGSL QMHRVSVHTV EYSVNIYDNG TVPQMCRHLA SSTHHVCVRT SRSNPSISSK
ESNDYVNIPT VEDTCETLTR IESTPENHLG LPSALRLEFA EGGHAGCGNA TDHDGFWAPG
PKCSDSLSDG DDLSQTSNDY VNMTGLDLEN IQENRPRGAF QCCRDYENVP WVDTNESQLP
TLEEVASSTV DHREPVWRTL SSVYHMAFQP SAQSEDSAMV HREEQSSEDS SDYETVLVAE
LEGRDWKQGP GTQHPSDEGT PGDLAGKLCE VVYPAGSLAT ETSDEDA
