ID   NTAL_RAT                Reviewed;         204 AA.
AC   Q8CGL2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Linker for activation of T-cells family member 2;
DE   AltName: Full=Linker for activation of B-cells;
DE   AltName: Full=Non-T-cell activation linker;
GN   Name=Lat2; Synonyms=Lab, Ntal, Wbscr5;
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 [MRNA].
RC   STRAIN=Wistar;
RA   Tumova M., Luskova P., Draber P.;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in FCER1 (high affinity immunoglobulin epsilon
CC       receptor)-mediated signaling in mast cells. May also be involved in BCR
CC       (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high
CC       affinity immunoglobulin gamma Fc receptor I)-mediated signaling in
CC       myeloid cells. Couples activation of these receptors and their
CC       associated kinases with distal intracellular events through the
CC       recruitment of GRB2 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: When phosphorylated, interacts with GRB2. May also interact
CC       with SOS1, GAB1 and CBL (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III
CC       membrane protein {ECO:0000250}. Note=Present in lipid rafts.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosines following cross-linking of BCR in B-
CC       cells, high affinity IgG receptor (FCGR1) in myeloid cells, or high
CC       affinity IgE receptor (FCER1) in mast cells; which induces the
CC       recruitment of GRB2.
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DR   EMBL; AY170849; AAO12808.1; -; mRNA.
DR   RefSeq; NP_776212.1; NM_173840.1.
DR   AlphaFoldDB; Q8CGL2; -.
DR   STRING; 10116.ENSRNOP00000031304; -.
DR   PhosphoSitePlus; Q8CGL2; -.
DR   PaxDb; Q8CGL2; -.
DR   GeneID; 317676; -.
DR   KEGG; rno:317676; -.
DR   UCSC; RGD:631397; rat.
DR   CTD; 7462; -.
DR   RGD; 631397; Lat2.
DR   eggNOG; ENOG502SH0N; Eukaryota.
DR   InParanoid; Q8CGL2; -.
DR   OrthoDB; 1271896at2759; -.
DR   PhylomeDB; Q8CGL2; -.
DR   Reactome; R-RNO-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   PRO; PR:Q8CGL2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0042113; P:B cell activation; ISO:RGD.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; ISO:RGD.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR   GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR   InterPro; IPR031428; LAT2.
DR   PANTHER; PTHR15646; PTHR15646; 1.
DR   Pfam; PF15703; LAT2; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity; Cell membrane; Immunity; Lipoprotein;
KW   Mast cell degranulation; Membrane; Palmitate; Phosphoprotein;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..204
FT                   /note="Linker for activation of T-cells family member 2"
FT                   /id="PRO_0000083336"
FT   TOPO_DOM        1..7
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..204
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          147..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         60
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHL0"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHL0"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHL0"
FT   MOD_RES         140
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZY6"
FT   MOD_RES         161
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZY6"
FT   MOD_RES         193
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZY6"
FT   LIPID           27
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           30
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   204 AA;  23130 MW;  16281048E33E1316 CRC64;
     MNAELELLWP LSGLLLLLLL GTTAWLCVQC SRPGVKRNEK IYEQRNQQEN EQSVASSQTY
     SLARPVRTGL QMDAASNKSF ERKNKLLFSH LEGPESPRYQ NFYKGSRRES DAAYVDPIPT
     DYYNWGCFQK PPEDNDSNSY ENVLICKPST PESGTEESED YQNSVSILQW RESKRTMGAR
     TSPSGSPDEE PDYVNGDVAT TEKI