ID   NTAL_CHICK              Reviewed;         198 AA.
AC   Q5S7W5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-23 AND CYS-26,
RP   PALMITOYLATION AT CYS-23 AND CYS-26, PHOSPHORYLATION, INTERACTION WITH
RP   GRB2, PHOSPHORYLATION AT TYR-136; TYR-155 AND TYR-184, AND FUNCTION.
RX   PubMed=15539154; DOI=10.1016/j.immuni.2004.09.007;
RA   Stork B., Engelke M., Frey J., Horejsi V., Hamm-Baarke A., Schraven B.,
RA   Kurosaki T., Wienands J.;
RT   "Grb2 and the non-T cell activation linker NTAL constitute a Ca(2+)-
RT   regulating signal circuit in B lymphocytes.";
RL   Immunity 21:681-691(2004).
CC   -!- FUNCTION: Involved in BCR (B-cell antigen receptor)-mediated signaling
CC       in B-cells. May also be involved in FCER1 (high affinity immunoglobulin
CC       epsilon receptor)-mediated signaling in mast 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 such as calcium
CC       mobilization through the recruitment of GRB2.
CC       {ECO:0000269|PubMed:15539154}.
CC   -!- SUBUNIT: When phosphorylated, interacts with GRB2.
CC       {ECO:0000269|PubMed:15539154}.
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; which
CC       induces the recruitment of GRB2. {ECO:0000269|PubMed:15539154}.
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DR   EMBL; AY743659; AAV36793.1; -; mRNA.
DR   RefSeq; NP_001007483.1; NM_001007482.1.
DR   AlphaFoldDB; Q5S7W5; -.
DR   SMR; Q5S7W5; -.
DR   STRING; 9031.ENSGALP00000001985; -.
DR   iPTMnet; Q5S7W5; -.
DR   PaxDb; Q5S7W5; -.
DR   GeneID; 417489; -.
DR   KEGG; gga:417489; -.
DR   CTD; 7462; -.
DR   VEuPathDB; HostDB:geneid_417489; -.
DR   eggNOG; ENOG502SH0N; Eukaryota.
DR   HOGENOM; CLU_099084_0_0_1; -.
DR   InParanoid; Q5S7W5; -.
DR   OrthoDB; 1271896at2759; -.
DR   PhylomeDB; Q5S7W5; -.
DR   PRO; PR:Q5S7W5; -.
DR   Proteomes; UP000000539; Unplaced.
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:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0042113; P:B cell activation; IBA:GO_Central.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR   InterPro; IPR031428; LAT2.
DR   PANTHER; PTHR15646; PTHR15646; 2.
DR   Pfam; PF15703; LAT2; 1.
PE   1: Evidence at protein 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..198
FT                   /note="Linker for activation of T-cells family member 2"
FT                   /id="PRO_0000083337"
FT   TOPO_DOM        1..4
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..24
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         136
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000305|PubMed:15539154"
FT   MOD_RES         155
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000305|PubMed:15539154"
FT   MOD_RES         184
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000305|PubMed:15539154"
FT   LIPID           23
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:15539154"
FT   LIPID           26
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000305|PubMed:15539154"
FT   MUTAGEN         23
FT                   /note="C->A: Abolishes phosphorylation following BCR
FT                   activation; when associated with A-26."
FT                   /evidence="ECO:0000269|PubMed:15539154"
FT   MUTAGEN         26
FT                   /note="C->A: Abolishes phosphorylation following BCR
FT                   activation; when associated with A-26."
FT                   /evidence="ECO:0000269|PubMed:15539154"
SQ   SEQUENCE   198 AA;  22277 MW;  6DDEC0FADD043CCF CRC64;
     MAQPELLWAA AGLMLLGVAV SACVRCQLYA TKRGKDGSQG SRLERPQRFE VIRSCSAVTR
     RPERIKEPEH LARKAPEELS TSCHVGFESS AEPRYQNFLT EDCLHEDAAY VEPVPLDYYS
     HNRFFSPPND EDSHSYQNVI IGDPCSSELD DAEDYENSTA IEVWKVQQAK AMLYAESQDE
     EPDYVNTDPT IDAVVLSK