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TYOBP_MACMU
ID   TYOBP_MACMU             Reviewed;         113 AA.
AC   Q8WNQ8;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=TYRO protein tyrosine kinase-binding protein {ECO:0000250|UniProtKB:O43914};
DE   AltName: Full=DNAX-activation protein 12 {ECO:0000250|UniProtKB:O43914};
DE   Flags: Precursor;
GN   Name=TYROBP {ECO:0000250|UniProtKB:O43914};
GN   Synonyms=DAP12 {ECO:0000250|UniProtKB:O43914};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   LaBonte M.L., Letvin N.L.;
RT   "Identification of rhesus monkey DAP10 and DAP12.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adapter protein which non-covalently associates with
CC       activating receptors found on the surface of a variety of immune cells
CC       to mediate signaling and cell activation following ligand binding by
CC       the receptors (By similarity). TYROBP is tyrosine-phosphorylated in the
CC       ITAM domain following ligand binding by the associated receptors which
CC       leads to activation of additional tyrosine kinases and subsequent cell
CC       activation (By similarity). Also has an inhibitory role in some cells
CC       (By similarity). Non-covalently associates with activating receptors of
CC       the CD300 family to mediate cell activation (By similarity). Also
CC       mediates cell activation through association with activating receptors
CC       of the CD200R family (By similarity). Required for neutrophil
CC       activation mediated by integrin (By similarity). Required for the
CC       activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (By
CC       similarity). Associates with natural killer (NK) cell receptors such as
CC       the KLRD1/KLRC2 heterodimer to mediate NK cell activation (By
CC       similarity). Associates with TREM1 to mediate activation of neutrophils
CC       and monocytes (By similarity). Associates with TREM2 on monocyte-
CC       derived dendritic cells to mediate up-regulation of chemokine receptor
CC       CCR7 and dendritic cell maturation and survival (By similarity).
CC       Association with TREM2 mediates cytokine-induced formation of
CC       multinucleated giant cells which are formed by the fusion of
CC       macrophages (By similarity). Stabilizes the TREM2 C-terminal fragment
CC       (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the
CC       release of pro-inflammatory cytokines (By similarity). In microglia,
CC       required with TREM2 for phagocytosis of apoptotic neurons (By
CC       similarity). Required with ITGAM/CD11B in microglia to control
CC       production of microglial superoxide ions which promote the neuronal
CC       apoptosis that occurs during brain development (By similarity).
CC       Promotes pro-inflammatory responses in microglia following nerve injury
CC       which accelerates degeneration of injured neurons (By similarity).
CC       Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10
CC       production by liver dendritic cells and inhibits their T cell
CC       allosimulatory ability (By similarity). Negatively regulates B cell
CC       proliferation (By similarity). Required for CSF1-mediated osteoclast
CC       cytoskeletal organization (By similarity). Positively regulates
CC       multinucleation during osteoclast development (By similarity).
CC       {ECO:0000250|UniProtKB:O43914, ECO:0000250|UniProtKB:O54885}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Homotrimer;
CC       disulfide-linked (By similarity). Homotetramer; disulfide-linked (By
CC       similarity). Homotrimers and homotetramers form when low levels of
CC       partner receptors are available and is competitive with assembly with
CC       interacting receptors (By similarity). They may represent alternative
CC       oligomerization states or may be intermediates in the receptor assembly
CC       process (By similarity). Binding of a metal cation aids in
CC       homooligomerization through coordination of the metal ion by the
CC       subunits of the oligomer (By similarity). Interacts with TREM1 (By
CC       similarity). Interacts with TREM2 (By similarity). Interacts with
CC       CLECSF5 (By similarity). Interacts with CD300LB and CD300C2 (By
CC       similarity). Interacts with CD300E (By similarity). Interacts (via ITAM
CC       domain) with SYK (via SH2 domains); activates SYK mediating neutrophils
CC       and macrophages integrin-mediated activation (By similarity). Interacts
CC       with KLRC2 (By similarity). Interacts with CD300H (By similarity).
CC       Interacts with KLRD1 (By similarity). {ECO:0000250|UniProtKB:O43914,
CC       ECO:0000250|UniProtKB:O54885}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43914};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- PTM: Following ligand binding by associated receptors, tyrosine
CC       phosphorylated in the ITAM domain which leads to activation of
CC       additional tyrosine kinases and subsequent cell activation.
CC       {ECO:0000250|UniProtKB:O43914}.
CC   -!- SIMILARITY: Belongs to the TYROBP family. {ECO:0000305}.
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DR   EMBL; AF321611; AAL37224.1; -; mRNA.
DR   RefSeq; NP_001028039.1; NM_001032867.1.
DR   AlphaFoldDB; Q8WNQ8; -.
DR   SMR; Q8WNQ8; -.
DR   STRING; 9544.ENSMMUP00000010492; -.
DR   GeneID; 574207; -.
DR   KEGG; mcc:574207; -.
DR   CTD; 7305; -.
DR   eggNOG; ENOG502SCVI; Eukaryota.
DR   HOGENOM; CLU_141718_0_0_1; -.
DR   InParanoid; Q8WNQ8; -.
DR   OMA; VFCFATH; -.
DR   TreeFam; TF336898; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0043277; P:apoptotic cell clearance; ISS:UniProtKB.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0002222; P:stimulatory killer cell immunoglobulin-like receptor signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR026200; Tyrobp.
DR   PANTHER; PTHR17554; PTHR17554; 1.
PE   3: Inferred from homology;
KW   Calcium; Cell membrane; Disulfide bond; Immunity; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..113
FT                   /note="TYRO protein tyrosine kinase-binding protein"
FT                   /id="PRO_0000022604"
FT   TOPO_DOM        28..40
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:O43914"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O43914"
FT   TOPO_DOM        62..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O43914"
FT   DOMAIN          80..108
FT                   /note="ITAM"
FT   REGION          75..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         50
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits in homooligomer"
FT                   /evidence="ECO:0000250|UniProtKB:O43914"
FT   SITE            54
FT                   /note="Important for interaction with transmembrane
FT                   receptors"
FT                   /evidence="ECO:0000250|UniProtKB:O43914"
FT   MOD_RES         91
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O54885"
FT   MOD_RES         102
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O54885"
FT   DISULFID        35
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:O43914"
SQ   SEQUENCE   113 AA;  12131 MW;  4BBCDC70B4CB6DE5 CRC64;
     MGGLEPCSRL LLLPLLLAVG GLRPVQAQAQ SDCSCSTVSP GVLAGIVLGD LVLTVLIALA
     VYFLGRLVPR GRGAAEAATR KQRITETESP YQELQGQRSD VYSDLNTQRP YYK
 
 
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