SIT1_RAT
ID SIT1_RAT Reviewed; 178 AA.
AC Q5M869;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Signaling threshold-regulating transmembrane adapter 1;
DE AltName: Full=SHP2-interacting transmembrane adapter protein;
DE AltName: Full=Suppression-inducing transmembrane adapter 1;
GN Name=Sit1; Synonyms=Sit;
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).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16160011; DOI=10.1182/blood-2005-06-2273;
RA Tedoldi S., Paterson J.C., Hansmann M.-L., Natkunam Y., Rudiger T.,
RA Angelisova P., Du M.Q., Roberton H., Roncador G., Sanchez L., Pozzobon M.,
RA Masir N., Barry R., Pileri S., Mason D.Y., Marafioti T., Horejsi V.;
RT "Transmembrane adaptor molecules: a new category of lymphoid-cell
RT markers.";
RL Blood 107:213-221(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-87; SER-89 AND
RP SER-164, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Negatively regulates T-cell antigen receptor (TCR)-mediated
CC signaling. Involved in positive selection of T-cells.
CC -!- SUBUNIT: Homodimer; disulfide-linked. When phosphorylated, interacts
CC with PTPN11/SHP2, GRB2 and CSK (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Lymph node, spleen and thymus.
CC {ECO:0000269|PubMed:16160011}.
CC -!- PTM: Phosphorylated on tyrosines upon TCR activation; which promotes
CC recruitment of PTPN11, GRB2 and CSK. {ECO:0000250}.
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DR EMBL; BC088199; AAH88199.1; -; mRNA.
DR RefSeq; NP_001019515.1; NM_001024344.1.
DR AlphaFoldDB; Q5M869; -.
DR STRING; 10116.ENSRNOP00000036171; -.
DR GlyGen; Q5M869; 1 site.
DR iPTMnet; Q5M869; -.
DR PhosphoSitePlus; Q5M869; -.
DR PaxDb; Q5M869; -.
DR PRIDE; Q5M869; -.
DR Ensembl; ENSRNOT00000035040; ENSRNOP00000036171; ENSRNOG00000021546.
DR GeneID; 500449; -.
DR KEGG; rno:500449; -.
DR UCSC; RGD:1559919; rat.
DR CTD; 27240; -.
DR RGD; 1559919; Sit1.
DR eggNOG; ENOG502S87Q; Eukaryota.
DR GeneTree; ENSGT00390000016476; -.
DR HOGENOM; CLU_111407_0_0_1; -.
DR InParanoid; Q5M869; -.
DR OMA; LFRWTSG; -.
DR OrthoDB; 1355800at2759; -.
DR PhylomeDB; Q5M869; -.
DR TreeFam; TF337816; -.
DR PRO; PR:Q5M869; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000021546; Expressed in thymus and 10 other tissues.
DR Genevisible; Q5M869; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0050863; P:regulation of T cell activation; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
DR InterPro; IPR033269; Sit1.
DR PANTHER; PTHR15604; PTHR15604; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..178
FT /note="Signaling threshold-regulating transmembrane adapter
FT 1"
FT /id="PRO_0000083342"
FT TOPO_DOM 1..23
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 72..75
FT /note="Interaction with GRB2"
FT /evidence="ECO:0000250"
FT REGION 81..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..133
FT /note="Interaction with PTPN11"
FT /evidence="ECO:0000250"
FT REGION 151..154
FT /note="Interaction with CSK"
FT /evidence="ECO:0000250"
FT REGION 170..173
FT /note="Interaction with GRB2"
FT /evidence="ECO:0000250"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P8"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 72
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P8"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P8"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 109
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P8"
FT MOD_RES 126
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P8"
FT MOD_RES 130
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P8"
FT MOD_RES 151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P8"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 170
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3P8"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 178 AA; 19368 MW; 518FD149CC3D7E2C CRC64;
MSRENNCTTA DLAWGIPSIT QAWGLWALFG VVTMLLLISL AALLSQWTRG RRRTQEEQGP
PSGRSVEEVP LYGNLHYLQT GRLSEESRSE EQDPSSGGLA RGAEEATCYT SLQLRPAQGR
IPSSGTPIKY CEVVLDSEPK PQASGPEPEL YASVCAQTRR ARASFPDQAY ANSQPAPS
