SKAP1_RAT
ID SKAP1_RAT Reviewed; 354 AA.
AC Q4V7G1; Q8CHI6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Src kinase-associated phosphoprotein 1;
DE AltName: Full=SKAP55 adapter protein;
DE AltName: Full=Src family-associated phosphoprotein 1;
DE AltName: Full=Src kinase-associated phosphoprotein of 55 kDa;
DE Short=SKAP-55;
DE AltName: Full=pp55;
GN Name=Skap1; Synonyms=Scap1, Skap55;
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], PROTEIN SEQUENCE OF 120-129; 138-147; 177-186
RP AND 344-352, FUNCTION, INTERACTION WITH FYB1, AND IDENTIFICATION IN A
RP COMPLEX WITH FYB1 AND CLNK.
RX PubMed=12681493; DOI=10.1016/s0014-5793(03)00234-5;
RA Fujii Y., Wakahara S., Nakao T., Hara T., Ohtake H., Komurasaki T.,
RA Kitamura K., Tatsuno A., Fujiwara N., Hozumi N., Ra C., Kitamura D.,
RA Goitsuka R.;
RT "Targeting of MIST to Src-family kinases via SKAP55-SLAP-130 adaptor
RT complex in mast cells(1).";
RL FEBS Lett. 540:111-116(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=15199160; DOI=10.1128/mcb.24.13.6067-6075.2004;
RA Utting O., Sedgmen B.J., Watts T.H., Shi X., Rottapel R., Iulianella A.,
RA Lohnes D., Veillette A.;
RT "Immune functions in mice lacking Clnk, an SLP-76-related adaptor expressed
RT in a subset of immune cells.";
RL Mol. Cell. Biol. 24:6067-6075(2004).
CC -!- FUNCTION: Positively regulates T-cell receptor signaling by enhancing
CC the MAP kinase pathway (By similarity). Required for optimal
CC conjugation between T-cells and antigen-presenting cells by promoting
CC the clustering of integrin ITGAL on the surface of T-cells (By
CC similarity). May be involved in high affinity immunoglobulin epsilon
CC receptor signaling in mast cells (PubMed:12681493).
CC {ECO:0000250|UniProtKB:Q86WV1, ECO:0000269|PubMed:12681493}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with FYN (By similarity).
CC Interacts with PTPRC (By similarity). Interacts with GRB2 when
CC phosphorylated on Tyr-267 (By similarity). Interacts with FYB1, which
CC is required for SKAP2 protein stability (By similarity). Interacts with
CC FYB1, which is required for SKAP2 protein stability (By similarity).
CC Part of a complex consisting of SKAP1, FYB1 and CLNK (PubMed:12681493).
CC Interacts with RASGRP1 (By similarity). Interacts with FYB2 (By
CC similarity). {ECO:0000250|UniProtKB:Q86WV1,
CC ECO:0000269|PubMed:12681493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86WV1}. Nucleus
CC {ECO:0000250|UniProtKB:Q86WV1}. Cell membrane
CC {ECO:0000250|UniProtKB:Q86WV1}. Note=Upon T-cell stimulation,
CC translocates to lipid rafts at the cell membrane.
CC {ECO:0000250|UniProtKB:Q86WV1}.
CC -!- TISSUE SPECIFICITY: Expressed in mast cells (at protein level).
CC {ECO:0000269|PubMed:15199160}.
CC -!- DOMAIN: The SH3 domain interacts with FYB1.
CC {ECO:0000250|UniProtKB:Q86WV1}.
CC -!- PTM: Phosphorylated on tyrosines. Phosphorylation by FYN on Tyr-267 is
CC required for GRB2 interaction (By similarity). Phosphorylation by FYN
CC on Tyr-290 abolishes interaction with FYB1. Tyr-236 is dephosphorylated
CC by PTPRC (By similarity). {ECO:0000250|UniProtKB:Q86WV1}.
CC -!- SIMILARITY: Belongs to the SKAP family. {ECO:0000305}.
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DR EMBL; AB092812; BAC53665.1; -; mRNA.
DR EMBL; BC097931; AAH97931.1; -; mRNA.
DR RefSeq; NP_775433.2; NM_173311.2.
DR AlphaFoldDB; Q4V7G1; -.
DR SMR; Q4V7G1; -.
DR MINT; Q4V7G1; -.
DR STRING; 10116.ENSRNOP00000033594; -.
DR PhosphoSitePlus; Q4V7G1; -.
DR PaxDb; Q4V7G1; -.
DR PRIDE; Q4V7G1; -.
DR Ensembl; ENSRNOT00000030159; ENSRNOP00000033594; ENSRNOG00000023881.
DR GeneID; 286975; -.
DR KEGG; rno:286975; -.
DR UCSC; RGD:708436; rat.
DR CTD; 8631; -.
DR RGD; 708436; Skap1.
DR eggNOG; ENOG502QSSU; Eukaryota.
DR GeneTree; ENSGT00390000017856; -.
DR HOGENOM; CLU_062032_0_0_1; -.
DR InParanoid; Q4V7G1; -.
DR OMA; IFYYYSN; -.
DR OrthoDB; 767446at2759; -.
DR PhylomeDB; Q4V7G1; -.
DR TreeFam; TF331055; -.
DR PRO; PR:Q4V7G1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000023881; Expressed in thymus and 15 other tissues.
DR Genevisible; Q4V7G1; RN.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0044853; C:plasma membrane raft; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042101; C:T cell receptor complex; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0042169; F:SH2 domain binding; IPI:RGD.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0033625; P:positive regulation of integrin activation; ISO:RGD.
DR GO; GO:1903039; P:positive regulation of leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR CDD; cd12044; SH3_SKAP1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035765; SKAP1_SH3.
DR InterPro; IPR037781; SKAP_fam.
DR PANTHER; PTHR15129; PTHR15129; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00233; PH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Immunity; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..354
FT /note="Src kinase-associated phosphoprotein 1"
FT /id="PRO_0000270175"
FT DOMAIN 107..210
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 289..350
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 285..290
FT /note="Interaction with FYB1"
FT /evidence="ECO:0000250"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3UUV5"
FT MOD_RES 236
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q86WV1"
FT MOD_RES 267
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q86WV1"
FT MOD_RES 290
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="I -> V (in Ref. 1; BAC53665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40903 MW; 4620FC5BFD290CBD CRC64;
MQAIALPEEI CWLLEDAEDF LAEGLQNENL SPGAQDQRDH ILRGFQQIKS RYCWDFQPQG
DDLGQDGSDE NLSGTHGPAL ASDASFWSDY QEEGIDDIIR GAQELDNVIK QGYLEKKSKD
HSFFGSEWQK RWCVISRGLF LYYANEKSKQ PKGTFLIKGY NVRMAPHLRK DSKKDSCFEL
TSQDRRSYEF TAFSPAEARD WVDQISFLLK DLSSLTIPFE EEEEEEEEDK EQEEMYNDID
GFDSARSGSQ GRAMALPEPL DKEEDVYEVL PDEDDLEEDA CGAHRRRVDY ADYYQGLWDC
HGDQPDELSF QRGDLIRILS KEYNMYGWWV GELNSIIGIV PKDYLTTAFE MEGR
