SKAP1_TAKRU
ID SKAP1_TAKRU Reviewed; 363 AA.
AC Q1KKW7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Src kinase-associated phosphoprotein 1;
DE AltName: Full=Src family-associated phosphoprotein 1;
GN Name=skap1; Synonyms=scap1;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16636282; DOI=10.1073/pnas.0601492103;
RA Lee A.P., Koh E.G.L., Tay A., Brenner S., Venkatesh B.;
RT "Highly conserved syntenic blocks at the vertebrate Hox loci and conserved
RT regulatory elements within and outside Hox gene clusters.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6994-6999(2006).
CC -!- FUNCTION: Positively regulates T-cell receptor signaling. Required for
CC optimal conjugation between T-cells and antigen-presenting cells (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cell membrane {ECO:0000250}. Note=Upon T-cell stimulation, translocates
CC to lipid rafts at the cell membrane. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosines. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SKAP family. {ECO:0000305}.
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DR EMBL; DQ481666; ABF22427.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1KKW7; -.
DR SMR; Q1KKW7; -.
DR STRING; 31033.ENSTRUP00000030563; -.
DR eggNOG; ENOG502QSSU; Eukaryota.
DR HOGENOM; CLU_062032_0_0_1; -.
DR InParanoid; Q1KKW7; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
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; PF14604; SH3_9; 1.
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 3: Inferred from homology;
KW Adaptive immunity; Cell membrane; Cytoplasm; Immunity; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..363
FT /note="Src kinase-associated phosphoprotein 1"
FT /id="PRO_0000270176"
FT DOMAIN 118..221
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 301..362
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 62..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..247
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 41279 MW; 4BFE711B49E12301 CRC64;
MEAVDLLANV SVTGLLLFWG DCEFFVSEIL YDENLSENAQ ETRKVLLNNF RVVHVRNPQE
FPFPSDYKEE DGSDDNRSSS LGRSAQSDDA SLASDNQDDG IPEYFGDIPP VAAQDIVNVL
KQGYLEKKRK DHSFFGSEWQ KRWCVLNNLV FYYFGSDKDK QQKGSFYISD YSVQLVTNLR
KDSRKTSCFE FFAPGRRPFQ FTAGSPQEAK EWVDQIKIVL RDLSSTVIPV DDEEEEEEEE
ETYDDIEGEG GPPLPQPLSG TWGRGGDTGA ADEEDEDIYE VLPEESPDSA DGSMERNNKP
EYANYYQGLW DCSADEPDEL PFQRGDLIYI ISKEYNIYGW WVGELNGAVG IVPKDFLHPA
YIL