ID SKAP1_XENTR Reviewed; 345 AA.
AC Q6DII7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Src kinase-associated phosphoprotein 1;
GN Name=skap1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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; BC075553; AAH75553.1; -; mRNA.
DR RefSeq; NP_001004990.1; NM_001004990.1.
DR AlphaFoldDB; Q6DII7; -.
DR SMR; Q6DII7; -.
DR STRING; 8364.ENSXETP00000050746; -.
DR PaxDb; 8364-ENSXETP00000057091; -.
DR DNASU; 448448; -.
DR GeneID; 448448; -.
DR KEGG; xtr:448448; -.
DR AGR; Xenbase:XB-GENE-490220; -.
DR CTD; 8631; -.
DR Xenbase; XB-GENE-490220; skap1.
DR eggNOG; ENOG502QSSU; Eukaryota.
DR InParanoid; Q6DII7; -.
DR OrthoDB; 2968233at2759; -.
DR Proteomes; UP000008143; Chromosome 10.
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; cd13380; PH_Skap1; 1.
DR Gene3D; 6.10.250.220; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR037781; SKAP_fam.
DR PANTHER; PTHR15129:SF1; SRC KINASE-ASSOCIATED PHOSPHOPROTEIN 1; 1.
DR PANTHER; PTHR15129; SRC-ASSOCIATED ADAPTOR PROTEIN; 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; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Cytoplasm; Immunity; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..345
FT /note="Src kinase-associated phosphoprotein 1"
FT /id="PRO_0000270177"
FT DOMAIN 109..212
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 283..344
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 226..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 39737 MW; 8019B387EA7B996F CRC64;
MQGYDIPRDV ISLLKDAETY LAECLQNEKL SGRAREQRDE ILHSFGQIRN RYGVEFALKG
GEAAFTHTGQ DDYDDIHNAS YAPSQASDEV SVASDYVEND SEVEEELDKI FKQGYLERRK
KDHGFFGSEW QKRWCVLTTR AFLYYSSEKG KQPKNGFLIK DSLAQMMPYI RKDSRRDSCF
EVVTPNQQVF QFTAASPSDA RDWVEQIQFL VKDTQSTIIP YEDDEETYDD IESTESSPVV
GLTNDSENSL QEDDVYESIP GDEETEESED ENYEMKPGEP VIFYGDYYQG LWNCFSDNSD
ELSFERGDLI HILSKEYHAY GWWVGELDGI VGIVPKDYLT LAFDL
//
