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   03-AUG-2022, entry version 96.
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; Q6DII7; -.
DR   DNASU; 448448; -.
DR   GeneID; 448448; -.
DR   KEGG; xtr:448448; -.
DR   CTD; 8631; -.
DR   Xenbase; XB-GENE-490220; skap1.
DR   eggNOG; ENOG502QSSU; Eukaryota.
DR   InParanoid; Q6DII7; -.
DR   OrthoDB; 767446at2759; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
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; 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   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