ID   SKAP2_TAKRU             Reviewed;         329 AA.
AC   Q1KKZ1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Src kinase-associated phosphoprotein 2;
DE   AltName: Full=Src family-associated phosphoprotein 2;
GN   Name=skap2; Synonyms=scap2;
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: May be involved in B-cell and macrophage adhesion processes.
CC       May play a role in src signaling pathway (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosines. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SKAP family. {ECO:0000305}.
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DR   EMBL; DQ481664; ABF22403.1; -; Genomic_DNA.
DR   RefSeq; XP_011604031.1; XM_011605729.1.
DR   AlphaFoldDB; Q1KKZ1; -.
DR   SMR; Q1KKZ1; -.
DR   GeneID; 101062242; -.
DR   CTD; 8935; -.
DR   InParanoid; Q1KKZ1; -.
DR   OrthoDB; 767446at2759; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042113; P:B cell activation; 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   3: Inferred from homology;
KW   B-cell activation; Cytoplasm; Phosphoprotein; Reference proteome;
KW   SH3 domain.
FT   CHAIN           1..329
FT                   /note="Src kinase-associated phosphoprotein 2"
FT                   /id="PRO_0000270184"
FT   DOMAIN          104..207
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          267..328
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          58..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..258
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  37940 MW;  A4FDAB5B78C68BDC CRC64;
     MLPIPEELTT LISDLELYLA DGLKGENLSK KAKEKREAFI KRIKEVKLSF PQDFKDKYAE
     DSEEEEDWDS NEGGSLQSER TDKDEEACEG AQQAPAVAAQ DLTSVFKAGY LEKRRKDHSF
     FGTEWQKRWC ALSGQTFYYY GSEKDKQQKG EFNIEGYRVK MNSSLRKDSK KDFCFEISAT
     DKRSYMFCAS SVKEAEEWVK QIDFVLKDMT GIIPEEEEEG QELYDDVGQM DEIYEVLPEE
     DMPSPPPKVE PVSKHPPPTP AVDKSTDYAN YYQGLWDCMG DLPDELSFKR GDAIYILSRE
     YQTFGWWVGE KNGQIGIVPK DYLMELYAL