ID   SWP70_BOVIN             Reviewed;         585 AA.
AC   P0C1G6;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Switch-associated protein 70;
DE            Short=SWAP-70;
GN   Name=SWAP70;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RT   "Bovine genome sequencing program: full-length cDNA sequencing.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 33-40; 448-457; 466-474; 482-490 AND 492-507,
RP   MUTAGENESIS OF ARG-230 AND LYS-291, DOMAIN, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Brain;
RX   PubMed=11961559; DOI=10.1038/416759a;
RA   Shinohara M., Terada Y., Iwamatsu A., Shinohara A., Mochizuki N.,
RA   Higuchi M., Gotoh Y., Ihara S., Nagata S., Itoh H., Fukui Y.,
RA   Jessberger R.;
RT   "SWAP-70 is a guanine-nucleotide-exchange factor that mediates signalling
RT   of membrane ruffling.";
RL   Nature 416:759-763(2002).
CC   -!- FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine
CC       nucleotide exchange factor (GEF) which, independently of RAS,
CC       transduces signals from tyrosine kinase receptors to RAC. It also
CC       mediates signaling of membrane ruffling. Regulates the actin
CC       cytoskeleton as an effector or adapter protein in response to agonist
CC       stimulated phosphatidylinositol (3,4)-bisphosphate production and cell
CC       protrusion (By similarity). {ECO:0000250, ECO:0000269|PubMed:11961559}.
CC   -!- SUBUNIT: The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}. Nucleus {ECO:0000250}. Cell projection, lamellipodium
CC       {ECO:0000250}. Note=In resting B-cells it is localized mainly in the
CC       cytoplasm and upon cell activation it is recruited to the plasma
CC       membrane and then translocates to the nucleus. In activated, class-
CC       switching B-cells it is associated with membrane IgG but not IgM.
CC       Localized to loose actin filament arrays located behind actively
CC       extending lamellipodia (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The PH domain is essential for phosphatidylinositol 3,4,5-
CC       trisphosphate binding. {ECO:0000269|PubMed:11961559}.
CC   -!- PTM: Tyrosine-phosphorylated. {ECO:0000250}.
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DR   EMBL; DV831848; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; DV869818; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; DV907929; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0C1G6; -.
DR   SMR; P0C1G6; -.
DR   STRING; 9913.ENSBTAP00000002578; -.
DR   PaxDb; P0C1G6; -.
DR   PRIDE; P0C1G6; -.
DR   eggNOG; ENOG502QSXX; Eukaryota.
DR   InParanoid; P0C1G6; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..585
FT                   /note="Switch-associated protein 70"
FT                   /id="PRO_0000240279"
FT   DOMAIN          210..306
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   COILED          316..532
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         230
FT                   /note="R->C: Abolishes binding to phosphatidylinositol
FT                   3,4,5-trisphosphate and blocks formation of membrane
FT                   ruffles."
FT                   /evidence="ECO:0000269|PubMed:11961559"
FT   MUTAGEN         291
FT                   /note="K->A: Abolishes binding to phosphatidylinositol
FT                   3,4,5-trisphosphate and blocks formation of membrane
FT                   ruffles."
FT                   /evidence="ECO:0000269|PubMed:11961559"
FT   CONFLICT        467
FT                   /note="W -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504
FT                   /note="Q -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   585 AA;  68921 MW;  246BCCC927455C02 CRC64;
     MGSLKDELLK GIWHAFTALD LDHSGKVSKS QLKVLSHNLC TVLKVPHDPV ALEEHFRDDD
     EGPVSNQGYM PYLNKFILEK VQDNFDKIEF NRMCWTLCVK KNLTKNPLFI TEEDAFKIWV
     IFNFLSEDKY PLIIVPEEIE YLLKKLTEAM GVSWQQEQFE NYKINFDDSK DGLSAWELIE
     LVGNGQFSKG MDRQTVSMAI NEVFNELILD VLKQGYMIKK GHRRKNWTER WFVLKPHIIS
     YYVSEDLKDK KGDILLDENC CVESLPDKDG KKCLFLIKCF DKTFEISASD KKKKQEWIQA
     IHSTIHLLKL GSPPPHKEAR QRRKELRKKL LAEQEELERQ MKELQIANEN KQQELEAVRK
     KLEEAASRAA EEEKKRLQTQ VELQARFSTE LEREKLIRQQ MEEQVAQKSS ELEQYLQRVR
     ELEDMYLKLQ EALEDERQAR QDEETVRKLQ ARLLEEESSK RAELEKWHLE QQQAIQTTEA
     EKQELENQRV IKEQALQEAL EQLQQLELER KQALEQYEGV KKKLEMAAKM TKSWKDKVAH
     HEGLIRLIEP GSKNAHLITN WGPAAFTQAE LEERQKSWKE KKTTE