ID   SWP70_CHICK             Reviewed;         586 AA.
AC   Q5F4B2; Q5ZL29;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Switch-associated protein 70;
DE            Short=SWAP-70;
GN   Name=SWAP70; ORFNames=RCJMB04_1e1, RCJMB04_8b3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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}.
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:0000250}.
CC   -!- PTM: Tyrosine-phosphorylated. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG31564.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ719905; CAG31564.1; ALT_FRAME; mRNA.
DR   EMBL; AJ851388; CAH65022.1; -; mRNA.
DR   RefSeq; NP_001026351.1; NM_001031180.1.
DR   AlphaFoldDB; Q5F4B2; -.
DR   SMR; Q5F4B2; -.
DR   STRING; 9031.ENSGALP00000009219; -.
DR   PaxDb; Q5F4B2; -.
DR   GeneID; 423044; -.
DR   KEGG; gga:423044; -.
DR   CTD; 23075; -.
DR   VEuPathDB; HostDB:geneid_423044; -.
DR   eggNOG; ENOG502QSXX; Eukaryota.
DR   InParanoid; Q5F4B2; -.
DR   OrthoDB; 1185498at2759; -.
DR   PhylomeDB; Q5F4B2; -.
DR   PRO; PR:Q5F4B2; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Coiled coil; Cytoplasm; DNA-binding;
KW   Membrane; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..586
FT                   /note="Switch-associated protein 70"
FT                   /id="PRO_0000240282"
FT   DOMAIN          210..306
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   COILED          316..538
FT                   /evidence="ECO:0000255"
FT   CONFLICT        139
FT                   /note="V -> I (in Ref. 1; CAG31564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264
FT                   /note="P -> R (in Ref. 1; CAG31564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   586 AA;  68411 MW;  920CD078E586DA37 CRC64;
     MVGLKEELLK AIWHAFTALD LDRSGKVSKS QLKVLSHNLC TVLNVPHDPV ALEEHFRDDD
     EGPVSNQGYM PYLNKFILEK VQGNFDKVEF NRMCWTLCAK KNLSKSPLLI SDEDAFKVWV
     IFNFLSEDKY PLIIVPEEVE YLLKKLTEAM GAGWQQEQFD LYKIALNTSR EGLSAWELID
     LIGSGQFSKG MDRQTVSMAI NEVFNELILD VLKQGYMLKK GHKRKNWTER WFVLKPNIIS
     YYVSEDLKDK KGDIILDGNC CVEPLPDKDG KKCLFLIKCL DKSFEISASD KKKKQEWIQA
     IQTTVSLLRA GSPPPHKEAR QKRKELRQKL LAEQEELERQ MKELQTANEN KQKELETVRK
     QLEAAAARAA EEEKKRLQTQ VELQDRFSLE LEREKMVRQK MEEQVAQKSS ELEQYLQRVR
     ELEEMYKQLQ EALEVEKQAR QDEETVRKLQ ARLLEEESAK RAELEKWHLQ QQQTIQMTEA
     EKQELENQRM IKEQALQVAM QQLEQLELER KEALEQYEEV KKKLETAANN TRSWKDKVAH
     HEGLIRLIEP GSKNPHLITN WGPAAFTEAE LEQRQKSWKG KKASSE