SWP70_MOUSE
ID SWP70_MOUSE Reviewed; 585 AA.
AC Q6A028; O88443; Q3TQR6; Q3UCA3; Q6P1D0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Switch-associated protein 70;
DE Short=SWAP-70;
GN Name=Swap70; Synonyms=Kiaa0640;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-24, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=9642267; DOI=10.1074/jbc.273.27.17025;
RA Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.;
RT "A B-cell-specific DNA recombination complex.";
RL J. Biol. Chem. 273:17025-17035(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10382743;
RX DOI=10.1002/(sici)1521-4141(199906)29:06<1812::aid-immu1812>3.0.co;2-j;
RA Borggrefe T., Masat L., Wabl M., Riwar B., Cattoretti G., Jessberger R.;
RT "Cellular, intracellular, and developmental expression patterns of murine
RT SWAP-70.";
RL Eur. J. Immunol. 29:1812-1822(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000269|PubMed:9642267}.
CC -!- INTERACTION:
CC Q6A028; Q61738-6: Itga7; NbExp=2; IntAct=EBI-2121215, EBI-1786329;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10382743}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9UH65}. Nucleus
CC {ECO:0000269|PubMed:10382743, ECO:0000269|PubMed:9642267}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:Q9UH65}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q9UH65}. Note=Localizes
CC predominantly to the nucleus in activated cells. Only a small amount
CC can be detected in the cytoplasm. {ECO:0000269|PubMed:10382743}.
CC -!- TISSUE SPECIFICITY: Spleen. Expressed only in B-cells that have been
CC induced to switch to various Ig isotypes. {ECO:0000269|PubMed:10382743,
CC ECO:0000269|PubMed:9642267}.
CC -!- DEVELOPMENTAL STAGE: Not detected in the spleen of 1-week old mice.
CC Detected from 2-weeks onwards and thereafter levels increase and then
CC from 12-weeks onwards levels decline. {ECO:0000269|PubMed:10382743}.
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=BAD32268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF053974; AAC40155.1; -; mRNA.
DR EMBL; AK172990; BAD32268.1; ALT_INIT; mRNA.
DR EMBL; AK146773; BAE27422.1; -; mRNA.
DR EMBL; AK150621; BAE29711.1; -; mRNA.
DR EMBL; AK163357; BAE37316.1; -; mRNA.
DR EMBL; BC065136; AAH65136.1; -; mRNA.
DR CCDS; CCDS21744.1; -.
DR RefSeq; NP_033328.3; NM_009302.3.
DR AlphaFoldDB; Q6A028; -.
DR SMR; Q6A028; -.
DR BioGRID; 203593; 10.
DR CORUM; Q6A028; -.
DR IntAct; Q6A028; 1.
DR STRING; 10090.ENSMUSP00000033325; -.
DR iPTMnet; Q6A028; -.
DR PhosphoSitePlus; Q6A028; -.
DR SwissPalm; Q6A028; -.
DR EPD; Q6A028; -.
DR MaxQB; Q6A028; -.
DR PaxDb; Q6A028; -.
DR PeptideAtlas; Q6A028; -.
DR PRIDE; Q6A028; -.
DR ProteomicsDB; 254701; -.
DR Antibodypedia; 1856; 412 antibodies from 36 providers.
DR DNASU; 20947; -.
DR Ensembl; ENSMUST00000033325; ENSMUSP00000033325; ENSMUSG00000031015.
DR GeneID; 20947; -.
DR KEGG; mmu:20947; -.
DR UCSC; uc009jfb.2; mouse.
DR CTD; 23075; -.
DR MGI; MGI:1298390; Swap70.
DR VEuPathDB; HostDB:ENSMUSG00000031015; -.
DR eggNOG; ENOG502QSXX; Eukaryota.
DR GeneTree; ENSGT00950000183017; -.
DR HOGENOM; CLU_029358_1_0_1; -.
DR InParanoid; Q6A028; -.
DR OMA; DYKVNFD; -.
DR OrthoDB; 1185498at2759; -.
DR PhylomeDB; Q6A028; -.
DR TreeFam; TF333160; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 20947; 3 hits in 110 CRISPR screens.
DR ChiTaRS; Swap70; mouse.
DR PRO; PR:Q6A028; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6A028; protein.
DR Bgee; ENSMUSG00000031015; Expressed in peripheral lymph node and 216 other tissues.
DR Genevisible; Q6A028; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:CACAO.
DR GO; GO:0045190; P:isotype switching; IDA:MGI.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:CACAO.
DR GO; GO:0033633; P:negative regulation of cell-cell adhesion mediated by integrin; IMP:CACAO.
DR GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; IMP:CACAO.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IMP:CACAO.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:CACAO.
DR GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IMP:CACAO.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:CACAO.
DR GO; GO:0032880; P:regulation of protein localization; IMP:CACAO.
DR GO; GO:0016444; P:somatic cell DNA recombination; IDA:MGI.
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; Cytoskeleton;
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_0000240281"
FT DOMAIN 210..306
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 347..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 316..529
FT /evidence="ECO:0000255"
FT COMPBIAS 353..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2
FT /note="R -> G (in Ref. 2; BAD32268)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="I -> V (in Ref. 2; BAD32268)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="G -> R (in Ref. 4; AAH65136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 68996 MW; 3FFD1B671976782C CRC64;
MRGLKDELLK AIWHAFTALD LDRSGKVSKS QLKVLSHNLC TVLKVPHDPV ALEEHFRDDD
EGPVSNQGYM PYLNKFILEK VQDNFDKIEF NRMCWTLCVK KNLTKSPLLI TEDDAFKVWV
IFNFLSEDKY PLIIVPEEIE YLLKKLTEAM GGGWQQEQFE HYKINFDDNK DGLSAWELIE
LIGNGQFSKG MDRQTVSMAI NEVFNELILD VLKQGYMMKK GHKRKNWTER WFVLKPNIIS
YYVSEDLKDK KGDILLDENC CVESLPDKDG KKCLFLIKCF DKTFEISASD KKKKQEWIQA
IYSTIHLLKL GSPPPHKEAR QRRKELRRKL LAEQEELERQ MKELQAANEN KQQELESVRK
KLEEAASRAA DEEKKRLQTQ VELQTRFSTE LEREKLIRQQ MEEQVAQKSS ELEQYLQRVR
ELEDMYLKLQ EALEDERQAR QDEETVRKLQ ARLLEEESSK RAELEKWHLE QQQAIQTTEA
EKQELEQQRV MKEQALQEAM AQLEQLELER KQALEQYEGV KKKLEMATHM TKSWKDKVAH
HEGLIRLIEP GSKNPHLITN WGPAAFTQAE LEEREKSWKE KKTTE
