ID   SWAP1_MOUSE             Reviewed;         278 AA.
AC   Q8VCI7; A7E2S1; Q8BRM3; Q9CV33;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=ATPase SWSAP1;
GN   Name=Swsap1;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Tongue;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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).
CC   -!- FUNCTION: ATPase which is preferentially stimulated by single-stranded
CC       DNA and is involved in homologous recombination repair (HRR). Has a
CC       DNA-binding activity which is independent of its ATPase activity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ZSWIM7; they form a functional complex involved
CC       in homologous recombination repair and stabilize each other. Interacts
CC       with RAD51, RAD51B, RAD51C, RAD51D and XRCC3; involved in homologous
CC       recombination repair (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26550.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK009864; BAB26550.1; ALT_INIT; mRNA.
DR   EMBL; AK043948; BAC31710.1; -; mRNA.
DR   EMBL; CJ185887; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC019749; AAH19749.1; -; mRNA.
DR   EMBL; BC150493; AAI50494.1; -; mRNA.
DR   CCDS; CCDS52739.1; -.
DR   RefSeq; NP_080146.1; NM_025870.1.
DR   AlphaFoldDB; Q8VCI7; -.
DR   STRING; 10090.ENSMUSP00000060331; -.
DR   iPTMnet; Q8VCI7; -.
DR   PhosphoSitePlus; Q8VCI7; -.
DR   EPD; Q8VCI7; -.
DR   jPOST; Q8VCI7; -.
DR   PaxDb; Q8VCI7; -.
DR   PRIDE; Q8VCI7; -.
DR   ProteomicsDB; 257107; -.
DR   Antibodypedia; 53827; 56 antibodies from 12 providers.
DR   Ensembl; ENSMUST00000053583; ENSMUSP00000060331; ENSMUSG00000051238.
DR   GeneID; 66962; -.
DR   KEGG; mmu:66962; -.
DR   UCSC; uc009onc.2; mouse.
DR   CTD; 126074; -.
DR   MGI; MGI:1914212; Swsap1.
DR   VEuPathDB; HostDB:ENSMUSG00000051238; -.
DR   eggNOG; ENOG502S62D; Eukaryota.
DR   GeneTree; ENSGT00390000007170; -.
DR   HOGENOM; CLU_099283_0_0_1; -.
DR   InParanoid; Q8VCI7; -.
DR   OMA; EMTITPW; -.
DR   OrthoDB; 1081973at2759; -.
DR   PhylomeDB; Q8VCI7; -.
DR   TreeFam; TF337313; -.
DR   BioGRID-ORCS; 66962; 5 hits in 109 CRISPR screens.
DR   ChiTaRS; Swsap1; mouse.
DR   PRO; PR:Q8VCI7; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8VCI7; protein.
DR   Bgee; ENSMUSG00000051238; Expressed in retinal neural layer and 211 other tissues.
DR   Genevisible; Q8VCI7; MM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0097196; C:Shu complex; ISO:MGI.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..278
FT                   /note="ATPase SWSAP1"
FT                   /id="PRO_0000294241"
FT   REGION          237..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        263
FT                   /note="P -> S (in Ref. 1; BAB26550)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  29385 MW;  7AEBA2DB68CEC6E4 CRC64;
     MAEALRRVLN AGCAARPGED GAAGPPLLLL GAPRSAQTSL LFAAALEAAG EGRGSVLFVT
     RRPLQSLPLS TPTAREHWRL QKVRFQYPSS IQELLQLLAS AHEAPAPTPS LLLLDGLEEY
     LAEDPSAQEA AYLAALLLDT AAFFSHRLGA NGSCGLVVAL ETQKEAEADA PHLPLLKRYF
     PAQCWLQPDA LGLGQHCCLR ASLELGKLSP RTEWSVSFLP CGEMKVTPWL AQASKLSPEK
     KDSSAGSQSL TLGCDNLPGP GSPLDGILTS ETGADSKT