SFR1_MOUSE
ID SFR1_MOUSE Reviewed; 319 AA.
AC Q8BP27; Q3TH62; Q3TI03; Q3TJK0; Q3UIQ6; Q8R3W0; Q9CRT7; Q9D0D7; Q9D116;
AC Q9D4W4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Swi5-dependent recombination DNA repair protein 1 homolog;
DE AltName: Full=Meiosis protein 5 homolog;
GN Name=Sfr1; Synonyms=Mei5, Meir5;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Amnion, Forelimb, Head, Medulla oblongata, Placenta, Stomach, and
RC Testis;
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] (ISOFORM 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-83 AND SER-99, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-71; SER-83; SER-87;
RP SER-99 AND SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-71; SER-83; SER-87;
RP SER-99 AND SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-71; SER-83; SER-87;
RP SER-99; SER-103 AND SER-143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC 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).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE SWI5-SFR1 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20976249; DOI=10.1371/journal.pgen.1001160;
RA Akamatsu Y., Jasin M.;
RT "Role for the mammalian Swi5-Sfr1 complex in DNA strand break repair
RT through homologous recombination.";
RL PLoS Genet. 6:E1001160-E1001160(2010).
CC -!- FUNCTION: Component of the SWI5-SFR1 complex, a complex required for
CC double-strand break repair via homologous recombination
CC (PubMed:20976249). Acts as a transcriptional modulator for ESR1.
CC {ECO:0000250|UniProtKB:Q86XK3, ECO:0000269|PubMed:20976249}.
CC -!- SUBUNIT: Component of the SWI5-SFR1 complex (PubMed:20976249).
CC Interacts with RAD51; the interaction is weak (By similarity).
CC {ECO:0000250|UniProtKB:Q86XK3, ECO:0000269|PubMed:20976249}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20976249}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BP27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BP27-2; Sequence=VSP_040905;
CC Name=3;
CC IsoId=Q8BP27-3; Sequence=VSP_040906, VSP_040907;
CC -!- SIMILARITY: Belongs to the SFR1/MEI5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23154.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004073; BAB23154.1; ALT_FRAME; mRNA.
DR EMBL; AK011531; BAB27680.1; -; mRNA.
DR EMBL; AK014266; BAB29232.1; -; mRNA.
DR EMBL; AK016079; BAB30105.1; -; mRNA.
DR EMBL; AK077875; BAC37045.1; -; mRNA.
DR EMBL; AK078147; BAC37148.1; -; mRNA.
DR EMBL; AK146810; BAE27450.1; -; mRNA.
DR EMBL; AK167406; BAE39495.1; -; mRNA.
DR EMBL; AK168068; BAE40043.1; -; mRNA.
DR EMBL; AK168427; BAE40336.1; -; mRNA.
DR EMBL; BC024403; AAH24403.1; -; mRNA.
DR CCDS; CCDS38019.1; -. [Q8BP27-1]
DR RefSeq; NP_080653.2; NM_026377.2. [Q8BP27-1]
DR AlphaFoldDB; Q8BP27; -.
DR SMR; Q8BP27; -.
DR BioGRID; 212442; 3.
DR STRING; 10090.ENSMUSP00000096954; -.
DR iPTMnet; Q8BP27; -.
DR PhosphoSitePlus; Q8BP27; -.
DR EPD; Q8BP27; -.
DR jPOST; Q8BP27; -.
DR MaxQB; Q8BP27; -.
DR PaxDb; Q8BP27; -.
DR PeptideAtlas; Q8BP27; -.
DR PRIDE; Q8BP27; -.
DR ProteomicsDB; 255396; -. [Q8BP27-1]
DR ProteomicsDB; 255397; -. [Q8BP27-2]
DR ProteomicsDB; 255398; -. [Q8BP27-3]
DR Antibodypedia; 48828; 90 antibodies from 13 providers.
DR DNASU; 67788; -.
DR Ensembl; ENSMUST00000099353; ENSMUSP00000096954; ENSMUSG00000025066. [Q8BP27-1]
DR GeneID; 67788; -.
DR KEGG; mmu:67788; -.
DR UCSC; uc008hvk.1; mouse. [Q8BP27-1]
DR CTD; 119392; -.
DR MGI; MGI:1915038; Sfr1.
DR VEuPathDB; HostDB:ENSMUSG00000025066; -.
DR eggNOG; ENOG502S1QX; Eukaryota.
DR GeneTree; ENSGT00390000018550; -.
DR HOGENOM; CLU_075586_1_0_1; -.
DR InParanoid; Q8BP27; -.
DR OMA; QPRENPP; -.
DR OrthoDB; 1628702at2759; -.
DR PhylomeDB; Q8BP27; -.
DR TreeFam; TF332725; -.
DR BioGRID-ORCS; 67788; 8 hits in 109 CRISPR screens.
DR ChiTaRS; Sfr1; mouse.
DR PRO; PR:Q8BP27; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BP27; protein.
DR Bgee; ENSMUSG00000025066; Expressed in primary oocyte and 262 other tissues.
DR Genevisible; Q8BP27; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032798; C:Swi5-Sfr1 complex; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; ISO:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR042429; SFR1.
DR InterPro; IPR018468; SFR1/Mei5.
DR PANTHER; PTHR28643; PTHR28643; 1.
DR Pfam; PF10376; Mei5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..319
FT /note="Swi5-dependent recombination DNA repair protein 1
FT homolog"
FT /id="PRO_0000089806"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 220..270
FT /evidence="ECO:0000255"
FT COMPBIAS 8..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..114
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XK3"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 47..62
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_040905"
FT VAR_SEQ 62..77
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040906"
FT VAR_SEQ 140..207
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040907"
FT CONFLICT 137
FT /note="A -> S (in Ref. 1; BAC37045)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="E -> D (in Ref. 1; BAE39495)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="P -> Q (in Ref. 1; BAE40043)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="E -> K (in Ref. 1; BAE40043)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="K -> R (in Ref. 1; BAB27680)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="H -> R (in Ref. 1; BAE39495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 35183 MW; 14F1B9FCF269455B CRC64;
MAEEGNQEFT SKMENSSDSA STSPDAPQPS ENPPSPPTSP AAPQTSENPP SPPTSPAVPQ
TRENPPSPPT SPAAPQPREN PPSPPTSPAA PQPRENPPSP PTSPAAPQPR ENPPSPHSNS
SGKQPLSGTP KERLKKARSS SHSFCSVVKR MKVENDENNE TLSEPGESSK EENCSKAQES
LKNKDSEPGE KSSEEKNTCE SKSSDTGSSN ALPKESENAI IREKLKQEKI RLIRQVEEKE
DLLRRLKLVK MYRIKNDVTE LENLIKKWRK CGQRLLCELQ SIMSEDEDEK LTLTELIDFY
GIDDNLLHYN RSEEEFTGV
