ID MMS22_MOUSE Reviewed; 1238 AA. AC B1AUR6; B7ZN61; D3YXA0; Q6R5F9; Q80UT0; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 24-JAN-2024, entry version 95. DE RecName: Full=Protein MMS22-like; DE AltName: Full=Methyl methanesulfonate-sensitivity protein 22-like; GN Name=Mms22l; 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] (ISOFORM 2). RC STRAIN=CD-1; RX PubMed=14691545; DOI=10.1371/journal.pbio.0000074; RA Sharov A.A., Piao Y., Matoba R., Dudekula D.B., Qian Y., VanBuren V., RA Falco G., Martin P.R., Stagg C.A., Bassey U.C., Wang Y., Carter M.G., RA Hamatani T., Aiba K., Akutsu H., Sharova L., Tanaka T.S., Kimber W.L., RA Yoshikawa T., Jaradat S.A., Pantano S., Nagaraja R., Boheler K.R., Taub D., RA Hodes R.J., Longo D.L., Schlessinger D., Keller J., Klotz E., Kelsoe G., RA Umezawa A., Vescovi A.L., Rossant J., Kunath T., Hogan B.L.M., Curci A., RA D'Urso M., Kelso J., Hide W., Ko M.S.H.; RT "Transcriptome analysis of mouse stem cells and early embryos."; RL PLoS Biol. 1:410-419(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 216-1238. RC STRAIN=129; TISSUE=Brain, and Mammary tumor; 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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: Component of the MMS22L-TONSL complex, a complex that CC promotes homologous recombination-mediated repair of double-strand CC breaks (DSBs) at stalled or collapsed replication forks. The MMS22L- CC TONSL complex is required to maintain genome integrity during DNA CC replication. It mediates the assembly of RAD51 filaments on single- CC stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs CC following histone replacement by histone chaperones and eviction of the CC replication protein A complex (RPA/RP-A) from DSBs. Following CC recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of CC RAD51 filaments and subsequent homologous recombination. Within the CC complex, MMS22L acts by binding ssDNA. {ECO:0000250|UniProtKB:Q6ZRQ5}. CC -!- SUBUNIT: Component of the MMS22L-TONSL complex, a complex at least CC composed of MMS22L and TONSL/NFKBIL2. Interacts with RAD51; interaction CC is direct. {ECO:0000250|UniProtKB:Q6ZRQ5}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6ZRQ5}. CC Chromosome {ECO:0000250|UniProtKB:Q6ZRQ5}. Note=Localizes to DNA damage CC sites, accumulates at stressed replication forks. Recruited to stalled CC or collapsed replication forks; directly binds replication protein A CC complex (RPA/RP-A)-coated single-stranded DNA (ssDNA). CC {ECO:0000250|UniProtKB:Q6ZRQ5}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=B1AUR6-1; Sequence=Displayed; CC Name=2; CC IsoId=B1AUR6-2; Sequence=VSP_040445, VSP_040446; CC -!- PTM: Degraded by the ubiquitin-proteasome system upon replication CC stress. {ECO:0000250|UniProtKB:Q6ZRQ5}. CC -!- SIMILARITY: Belongs to the MMS22 family. MMS22L subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI37911.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI45029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY512923; AAR87794.1; -; mRNA. DR EMBL; AL671913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX296536; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC051674; AAH51674.1; -; mRNA. DR EMBL; BC137910; AAI37911.1; ALT_INIT; mRNA. DR EMBL; BC145028; AAI45029.1; ALT_INIT; mRNA. DR CCDS; CCDS18006.2; -. [B1AUR6-1] DR RefSeq; NP_955761.2; NM_199467.2. [B1AUR6-1] DR AlphaFoldDB; B1AUR6; -. DR BioGRID; 229314; 4. DR STRING; 10090.ENSMUSP00000103857; -. DR iPTMnet; B1AUR6; -. DR PhosphoSitePlus; B1AUR6; -. DR EPD; B1AUR6; -. DR MaxQB; B1AUR6; -. DR PaxDb; 10090-ENSMUSP00000103857; -. DR PeptideAtlas; B1AUR6; -. DR ProteomicsDB; 295570; -. [B1AUR6-1] DR ProteomicsDB; 295571; -. [B1AUR6-2] DR Pumba; B1AUR6; -. DR Antibodypedia; 55212; 24 antibodies from 8 providers. DR DNASU; 212377; -. DR Ensembl; ENSMUST00000108222.9; ENSMUSP00000103857.3; ENSMUSG00000045751.17. [B1AUR6-1] DR GeneID; 212377; -. DR KEGG; mmu:212377; -. DR UCSC; uc008sdv.2; mouse. [B1AUR6-1] DR UCSC; uc008sdy.1; mouse. [B1AUR6-2] DR AGR; MGI:2684980; -. DR CTD; 253714; -. DR MGI; MGI:2684980; Mms22l. DR VEuPathDB; HostDB:ENSMUSG00000045751; -. DR eggNOG; ENOG502QQCR; Eukaryota. DR GeneTree; ENSGT00390000011769; -. DR InParanoid; B1AUR6; -. DR OMA; RVYLCLL; -. DR OrthoDB; 3109168at2759; -. DR PhylomeDB; B1AUR6; -. DR TreeFam; TF353832; -. DR BioGRID-ORCS; 212377; 35 hits in 119 CRISPR screens. DR ChiTaRS; Mms22l; mouse. DR PRO; PR:B1AUR6; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; B1AUR6; Protein. DR Bgee; ENSMUSG00000045751; Expressed in ventricular zone and 146 other cell types or tissues. DR ExpressionAtlas; B1AUR6; baseline and differential. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0035101; C:FACT complex; IEA:Ensembl. DR GO; GO:0042555; C:MCM complex; IEA:Ensembl. DR GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB. DR GO; GO:0035861; C:site of double-strand break; ISO:MGI. DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB. DR GO; GO:0071168; P:protein localization to chromatin; ISO:MGI. DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB. DR InterPro; IPR042320; MMS22-like. DR InterPro; IPR029424; MMS22L_C. DR InterPro; IPR029425; MMS22L_N. DR PANTHER; PTHR28547; PROTEIN MMS22-LIKE; 1. DR PANTHER; PTHR28547:SF1; PROTEIN MMS22-LIKE; 1. DR Pfam; PF14911; MMS22L_C; 1. DR Pfam; PF14910; MMS22L_N; 1. DR Genevisible; B1AUR6; MM. PE 1: Evidence at protein level; KW Alternative splicing; Chromatin regulator; Chromosome; DNA damage; KW DNA repair; DNA-binding; Nucleus; Reference proteome. FT CHAIN 1..1238 FT /note="Protein MMS22-like" FT /id="PRO_0000403772" FT VAR_SEQ 1..276 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14691545" FT /id="VSP_040445" FT VAR_SEQ 793 FT /note="N -> NS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14691545" FT /id="VSP_040446" SQ SEQUENCE 1238 AA; 140582 MW; 9C2733D598CF2F2D CRC64; MDGCSAASTF LTDSLELELG TEWCKPPCFS CAFDNREGKF SGESYLASGA LKRLILNLDP LPTNFEEDTV ELFGFQWVTE TALVYSCREL FHLFRQQIFN LESLVQVSCD FGKIATLHAK ADSIRQQCVV FLHYIKVFIF RCLKVQEAES HSRPAHPYEA LEAQLPSMLV DELRGLLLYI GHLAALPSVT VGAFVNQNQM KLFPPSWHLL HLYLDTHWLV LEILHILGEK LKQVVYGRQF IGQAGDNLTN VSLFEEHCEH LFCDLICLSL NRFDKVMPSE ALLISHCPCS CVKELWVLLI HLLDHRRKWS VADSFWNWLN KLLRTLFEKS SDQRRSSVSL TQAKDPLGFS WWISVHVASL YQIDRHGVSD KMKQMESNWS FIEELLKRSV TVQDSILEEQ LRMHLHCCLT LCDFWEPNIS VVTILWEYYS KNLNSSFSIS WLPLKGLTNI IKSPLSMLTL VRNCCSDKQD PDLYKSSSSY IIFLCILAKV VKKAMRTSGP HPWKQVKGRI YSKFHQKRME ELTEVGLQNF FSLFLLLAAV AEIEDVASHV LDLLRFLRPA SMSSHGALVW KGQMAFLLMY AQKNLDIGVW AEKLSCEFQE KAKEFLVSKN DEMVQRHALW TLLCIYIDGV QEVFETSSCL YPSHEHLLND GFSMLLPACR ESELRTVLNF LQAVLARIRS VHQQLCQELQ RENVDLTVQS SLSAKERPLA AVAGALWRHF FSFLKSQRMT QVVPLSQLAD AAADFTLLAV DMPNTAPPDL QPQPVISIIQ LFGWDDIIWP QVVARYLSHL LQNSTVYEAL SQSSCVSSQS LTIRSWVRCV LQMHIKHLSD PDLLIDVNPE QAVEKEYMEQ LAEMTRLLFT LSEVKSVFSK AQIEQLPSPD DPKQALIQFL EAVGVTYRTL QTFSDKSAMV TKSLEYLGEV LKYIKPYLGK KVSSAGLQLT YGIMGILVKS WAHIFATSKA QKLLFRIIDC LLLPHTVLQQ DKELPGPMLT AIQKTLPLYL QGICIVCCQS QNPNAYLNQL LRNVIEQYIG RFLPTSPCVS DLGQHPVLLA LRNPASVPSM TPLRKHTVHA IRKSYLEFKG SSPPPRLASV LAFVLQLFKD TEMGACDLEL LLPGILKCLV LVNEPQVKKL ATENLQCMVQ TCQVGSEGGP ATQLTSLFRQ FIQDYGMQYS YQVYSILETV ATLNQHVVIQ LIPTLTQSLK DSELKWGLGR NIAQREAYSR LLSGLGQVGQ GEKQRLEK //