ID   MMS22_BOVIN             Reviewed;        1244 AA.
AC   E1BGH8;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Protein MMS22-like;
DE   AltName: Full=Methyl methanesulfonate-sensitivity protein 22-like;
GN   Name=MMS22L;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
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   -!- 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}.
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DR   EMBL; AAFC03054673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03056615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E1BGH8; -.
DR   STRING; 9913.ENSBTAP00000000830; -.
DR   CarbonylDB; E1BGH8; -.
DR   PaxDb; E1BGH8; -.
DR   PRIDE; E1BGH8; -.
DR   eggNOG; ENOG502QQCR; Eukaryota.
DR   HOGENOM; CLU_007143_0_0_1; -.
DR   InParanoid; E1BGH8; -.
DR   OrthoDB; 523276at2759; -.
DR   TreeFam; TF353832; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR   GO; GO:0090734; C:site of DNA damage; 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: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; PTHR28547; 1.
DR   Pfam; PF14911; MMS22L_C; 1.
DR   Pfam; PF14910; MMS22L_N; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator; Chromosome; DNA damage; DNA repair; DNA-binding;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..1244
FT                   /note="Protein MMS22-like"
FT                   /id="PRO_0000403771"
SQ   SEQUENCE   1244 AA;  142274 MW;  380A93AC2CF2B3CE CRC64;
     MDNCPPASTF LTDSLELELQ TEWCNPPCFS CDFDNRGGGK HFSGESYLSS GALKRVILNL
     DPLPTNFEED TVEIFGIEWV TETALVNSSR VLFHLFRQQL YNLETLLQAS CDFGKISTLH
     CKAHNIRQLC VTFLHYVKVF IFRSLQVRNA ESHVPVHPYE TLEAQLPSVL VDELHGLLLY
     IGHLSELPTT NTGAFVNQNQ TKLYPPSWHL LHLHLDIHWL VLEILHMLGE KLKQVVYSHQ
     FMNLAGDNLT NVSLFEEHCE NLLCDLINLS LNRYDKKVRP SEALMSHHCP CPCIKELWVL
     LIHLLNHRSK WSLSESFWNW LNKLLKTLLE KSNDQRRSVL IVQPRDPLGF SWWIITHVAS
     FYQFDRHGTP DEMRQMESNW NFVEELLKKS ISVQDGILEE QLRMYLHCCL TLCDFWEPNI
     AIVTILWEYY SKNLNSSFSI SWLPLKGLTY IIKSPLSMLE MVKTCCCDKQ DHDLYKSSSS
     YTIFLCILAK VVKKAMKNNG PHPWKQVKGR IYSKFHQKRM EELTEVGLQN FFSLFLLLAA
     VAEVEDVASH VLRLLDFLKP TFKTSPLIWK GQMAFLLMYT QKNLDIGVLA EKFSNAFREK
     AKEFLVSKND EMGQRQTLWT LLSIYMDSVQ EVFETSRCLH PSHEKLLNDG FSMLLRACQE
     SELRTVLNFL QAVLARIRSL HQQLRQELQR EHGDLSVQSS LSTKERHLAA VASALWRHFF
     SFLKSQRMSQ IVPLSQLADA AADFTLLAMD LPSTAPSDLQ PQPVTSMIQL FGWDDIIWPQ
     VVARYLSHFL QNSMLCEALS HSGCVSFQAL TVRSWIRCIL QMYVKNLHVP DDSFIDINPE
     QAVEKDYMEQ LTELTRLLFK LSEVKNIFSK SQVELPIPDD PKKALIRFFE AVGITYGNLQ
     TVSDKSAMVT KSLEYLGEIL KYIKPYLGKK VSSAGLQLTY TMMGTLVKSW ALIFATSKAQ
     KLLFRIIDCL LLPHTVLQQE KELPAPMLTA IQKSLPLYLQ GMCIVCCQSQ NTNAYLNQLL
     GNVIEQYIGR FLPASAHVLG LGQHPVLLAL KNSASVPPMS LLKKCIVHVI RKSYFEFKGS
     LLPPRLASIL AFILQLVKET NTDVSEIELL LPGVLKCLLL VSEPQVKRLA TENLQCMVRA
     CQVGSGGEPA AQLTSVFRQF IEDYGMRYDY QIYSILEAVA ALDQQVVIHL VPTLTQSLKN
     SERKWGLGRN SAQREAYSKL LSQLGQVGQD EIQRLENDHI ESML