MMS22_CHICK
ID MMS22_CHICK Reviewed; 1243 AA.
AC E1C2Z0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Protein MMS22-like;
DE AltName: Full=Methyl methanesulfonate-sensitivity protein 22-like;
GN Name=MMS22L;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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.
CC {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.
CC {ECO:0000250|UniProtKB:Q6ZRQ5}.
CC -!- SIMILARITY: Belongs to the MMS22 family. MMS22L subfamily.
CC {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; AADN02002275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1C2Z0; -.
DR STRING; 9031.ENSGALP00000024966; -.
DR PaxDb; E1C2Z0; -.
DR VEuPathDB; HostDB:geneid_421799; -.
DR eggNOG; ENOG502QQCR; Eukaryota.
DR InParanoid; E1C2Z0; -.
DR PhylomeDB; E1C2Z0; -.
DR TreeFam; TF353832; -.
DR Proteomes; UP000000539; 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..1243
FT /note="Protein MMS22-like"
FT /id="PRO_0000403773"
SQ SEQUENCE 1243 AA; 140908 MW; 88AD93ED0DE1AF56 CRC64;
MDSFTPPLLS DSLQMAMEVE NEKSNPPCFS CIFDNQNGGR SFSGESYLAS GSLKRVLLRL
DPSPNDYEED AIEMFGFQWV TETALVESCG LLFGLLRQQI YKLEDLIEMN SSDFGKAANL
HSEAENIRRL CINFLHYVKV FIFRYLEPPK TENDGVLHPY EELEAQFPSL LVEELHSLTL
HIGHLCELPS NVLAAFTIQH QAKIFPPSWH LLHLHLDIHW LVLEILHVLS EKMMRQVVYA
NHFINLTGEN LTNISLFETH CENLISDLIS LSIQKYTKVR PSEALTSHHY PCNCIKELWI
LLIQLLGFRN KGSQTECFWS LVNKKLKSIF ERPTSSESVS VFGTTQCKDP LSFSLWIVTH
LASLYQFDRN GNLEEKKQKE SNWKFVEELL KNSIGAQTGV LEEHLRMHLQ CCLTLCRFWD
WNLSVITILW DYYSKNLNSC FTVPWLGLKG LASISKTSLS MLELVKSCCC EQQIPTLYKS
SNSYLIFLSI LARMMKEEAE SSGVHPWKQI KGRIYSKFHR KRMQELTEVG LQNFFNLFLL
LAIVAETEDI VSRVLDLLDF LTPSLVSPSQ RALIWRGHFA FLLIYVEKNM DISVLAEKLS
NAFRVKAKEF LVTKNDYTQK QNLWTLISTY IDGVQEVFET SCYLSLSEEK LLNDGFTMLL
PACRGAELSM VLNFLQVVIA RLRSVHKRVS QGLQPGNADS NAQLPLVAKE HHLAVASALW
RNFFPYLKSQ RMSQTPPSPQ LADTAAGFAL LALDIPSKAL SDLQPQPVLS MMQLFGWDDM
VWPHLVSRYL SHLIQNSALC EAFSTMGYTS YEALTVRSWF RCVLQMFIDQ PSGTLAKTDA
ERTVGKAYME QLTEMTRLIF KLKEVESILS KARVEEPVLK QDPKNALVQF IKAVGRTYSG
LQTLPEKSAM VLKALEYLGD VLKYVKPYLK AKGPPEGLQL AYWIIGCLVK FWAPILATSK
AQQLLFRIID CLLLPHSVLQ QDKELPGALL SAIQESLHLY LQGLSFICCQ SQARGAYLNQ
LLGSIVQQYF GRFLPPSPTA LGAGQHPMLT ALCSSITVPQ ALRLRKTTLH VINEHYMQFK
GSAPPPRLAS VLAFILEVLQ RTQASELCDV ELVLPAVLKC MVLVNELQVK KISTVIVQYM
VQGCQARSGG EHATQLTSVF RQFIQDYTAV YDHRVFSILE TVAVLDQTLV TSLIPTLTQS
LKDSEYKQGL GRNAAQREAY KRLLTHLSEA GQNEIQKLEN EAG
