PMS2_CHICK
ID PMS2_CHICK Reviewed; 869 AA.
AC F1NQJ3; Q5ZJ94;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 3.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Mismatch repair endonuclease PMS2 {ECO:0000305};
DE EC=3.1.-.-;
DE AltName: Full=DNA mismatch repair protein PMS2 {ECO:0000305};
DE AltName: Full=PMS1 protein homolog 2 {ECO:0000250|UniProtKB:P54278};
GN Name=PMS2 {ECO:0000250|UniProtKB:P54278};
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 MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
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).
RN [3]
RP FUNCTION.
RX PubMed=23314153; DOI=10.1093/nar/gks1470;
RA Campo V.A., Patenaude A.M., Kaden S., Horb L., Firka D., Jiricny J.,
RA Di Noia J.M.;
RT "MSH6- or PMS2-deficiency causes re-replication in DT40 B cells, but it has
RT little effect on immunoglobulin gene conversion or on repair of AID-
RT generated uracils.";
RL Nucleic Acids Res. 41:3032-3046(2013).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Involved in B cell growth by positively regulating B cell
CC proliferation and controlling replication efficiency. Controls cell
CC cycle to prevent re-replication and defects in DNA damage-induced G2
CC checkpoint. Doesn't seem to counteract or control the immunoglobulin
CC gene conversion (Ig GC) and to contribute to guanine/uracil mismatch
CC repair. {ECO:0000269|PubMed:23314153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54278}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG32199.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAG32199.1; Type=Frameshift; 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; AJ720540; CAG32199.1; ALT_SEQ; mRNA.
DR EMBL; AADN03006912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001305951.1; NM_001319022.1.
DR RefSeq; XP_015149767.1; XM_015294281.1.
DR AlphaFoldDB; F1NQJ3; -.
DR SMR; F1NQJ3; -.
DR STRING; 9031.ENSGALP00000005417; -.
DR PaxDb; F1NQJ3; -.
DR PRIDE; F1NQJ3; -.
DR Ensembl; ENSGALT00000005427; ENSGALP00000005417; ENSGALG00000003430.
DR GeneID; 101752182; -.
DR KEGG; gga:101752182; -.
DR CTD; 5395; -.
DR VEuPathDB; HostDB:geneid_101752182; -.
DR eggNOG; KOG1978; Eukaryota.
DR GeneTree; ENSGT00940000155381; -.
DR HOGENOM; CLU_004131_0_2_1; -.
DR OMA; HIPRPSK; -.
DR OrthoDB; 735423at2759; -.
DR PRO; PR:F1NQJ3; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000003430; Expressed in spermatid and 14 other tissues.
DR ExpressionAtlas; F1NQJ3; baseline and differential.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central.
DR GO; GO:0032389; C:MutLalpha complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0032407; F:MutSalpha complex binding; IEA:Ensembl.
DR GO; GO:0032138; F:single base insertion or deletion binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IBA:GO_Central.
DR Gene3D; 3.30.1370.100; -; 1.
DR Gene3D; 3.30.1540.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR002099; DNA_mismatch_repair_N.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR038973; MutL/Mlh/Pms.
DR InterPro; IPR014790; MutL_C.
DR InterPro; IPR042120; MutL_C_dimsub.
DR InterPro; IPR042121; MutL_C_regsub.
DR InterPro; IPR037198; MutL_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10073; PTHR10073; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF08676; MutL_C; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00853; MutL_C; 1.
DR SUPFAM; SSF118116; SSF118116; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00585; mutl; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 2: Evidence at transcript level;
KW DNA damage; Endonuclease; Hydrolase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..869
FT /note="Mismatch repair endonuclease PMS2"
FT /id="PRO_0000436969"
FT CONFLICT 578
FT /note="T -> S (in Ref. 1; CAG32199)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="V -> L (in Ref. 1; CAG32199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 869 AA; 97996 MW; 2E97E09EE115DCED CRC64;
MEEAAPCSEP AKTIKRIDRE SVHRICSGQV VLSLGTAVKE LVENSLDAGA TNIDVRLKDH
GAELIEVSDN GGGVEEENFE GLTLKHYTSK IQDFSDLIHV ETFGFRGEAL SSLCALSDVT
ISTCHKSAKV GTRLVFDHNG KITQKAPYPR QQGTTVSIQQ LFHTLPVRHK EFQRNIKKEY
AKMVQILQAY CIISKGVRIN CTNQVGQGKK SPVVSTTGGP NLKENIGAVF GKKQLQSLIP
FVQLPPNEAV CEEYGLKSTD LPEKLYSITG FISRCDHGVG RSTTDRQFFF INQRPCDPAK
VVKLVNEVYH LYNKHQYPFI VLNICVDSEC VDINVTPDKR QILLQEEKLL LAILKTSLIE
MFGSDVNKLN VNQNLLDIVG NVKAPPGDAE KPWVEMSHHS ETENPSSEGK RVMTLSRLRE
SFSLHQTESY FQSPKKVKQR HSSSKQLSLD TILSTVRTQK AVLSEDSESC HEMKSKMPVP
RKYLRKVDDI DSGFCSTSES DAGYNTPEAG SCVISESVNN PIEEEFCSSE EQHQNEYLKT
VGHSEKSLEC DIQVLGTEHK LNRVNDCNNQ TNLPQEATNS LPRVRRFKNE ADDFKAGIHP
KVENTRNYMP CVDVLVEVKK KTVPLEFSMK ALAERVRKIV QQQQKCTETQ NYRRFRAKIS
PGENKVAEDE LRKEISKEMF AKMEIIGQFN LGFIIAKLNS DLFIIDQHAT DEKYNFEMLQ
QHTVLQGQKL IAPQNLNLTA VNETVLIENL EIFRKNGFDF VINENAPVTQ RVKLISLPTS
KNWTFGPQDI DELIFMLSDC PGVMCRPSRV RQMFASRACR KSVMIGTALN VQEMKKLVTH
MGEIEHPWNC PHGRPTMRHI ASLDLIASE
