DCR1A_MOUSE
ID DCR1A_MOUSE Reviewed; 1026 AA.
AC Q9JIC3; Q571H5; Q6GQR6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA cross-link repair 1A protein;
DE AltName: Full=Beta-lactamase MBLAC2;
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:Q6PJP8};
DE AltName: Full=SNM1 homolog A;
GN Name=Dclre1a; Synonyms=Kiaa0086, Snm1, Snm1a;
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 [MRNA], AND FUNCTION.
RC STRAIN=129/Sv;
RX PubMed=10848582; DOI=10.1128/mcb.20.13.4553-4561.2000;
RA Dronkert M.L.G., de Wit J., Boeve M., Vasconcelos M.L., van Steeg H.,
RA Tan T.L.R., Hoeijmakers J.H.J., Kanaar R.;
RT "Disruption of mouse SNM1 causes increased sensitivity to the DNA
RT interstrand cross-linking agent mitomycin C.";
RL Mol. Cell. Biol. 20:4553-4561(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-1023.
RC TISSUE=Spleen;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Kitamura H., Nagase T.,
RA Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=15542852; DOI=10.1128/mcb.24.23.10448-10455.2004;
RA Akhter S., Richie C.T., Deng J.M., Brey E., Zhang X., Patrick C. Jr.,
RA Behringer R.R., Legerski R.J.;
RT "Deficiency in SNM1 abolishes an early mitotic checkpoint induced by
RT spindle stress.";
RL Mol. Cell. Biol. 24:10448-10455(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574 AND SER-578, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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: May be required for DNA interstrand cross-link repair. Also
CC required for checkpoint mediated cell cycle arrest in early prophase in
CC response to mitotic spindle poisons. {ECO:0000269|PubMed:10848582,
CC ECO:0000269|PubMed:15542852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q6PJP8};
CC -!- SUBUNIT: Binds constitutively to TP53BP1. Binds CDC27, which is itself
CC a component of the anaphase promoting complex (APC). Binds PIAS1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=In some cells it may
CC be found in typically 1 or 2 discrete nuclear aggregates of unknown
CC function which also contain TP53BP1. Also found in multiple discrete
CC nuclear foci which increase in number following treatment with ionizing
CC radiation or interstrand cross-linking agents. These foci overlap with
CC those formed by the MRN complex (composed of MRE11, RAD50 and NBN) and
CC BRCA1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72667.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF241240; AAF64472.1; -; mRNA.
DR EMBL; BC072667; AAH72667.1; ALT_SEQ; mRNA.
DR EMBL; AK220214; BAD90139.1; -; mRNA.
DR AlphaFoldDB; Q9JIC3; -.
DR SMR; Q9JIC3; -.
DR STRING; 10090.ENSMUSP00000138290; -.
DR iPTMnet; Q9JIC3; -.
DR PhosphoSitePlus; Q9JIC3; -.
DR PaxDb; Q9JIC3; -.
DR PRIDE; Q9JIC3; -.
DR ProteomicsDB; 279887; -.
DR MGI; MGI:1930042; Dclre1a.
DR eggNOG; KOG1361; Eukaryota.
DR InParanoid; Q9JIC3; -.
DR PhylomeDB; Q9JIC3; -.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR ChiTaRS; Dclre1a; mouse.
DR PRO; PR:Q9JIC3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JIC3; protein.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:MGI.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA damage; DNA repair; Hydrolase;
KW Isopeptide bond; Metal-binding; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1026
FT /note="DNA cross-link repair 1A protein"
FT /id="PRO_0000209117"
FT ZN_FING 118..148
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 1..189
FT /note="Nuclear localization region"
FT /evidence="ECO:0000250"
FT REGION 12..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..602
FT /note="Nuclear focus formation"
FT /evidence="ECO:0000250"
FT REGION 474..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJP8"
FT CROSSLNK 434
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJP8"
FT CROSSLNK 522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJP8"
FT CROSSLNK 657
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJP8"
FT CONFLICT 5
FT /note="T -> TF (in Ref. 2; AAH72667)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="T -> A (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="S -> N (in Ref. 3; BAD90139)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="S -> P (in Ref. 3; BAD90139)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..269
FT /note="RD -> KT (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..293
FT /note="SMG -> YVA (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
FT CONFLICT 296..306
FT /note="LPENDTDSCEI -> EMTLTAVV (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..324
FT /note="QEL -> PRA (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="G -> C (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="A -> G (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="A -> P (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="S -> F (in Ref. 2; AAH72667)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="G -> R (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="S -> I (in Ref. 2; AAH72667)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="K -> KGK (in Ref. 2; AAH72667)"
FT /evidence="ECO:0000305"
FT CONFLICT 774..775
FT /note="LL -> FV (in Ref. 1; AAF64472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1026 AA; 113567 MW; BFDB4E03135FB901 CRC64;
MLEDTWEEEI WEYKSKRKPK PVHPNNCSEN ISESVEKSTD GKHQSKGNEK RTSENPGKTK
DHKVCLAETD SQISAGSSQS SSCRDESQQS QNKETTPKKQ HRTRRGKQVT PKVRPVYDGY
CPSCQMPFSS LLGQTPQWHV FECLDSPPIS DTECPEGLLC TSTIPSHYKK YTHILLAQSR
DSKEPLGSPS DALAGLFAAA APGSPCNLEE RRSMTLKTEN LRKVSDHSLL MMQYLETSQP
SAEINRKNVS SPCSQTSPVP QCAEFVKRDQ LVGGGSPLAE VALNSQSKSG SMGLPLPEND
TDSCEISYSP LHSDEETYDI DQELDDSQQE LFFTQSSKDS SLEEDGSAIF ENLHGPSPKE
AEGIRPTAKS LVAQARCSAP SEGSTLSDSF LLLSYTSNRL SQEDLPHTDA AFHLLSPALA
VGGAASNYQT SKAKLDEPEK FLSLASSHQQ QKIETSAVGN QTSLPLLTRA RSKPLEKEGG
KCLPLHPTQS QTRGSPRKGL GAPGANCACR NAQKRSSMPL DKPLGTSPSS PKCSPSQPSK
KVMKQMDIGV FFGLPPKRQE TSLRESASEG PNVSPVVSPN QKRPRLCKRK AQSSLSDLEF
DAKNLNESQH SVGLSGEKRQ HRRKRHKTSN SPREGPCQRR SGHLMNNPEL GPVSLSKAFV
RRTRGRTQRG NMNISESSGA GEVRRTCPFY KRIPGTGFTV DAFQYGEIEG CTAYFLTHFH
SDHYAGLSKD FTRPVYCSEI TGNLLKKKLR VQEQYIRQLP MDTECVVDSV KVVLLDANHC
PGATMILFQL PNGAVILHTG DFRADPSMER SRLAGRKVHT LFLDTTYCSP EYTFPSQQEV
IQFAINTAFE AVTLNPRALV VCGTYCIGKE KVFLAIADVL GSKVGMSQEK YKTLQCLNIP
EVSSLITTDM CDSLVHLLPM MQINFKGLQS HLKKCGGKYD QILAFRPTGW THSNNITSTA
DIIPQTRGNI SIYGIPYSEH SSYLEMKRFV QWLKPQKIIP TVNVGSFRSR NTMEKYFKEW
RLEAGY
