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POLI_MOUSE
ID   POLI_MOUSE              Reviewed;         717 AA.
AC   Q6R3M4; Q641P1; Q6R3M3; Q9R1A6;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=DNA polymerase iota;
DE            EC=2.7.7.7 {ECO:0000269|PubMed:15026325};
DE   AltName: Full=Rad30 homolog B;
GN   Name=Poli; Synonyms=Rad30b;
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] (ISOFORM 1), VARIANTS SER-4; ARG-7 AND SER-518,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Testis;
RX   PubMed=10458907; DOI=10.1006/geno.1999.5906;
RA   McDonald J.P., Rapic-Otrin V., Epstein J.A., Broughton B.C., Wang X.,
RA   Lehmann A.R., Wolgemuth D.J., Woodgate R.;
RT   "Novel human and mouse homologs of Saccharomyces cerevisiae DNA polymerase
RT   eta.";
RL   Genomics 60:20-30(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   VARIANTS SER-4; ARG-7; LYS-334; ALA-378; SER-518; TYR-524; GLU-569;
RP   ASP-574; ARG-606 AND ILE-643, AND ALTERNATIVE SPLICING.
RC   STRAIN=A/J, and BALB/cJ;
RX   PubMed=15026325; DOI=10.1158/0008-5472.can-03-3080;
RA   Wang M., Devereux T.R., Vikis H.G., McCulloch S.D., Holliday W., Anna C.,
RA   Wang Y., Bebenek K., Kunkel T.A., Guan K., You M.;
RT   "Pol iota is a candidate for the mouse pulmonary adenoma resistance 2
RT   locus, a major modifier of chemically induced lung neoplasia.";
RL   Cancer Res. 64:1924-1931(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-518.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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   INTERACTION WITH REV1.
RX   PubMed=14657033; DOI=10.1093/emboj/cdg626;
RA   Guo C., Fischhaber P.L., Luk-Paszyc M.J., Masuda Y., Zhou J., Kamiya K.,
RA   Kisker C., Friedberg E.C.;
RT   "Mouse Rev1 protein interacts with multiple DNA polymerases involved in
RT   translesion DNA synthesis.";
RL   EMBO J. 22:6621-6630(2003).
RN   [5]
RP   FUNCTION, INTERACTION WITH UBIQUITIN, SUBCELLULAR LOCATION, UBIQUITINATION,
RP   MOTIF, AND MUTAGENESIS OF LEU-508; PRO-509; LEU-693; PRO-694;
RP   496-LEU--ASN-524 AND 681-PHE--GLY-709.
RX   PubMed=16357261; DOI=10.1126/science.1120615;
RA   Bienko M., Green C.M., Crosetto N., Rudolf F., Zapart G., Coull B.,
RA   Kannouche P., Wider G., Peter M., Lehmann A.R., Hofmann K., Dikic I.;
RT   "Ubiquitin-binding domains in Y-family polymerases regulate translesion
RT   synthesis.";
RL   Science 310:1821-1824(2005).
CC   -!- FUNCTION: Error-prone DNA polymerase specifically involved in DNA
CC       repair (PubMed:15026325, PubMed:16357261). Plays an important role in
CC       translesion synthesis, where the normal high-fidelity DNA polymerases
CC       cannot proceed and DNA synthesis stalls (PubMed:15026325,
CC       PubMed:16357261). Favors Hoogsteen base-pairing in the active site.
CC       Inserts the correct base with high-fidelity opposite an adenosine
CC       template (By similarity). Exhibits low fidelity and efficiency opposite
CC       a thymidine template, where it will preferentially insert guanosine (By
CC       similarity). May play a role in hypermutation of immunoglobulin genes
CC       (By similarity). Forms a Schiff base with 5'-deoxyribose phosphate at
CC       abasic sites, but may not have lyase activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UNA4, ECO:0000269|PubMed:15026325,
CC       ECO:0000269|PubMed:16357261}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000269|PubMed:15026325};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNA4};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9UNA4};
CC       Note=Binds nucleotide much more tightly and catalyzes nucleotide
CC       insertion much more efficiently in the presence of Mg(2+) than in the
CC       presence of Mn(2+). {ECO:0000250|UniProtKB:Q9UNA4};
CC   -!- SUBUNIT: Interacts with POLH (By similarity). Interacts with REV1
CC       (PubMed:14657033). Interacts with ubiquitin (PubMed:16357261).
CC       {ECO:0000250|UniProtKB:Q9UNA4, ECO:0000269|PubMed:14657033,
CC       ECO:0000269|PubMed:16357261}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Binding to ubiquitin
CC       mediates localization to replication forks after UV-induced DNA damage.
CC       {ECO:0000269|PubMed:16357261}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6R3M4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6R3M4-2; Sequence=VSP_012800;
CC   -!- TISSUE SPECIFICITY: Detected in testis, and at very low levels in
CC       spleen, lung and brain. Detected in round spermatids, but not in
CC       prophase spermatocytes. {ECO:0000269|PubMed:10458907}.
CC   -!- DOMAIN: The catalytic core consists of fingers, palm and thumb
CC       subdomains, but the fingers and thumb subdomains are much smaller than
CC       in high-fidelity polymerases; residues from five sequence motifs of the
CC       Y-family cluster around an active site cleft that can accommodate DNA
CC       and nucleotide substrates with relaxed geometric constraints, with
CC       consequently higher rates of misincorporation and low processivity.
CC       {ECO:0000250|UniProtKB:Q9UNA4}.
CC   -!- DOMAIN: Ubiquitin-binding motif 1 and ubiquitin-binding motif 2
CC       regulate POLI protein monoubiquitination and localization to nuclear
CC       foci after UV-induced DNA damage. {ECO:0000269|PubMed:16357261}.
CC   -!- PTM: Monoubiquitinated (PubMed:16357261). Protein monoubiquitination
CC       prevents POLI binding to ubiquitin via the ubiquitin-binding motif 1
CC       and ubiquitin-binding motif 2 (PubMed:16357261).
CC       {ECO:0000269|PubMed:16357261}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR   EMBL; AF151691; AAD50424.1; -; mRNA.
DR   EMBL; AY515316; AAS75834.1; -; mRNA.
DR   EMBL; AY515317; AAS75835.1; -; mRNA.
DR   EMBL; BC082278; AAH82278.1; -; mRNA.
DR   CCDS; CCDS50317.1; -. [Q6R3M4-2]
DR   RefSeq; NP_001129562.1; NM_001136090.2.
DR   RefSeq; NP_001276444.1; NM_001289515.1.
DR   RefSeq; NP_001276445.1; NM_001289516.1.
DR   RefSeq; XP_006526009.1; XM_006525946.3.
DR   PDB; 2KWU; NMR; -; A=673-717.
DR   PDB; 2KWV; NMR; -; A=487-532.
DR   PDB; 3AI4; X-ray; 1.60 A; A=668-717.
DR   PDBsum; 2KWU; -.
DR   PDBsum; 2KWV; -.
DR   PDBsum; 3AI4; -.
DR   AlphaFoldDB; Q6R3M4; -.
DR   BMRB; Q6R3M4; -.
DR   SMR; Q6R3M4; -.
DR   BioGRID; 204998; 6.
DR   IntAct; Q6R3M4; 1.
DR   STRING; 10090.ENSMUSP00000112563; -.
DR   BindingDB; Q6R3M4; -.
DR   ChEMBL; CHEMBL5159; -.
DR   iPTMnet; Q6R3M4; -.
DR   PhosphoSitePlus; Q6R3M4; -.
DR   MaxQB; Q6R3M4; -.
DR   PaxDb; Q6R3M4; -.
DR   PRIDE; Q6R3M4; -.
DR   ProteomicsDB; 289945; -. [Q6R3M4-1]
DR   ProteomicsDB; 289946; -. [Q6R3M4-2]
DR   GeneID; 26447; -.
DR   KEGG; mmu:26447; -.
DR   CTD; 11201; -.
DR   MGI; MGI:1347081; Poli.
DR   eggNOG; KOG2095; Eukaryota.
DR   InParanoid; Q6R3M4; -.
DR   PhylomeDB; Q6R3M4; -.
DR   Reactome; R-MMU-5656121; Translesion synthesis by POLI.
DR   Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR   BioGRID-ORCS; 26447; 1 hit in 108 CRISPR screens.
DR   PRO; PR:Q6R3M4; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q6R3M4; protein.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071494; P:cellular response to UV-C; IMP:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0019985; P:translesion synthesis; IMP:MGI.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR024728; PolY_HhH_motif.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF11798; IMS_HHH; 1.
DR   SUPFAM; SSF100879; SSF100879; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA damage; DNA repair;
KW   DNA replication; DNA synthesis; DNA-binding; DNA-directed DNA polymerase;
KW   Magnesium; Manganese; Metal-binding; Mutator protein;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Schiff base;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..717
FT                   /note="DNA polymerase iota"
FT                   /id="PRO_0000173989"
FT   DOMAIN          30..243
FT                   /note="UmuC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..307
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT   REGION          343..360
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT   REGION          549..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           500..517
FT                   /note="Ubiquitin-binding 1 (UBM1)"
FT                   /evidence="ECO:0000269|PubMed:16357261"
FT   MOTIF           685..702
FT                   /note="Ubiquitin-binding 2 (UBM2)"
FT                   /evidence="ECO:0000269|PubMed:16357261"
FT   COMPBIAS        574..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..680
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         34
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT   BINDING         35
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT   BINDING         39
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT   BINDING         71
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT   BINDING         126
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT   VAR_SEQ         1..43
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012800"
FT   VARIANT         4
FT                   /note="L -> S (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:10458907,
FT                   ECO:0000269|PubMed:15026325"
FT   VARIANT         7
FT                   /note="G -> R (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:10458907,
FT                   ECO:0000269|PubMed:15026325"
FT   VARIANT         334
FT                   /note="Q -> K (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:15026325"
FT   VARIANT         378
FT                   /note="S -> A (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:15026325"
FT   VARIANT         518
FT                   /note="Y -> S (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:10458907,
FT                   ECO:0000269|PubMed:15026325, ECO:0000269|PubMed:15489334"
FT   VARIANT         524
FT                   /note="N -> Y (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:15026325"
FT   VARIANT         569
FT                   /note="A -> E (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:15026325"
FT   VARIANT         574
FT                   /note="E -> D (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:15026325"
FT   VARIANT         606
FT                   /note="Q -> R (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:15026325"
FT   VARIANT         643
FT                   /note="T -> I (in strain: BALB/c)"
FT                   /evidence="ECO:0000269|PubMed:15026325"
FT   MUTAGEN         496..524
FT                   /note="Missing: Abolishes ubiquitin binding and
FT                   localization to nuclear foci after UV-induced DNA damage."
FT                   /evidence="ECO:0000269|PubMed:16357261"
FT   MUTAGEN         508
FT                   /note="L->A: Impairs ubiquitin binding and post-translation
FT                   modification via ubiquitination; when associated with A-
FT                   509. Abolishes ubiquitin binding and localization to
FT                   nuclear foci after UV-induced DNA damage but does not
FT                   affect catalytic activity; when associated with A-508, A-
FT                   693 and A-694."
FT                   /evidence="ECO:0000269|PubMed:16357261"
FT   MUTAGEN         509
FT                   /note="P->A: Impairs ubiquitin binding and post-translation
FT                   modification via ubiquitination; when associated with A-
FT                   508. Abolishes ubiquitin binding and localization to
FT                   nuclear foci after UV-induced DNA damage but does not
FT                   affect catalytic activity; when associated with A-509, A-
FT                   693 and A-694."
FT                   /evidence="ECO:0000269|PubMed:16357261"
FT   MUTAGEN         681..709
FT                   /note="Missing: Abolishes ubiquitin binding and
FT                   localization to nuclear foci after UV-induced DNA damage."
FT                   /evidence="ECO:0000269|PubMed:16357261"
FT   MUTAGEN         693
FT                   /note="L->A: Impairs ubiquitin binding and post-translation
FT                   modification via ubiquitination; when associated with A-
FT                   694. Abolishes ubiquitin binding and localization to
FT                   nuclear foci after UV-induced DNA damage but does not
FT                   affect catalytic activity; when associated with A-508, A-
FT                   509 and A-694."
FT                   /evidence="ECO:0000269|PubMed:16357261"
FT   MUTAGEN         694
FT                   /note="P->A: Impairs ubiquitin binding and post-translation
FT                   modification via ubiquitination; when associated with A-
FT                   693. Abolishes ubiquitin binding and localization to
FT                   nuclear foci after UV-induced DNA damage but does not
FT                   affect catalytic activity; when associated with A-508, A-
FT                   509 and A-693."
FT                   /evidence="ECO:0000269|PubMed:16357261"
FT   CONFLICT        583
FT                   /note="G -> R (in Ref. 1; AAD50424)"
FT                   /evidence="ECO:0000305"
FT   HELIX           502..504
FT                   /evidence="ECO:0007829|PDB:2KWV"
FT   TURN            505..507
FT                   /evidence="ECO:0007829|PDB:2KWV"
FT   HELIX           510..516
FT                   /evidence="ECO:0007829|PDB:2KWV"
FT   STRAND          682..684
FT                   /evidence="ECO:0007829|PDB:2KWU"
FT   HELIX           687..690
FT                   /evidence="ECO:0007829|PDB:3AI4"
FT   HELIX           695..700
FT                   /evidence="ECO:0007829|PDB:3AI4"
FT   HELIX           701..705
FT                   /evidence="ECO:0007829|PDB:3AI4"
SQ   SEQUENCE   717 AA;  79653 MW;  43E5D2D0ECB3AA85 CRC64;
     MEPLHAGAAG SSRAVCSQGP PTQISSSRVI VHVDLDCFYA QVEMISNPEL KDRPLGVQQK
     YLVVTCNYEA RKLGVRKLMN VRDAKEKCPQ LVLVNGEDLS RYREMSYKVT ELLEEFSPAV
     ERLGFDENFV DLTEMVEKRL QQLPSEEVPS VTVFGHVYNN QSVNLHNIMH RRLVVGSQIA
     AEMREAMYNQ LGLTGCAGVA PNKLLAKLVS GVFKPNQQTV LLPESCQHLI HSLNHIKEIP
     GIGYKTAKRL EVLGINSVHD LQTFPIKTLE KELGIAIAQR IQQLSFGEDK SPVTPSGPPQ
     SFSEEDTFKK CSSEVEAKAK IEELLSSLLT RVCQDGRKPH TVRLVIRRYS DKHCNRESRQ
     CPIPSHVIQK LGTGNHDSMP PLIDILMKLF RNMVNVKMPF HLTLMSVCFC NLKALSSAKK
     GPMDCYLTSL STPAYTDKRA FKVKDTHTED SHKEKEANWD CLPSRRIEST GTGESPLDAT
     CFPKEKDTSD LPLQALPEGV DQEVFKQLPA DIQEEILYGK SRENLKGKGS LSCPLHASRG
     VLSFFSTKQM QASRLSPRDT ALPSKRVSAA SPCEPGTSGL SPGSTSHPSC GKDCSYYIDS
     QLKDEQTSQG PTESQGCQFS STNPAVSGFH SFPNLQTEQL FSTHRTVDSH KQTATASHQG
     LESHQGLESR ELDSAEEKLP FPPDIDPQVF YELPEEVQKE LMAEWERAGA ARPSAHR
 
 
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