P52431 (DPOD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase delta catalytic subunit
EC=2.7.7.7

Gene names

Name:

Pold1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1105 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex.
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Cofactor	Binds 1 4Fe-4S cluster By similarity.
Subunit structure	Heterotetramer composed of subunits of 125 kDa, 50 kDa, 66 kDa and 12 kDa. The 125 kDa subunit contains the polymerase active site and most likely the active site for the 3'-5' exonuclease activity. Interacts with WRNIP1. Interacts with POLD4 and PCNA By similarity.
Subcellular location	Nucleus.
Domain	The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes By similarity.
Miscellaneous	In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.
Sequence similarities	Belongs to the DNA polymerase type-B family. Contains 1 CysA-type zinc finger.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	4Fe-4S DNA-binding Iron Iron-sulfur Metal-binding Zinc
Molecular function	DNA-directed DNA polymerase Exonuclease Hydrolase Nuclease Nucleotidyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication proofreading Inferred from mutant phenotype PubMed 12429860. Source: MGI DNA replication, removal of RNA primer Inferred from Biological aspect of Ancestor. Source: RefGenome DNA synthesis involved in DNA repair Inferred from electronic annotation. Source: Compara S phase of mitotic cell cycle Inferred from Biological aspect of Ancestor. Source: RefGenome base-excision repair, gap-filling Inferred from mutant phenotype PubMed 15177179. Source: MGI nucleotide-excision repair, DNA gap filling Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of mitotic cell cycle Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	delta DNA polymerase complex Inferred from Biological aspect of Ancestor. Source: RefGenome nucleotide-excision repair complex Inferred from electronic annotation. Source: Compara
Molecular_function	3'-5' exonuclease activity Inferred from mutant phenotype PubMed 12429860. Source: MGI 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from Biological aspect of Ancestor. Source: RefGenome chromatin binding Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1105	1105	DNA polymerase delta catalytic subunit		PRO_0000046444
Regions
	Zinc finger	1010 – 1027	18	CysA-type
	Motif	4 – 19	16	Nuclear localization signal Potential
	Motif	1056 – 1074	19	CysB motif
Sites
	Metal binding	1010	1	Zinc By similarity
	Metal binding	1013	1	Zinc By similarity
	Metal binding	1024	1	Zinc By similarity
	Metal binding	1027	1	Zinc By similarity
	Metal binding	1056	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	1059	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	1069	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	1074	1	Iron-sulfur (4Fe-4S) By similarity
Amino acid modifications
	Modified residue	1005	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	112	1	G → R in CAA79895. Ref.1
	Sequence conflict	114	1	L → P in AAB99910. Ref.2
	Sequence conflict	576	1	S → G in CAA79895. Ref.1
	Sequence conflict	576	1	S → G in AAB99910. Ref.2
	Sequence conflict	793	1	E → K in AAB99910. Ref.2
	Sequence conflict	1000	1	L → F in AAB99910. Ref.2
	Sequence conflict	1035	1	Y → S in CAA79895. Ref.1
	Sequence conflict	1045 – 1052	8	LEERFSRL → WKNGSLRF in AAB99910. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P52431 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 2AE377D42E3A6A86	FASTA	1,105	123,790
	10 20 30 40 50 60 MDCKRRQGPG PGVPPKRARG HLWDEDEPSP SQFEANLALL EEIEAENRLQ EAEEELQLPP 70 80 90 100 110 120 EGTVGGQFST ADIDPRWRRP TLRALDPSTE PLIFQQLEID HYVGSAPPLP EGPLPSRNSV 130 140 150 160 170 180 PILRAFGVTD EGFSVCCHIQ GFAPYFYTPA PPGFGAEHLS ELQQELNAAI SRDQRGGKEL 190 200 210 220 230 240 SGPAVLAIEL CSRESMFGYH GHGPSPFLRI TLALPRLMAP ARRLLEQGVR VPGLGTPSFA 250 260 270 280 290 300 PYEANVDFEI RFMVDADIVG CNWLELPAGK YVRRAEKKAT LCQLEVDVLW SDVISHPPEG 310 320 330 340 350 360 QWQRIAPLRV LSFDIECAGR KGIFPEPERD PVIQICSLGL RWGEPEPFLR LALTLRPCAP 370 380 390 400 410 420 ILGAKVQSYE REEDLLQAWA DFILAMDPDV ITGYNIQNFD LPYLISRAQA LKVDRFPFLG 430 440 450 460 470 480 RVTGLRSNIR DSSFQSRQVG RRDSKVISMV GRVQMDMLQV LLREHKLRSY TLNAVSFHFL 490 500 510 520 530 540 GEQKEDVQHS IITDLQNGNE QTRRRLAVYC LKDAFLPLRL LERLMVLVNN VEMARVTGVP 550 560 570 580 590 600 LGYLLTRGQQ VKVVSQLLRQ AMRQGLLMPV VKTEGSEDYT GATVIEPLKG YYDVPIATLD 610 620 630 640 650 660 FSSLYPSIMM AHNLCYTTLL RPGAAQKLGL KPDEFIKTPT GDEFVKSSVR KGLLPQILEN 670 680 690 700 710 720 LLSARKRAKA ELAQETDPLR RQVLDGRQLA LKVSANSVYG FTGAQVGKLP CLEISQSVTG 730 740 750 760 770 780 FGRQMIEKTK QLVESKYTVE NGYDANAKVV YGDTDSVMCR FGVSSVAEAM SLGREAANWV 790 800 810 820 830 840 SSHFPSPIRL EFEKVYFPYL LISKKRYAGL LFSSRSDAHD KMDCKGLEAV RRDNCPLVAN 850 860 870 880 890 900 LVTSSLRRIL VDRDPDGAVA HAKDVISDLL CNRIDISQLV ITKELTRAAA DYAGKQAHVE 910 920 930 940 950 960 LAERMRKRDP GSAPSLGDRV PYVIIGAAKG VAAYMKSEDP LFVLEHSLPI DTQYYLEQQL 970 980 990 1000 1010 1020 AKPLLRIFEP ILGEGRAESV LLRGDHTRCK TVLTSKVGGL LAFTKRRNCC IGCRSVIDHQ 1030 1040 1050 1060 1070 1080 GAVCKFCQPR ESELYQKEVS HLNALEERFS RLWTQCQRCQ GSLHEDVICT SRDCPIFYMR 1090 1100 KKVRKDLEDQ ERLLQRFGPP GPEAW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a mouse cDNA encoding DNA polymerase delta: refinement of the homology boxes." Cullmann G., Hindges R., Berchtold M.W., Huebscher U. Gene 134:191-200(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"Mouse DNA polymerase delta gene (Pold1) maps to chromosome 7." Goldsby R.E., Singh M., Preston B.D. Mamm. Genome 9:92-93(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart and Liver.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 408-415, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z21848 mRNA. Translation: CAA79895.1. AF024570 Genomic DNA. Translation: AAB99910.1. AK167569 mRNA. Translation: BAE39632.1. AK168967 mRNA. Translation: BAE40772.1. AK169040 mRNA. Translation: BAE40829.1.
IPI	IPI00323143.
PIR	S40243.
RefSeq	NP_035261.3. NM_011131.3.
UniGene	Mm.16549.
3D structure databases
ProteinModelPortal	P52431.
SMR	P52431. Positions 297-969.
ModBase	Search...
Protein-protein interaction databases
IntAct	P52431. 1 interaction.
STRING	10090.ENSMUSP00000039776.
PTM databases
PhosphoSite	P52431.
Proteomic databases
PaxDb	P52431.
PRIDE	P52431.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000049343; ENSMUSP00000039776; ENSMUSG00000038644.
GeneID	18971.
KEGG	mmu:18971.
Organism-specific databases
CTD	5424.
MGI	MGI:97741. Pold1.
Phylogenomic databases
eggNOG	COG0417.
GeneTree	ENSGT00560000077365.
HOGENOM	HOG000036616.
HOVERGEN	HBG051395.
InParanoid	Q3TFX6.
KO	K02327.
OMA	MIEQTKQ.
OrthoDB	EOG4KWJS2.
Gene expression databases
ArrayExpress	P52431.
Bgee	P52431.
Genevestigator	P52431.
GermOnline	ENSMUSG00000038644. Mus musculus.
Family and domain databases
Gene3D	3.90.1600.10. 2 hits.
InterPro	IPR006172. DNA-dir_DNA_pol_B. IPR017964. DNA-dir_DNA_pol_B_CS. IPR006133. DNA-dir_DNA_pol_B_exonuc. IPR006134. DNA-dir_DNA_pol_B_multi_dom. IPR004578. DNA-dir_DNA_pol_B_pol2. IPR023211. DNA_pol_palm_dom. IPR012337. RNaseH-like_dom. IPR025687. Znf-C4pol. [Graphical view]
Pfam	PF00136. DNA_pol_B. 1 hit. PF03104. DNA_pol_B_exo1. 1 hit. PF14260. zf-C4pol. 1 hit. [Graphical view]
PRINTS	PR00106. DNAPOLB.
SMART	SM00486. POLBc. 1 hit. [Graphical view]
SUPFAM	SSF53098. RNaseH_fold. 1 hit.
TIGRFAMs	TIGR00592. pol2. 1 hit.
PROSITE	PS00116. DNA_POLYMERASE_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	POLD1. mouse.
NextBio	295320.
PMAP-CutDB	P52431.
SOURCE	Search...

Entry information

Entry name

DPOD1_MOUSE

Accession

Primary (citable) accession number: P52431
Secondary accession number(s): O54883, Q3TFX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program