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Protein

DNA polymerase alpha catalytic subunit

Gene

Pola1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes (By similarity).By similarity

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1290 – 12901ZincBy similarity
Metal bindingi1293 – 12931ZincBy similarity
Metal bindingi1317 – 13171ZincBy similarity
Metal bindingi1322 – 13221ZincBy similarity
Metal bindingi1355 – 13551Iron-sulfur (4Fe-4S)By similarity
Metal bindingi1360 – 13601Iron-sulfur (4Fe-4S)By similarity
Metal bindingi1378 – 13781Iron-sulfur (4Fe-4S)By similarity
Metal bindingi1381 – 13811Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1290 – 132031CysA-typeAdd
BLAST

GO - Molecular functioni

  • 3'-5' exonuclease activity Source: InterPro
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • chromatin binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA-directed DNA polymerase activity Source: UniProtKB
  • double-stranded DNA binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • nucleoside binding Source: InterPro
  • nucleotide binding Source: UniProtKB
  • purine nucleotide binding Source: RGD
  • pyrimidine nucleotide binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase alpha catalytic subunit (EC:2.7.7.7)
Alternative name(s):
DNA polymerase alpha catalytic subunit p180
Gene namesi
Name:Pola1
Synonyms:Pola
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621816. Pola1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›1451›1451DNA polymerase alpha catalytic subunitPRO_0000046430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921PhosphoserineBy similarity
Modified residuei196 – 1961PhosphoserineBy similarity
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei230 – 2301N6-acetyllysineBy similarity
Modified residuei977 – 9771N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO89042.
PRIDEiO89042.

PTM databases

iPTMnetiO89042.
PhosphoSiteiO89042.

Interactioni

Subunit structurei

The DNA polymerase alpha complex is composed of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the small and the large primase subunits PRIM1 and PRIM2 respectively. Interacts with PARP1; this interaction functions as part of the control of replication fork progression. Interacts with MCM10 and WDHD1; these interactions recruit the polymerase alpha complex to the pre-replicative complex bound to DNA. Interacts with RPA1; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018147.

Structurei

3D structure databases

ProteinModelPortaliO89042.
SMRiO89042. Positions 1352-1389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni657 – 72266DNA-binding regionSequence analysisAdd
BLAST
Regioni1252 – 1383132DNA-binding regionSequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1355 – 138127CysB motifAdd
BLAST

Domaini

The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes.By similarity

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Curated
Contains 1 CysA-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1290 – 132031CysA-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0970. Eukaryota.
COG0417. LUCA.
HOGENOMiHOG000163524.
HOVERGENiHBG080008.
InParanoidiO89042.
KOiK02320.
PhylomeDBiO89042.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProiIPR006172. 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.
IPR024647. DNA_pol_a_cat_su_N.
IPR023211. DNA_pol_palm_dom.
IPR029702. POLA/Pol1.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view]
PANTHERiPTHR10322:SF21. PTHR10322:SF21. 4 hits.
PfamiPF12254. DNA_pol_alpha_N. 1 hit.
PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08996. zf-DNA_Pol. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

O89042-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPVHGDDCK LETSAVSDSG SFVASRARRE KKSKKGRQEA LERLKKAKAG
60 70 80 90 100
EKYKYEVEDL TSVYEEVDEE QYSKLVQARQ DDDWIVDDDG IGYVEDGREI
110 120 130 140 150
FDDDLEDDAL DTCGEGSDGK AHRKDRKDVK KPSVTKPNNI KAMFIASAGK
160 170 180 190 200
KTTDKTVDLS KDDLLGDILQ DLNTETPQIA PPPVLIPKKK RSTGASPNPF
210 220 230 240 250
SVHTATAVPS GKIASPVSRK EPPLTPVPLK RAEFAGDLAQ PECPEDEQES
260 270 280 290 300
GVIEFEDGDF DEPMDTEEVD EEEPVTAKIW DQESEPVEGV KHEADPETGT
310 320 330 340 350
TSFLDSFLPD VSCWDIDQKD ENSFLLQEVQ VDSNHLPLVK GADDEQVFQF
360 370 380 390 400
YWLDAYEDPY NQPGVVFLFG KVWVESAKTH VSCCVMVKNI ERTLYFLPRE
410 420 430 440 450
MKIDLNTGKE TATPITMKDV YEEFDSKISA KYKIMKFKSK IVEKNYAFEI
460 470 480 490 500
PDVPEKSEYL EVRYSAEVPQ LPQNLKGETF SHVFGTNTSS LELFLMNRKI
510 520 530 540 550
KGPCWLEVKN PQLLNQPISW CKFEAMALKP DLVNVIKDVS PPPLVVMSFS
560 570 580 590 600
MKTMQNVQNH QHEIIAMAAL VHHNFPLDKA PPKPPFQTHF CVVSKPKDCI
610 620 630 640 650
FPCAFKEVIK KKNMEVEVAA TERTLLGFFL AKVHKLDPDI LVGHNICGFE
660 670 680 690 700
LEVLLQRINE CKVPFWSKIG RLRRSNMPKL GSRSGFGERN ATCGRMICDV
710 720 730 740 750
EISVKELIHC KSYHLSELVQ QILKTERIVI PTENIRNMYS EPSHLLYLLE
760 770 780 790 800
HIWKDARFIL QIMCELNVLP LALQITNIAG NIMSRTLMGG RSERNEFLLL
810 820 830 840 850
HAFYENNYIV PDKQIFRKPQ QKPGDEDEEI DGDTNKYKKG RKKAAYAGGL
860 870 880 890 900
VLDPKVGFYD KFILLLDFNS LYPSIIQEFN ICFTTVQRVA SETLKATEDE
910 920 930 940 950
EQEQIPELPD PNLDMGILPR EIRKLVERRK QVKQLMKQQD LNPDLVLQYD
960 970 980 990 1000
IRQKALKLTA NSMYGCLGFS YSRFYAKPLA ALVTYKGREI LMHTKEMVQK
1010 1020 1030 1040 1050
MNLEVIYGDT DSIMINTNST NLEEVFKLGN KVKNEVNKLY KLLEIDIDGV
1060 1070 1080 1090 1100
FKSLLLLKKK KYAALVVEPT SDGNYITKQE LKGLDIVRRD WCDLAKDTGN
1110 1120 1130 1140 1150
FVIGQILSDQ SRDTIVENIQ KRLIEIGENV LNGSVPVSQF EINKALTKDP
1160 1170 1180 1190 1200
QDYPDKKSLP HVHVALWINS QGGRKVKAGD TVSYVICQDG SNLPATQRAY
1210 1220 1230 1240 1250
APEQLQKQDN LAIDTQYYLA QQIHPVVARI CEPIDGIDAV LIALWLGLDS
1260 1270 1280 1290 1300
TQFRVHQYHK DEENDALLGG PAQLTDEEKY KDCEKFKCLC PSCGTENIYD
1310 1320 1330 1340 1350
NVFEGSGMDM EPSLNRCSNI DCKASPATFM VQLSNKLIMD IRRCIKKYYD
1360 1370 1380 1390 1400
GWLICEEPTC RNRIRRLPLH FSRNGPLCPA CMKAVLRPEY SDKSLYTQLC
1410 1420 1430 1440 1450
FYRYIFDADC ALEKLPEHEK DKLKKQFFTP RVLQDYRKVK NIAEHFLSWS

G
Length:1,451
Mass (Da):165,306
Last modified:November 1, 1998 - v1
Checksum:iF0E1B16F8B8D5CD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1451 – 14511

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011605 mRNA. Translation: CAA09720.1.
RefSeqiNP_445931.1. NM_053479.1.
UniGeneiRn.187125.
Rn.92345.

Genome annotation databases

GeneIDi85241.
KEGGirno:85241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011605 mRNA. Translation: CAA09720.1.
RefSeqiNP_445931.1. NM_053479.1.
UniGeneiRn.187125.
Rn.92345.

3D structure databases

ProteinModelPortaliO89042.
SMRiO89042. Positions 1352-1389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018147.

PTM databases

iPTMnetiO89042.
PhosphoSiteiO89042.

Proteomic databases

PaxDbiO89042.
PRIDEiO89042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi85241.
KEGGirno:85241.

Organism-specific databases

CTDi5422.
RGDi621816. Pola1.

Phylogenomic databases

eggNOGiKOG0970. Eukaryota.
COG0417. LUCA.
HOGENOMiHOG000163524.
HOVERGENiHBG080008.
InParanoidiO89042.
KOiK02320.
PhylomeDBiO89042.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProiIPR006172. 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.
IPR024647. DNA_pol_a_cat_su_N.
IPR023211. DNA_pol_palm_dom.
IPR029702. POLA/Pol1.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view]
PANTHERiPTHR10322:SF21. PTHR10322:SF21. 4 hits.
PfamiPF12254. DNA_pol_alpha_N. 1 hit.
PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08996. zf-DNA_Pol. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A mutation detected in DNA polymerase delta cDNA from Novikoff hepatoma cells correlates with abnormal catalytic properties of the enzyme."
    Popanda O., Flohr T., Fox G., Thielmann H.W.
    J. Cancer Res. Clin. Oncol. 125:598-608(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.

Entry informationi

Entry nameiDPOLA_RAT
AccessioniPrimary (citable) accession number: O89042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.