DPOA2_SCHPO
ID DPOA2_SCHPO Reviewed; 574 AA.
AC O74946;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DNA polymerase alpha subunit B;
GN Name=spb70 {ECO:0000303|PubMed:15314153, ECO:0000312|PomBase:SPCC553.09c};
GN Synonyms=pol12 {ECO:0000312|PomBase:SPCC553.09c}; ORFNames=SPCC553.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA COMPLEX, INTERACTION
RP WITH ORC1 AND ORC2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-450 AND
RP ASN-527.
RX PubMed=15314153; DOI=10.1128/mcb.24.17.7419-7434.2004;
RA Uchiyama M., Wang T.S.;
RT "The B-subunit of DNA polymerase alpha-primase associates with the origin
RT recognition complex for initiation of DNA replication.";
RL Mol. Cell. Biol. 24:7419-7434(2004).
CC -!- FUNCTION: Accessory subunit of the DNA polymerase alpha complex (also
CC known as the alpha DNA polymerase-primase complex) which plays an
CC essential role in the initiation of DNA synthesis (PubMed:15314153).
CC During the S phase of the cell cycle, the DNA polymerase alpha complex
CC (composed of a catalytic subunit pol1, an accessory subunit spb70/pol12
CC and two primase subunits, the catalytic subunit spp1/pri1 and the
CC regulatory subunit spp2/pri2) is recruited to DNA at the replicative
CC forks (By similarity). The primase subunit of the polymerase alpha
CC complex initiates DNA synthesis by oligomerising short RNA primers on
CC both leading and lagging strands (By similarity).
CC {ECO:0000250|UniProtKB:P09884, ECO:0000250|UniProtKB:P20664,
CC ECO:0000269|PubMed:15314153}.
CC -!- SUBUNIT: Component of the alpha DNA polymerase complex (also known as
CC the alpha DNA polymerase-primase complex) consisting of four subunits:
CC the catalytic subunit pol1, the accessory subunit spb70/pol12, and the
CC primase complex subunits spp1/pri1 and spp2/pri2 respectively
CC (PubMed:15314153). Interacts with orc1 (PubMed:15314153). Interacts
CC with orc2; the interaction occurs on the chromatin, is stable thoughout
CC the cell cycle and is independent from spb70 role in the alpha DNA
CC polymerase complex (PubMed:15314153). {ECO:0000269|PubMed:15314153}.
CC -!- INTERACTION:
CC O74946; P28040: pol1; NbExp=2; IntAct=EBI-849056, EBI-455823;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15314153}. Chromosome
CC {ECO:0000269|PubMed:15314153}. Note=Present both in soluble and
CC chromatin-bound form. {ECO:0000269|PubMed:15314153}.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA19261.1; -; Genomic_DNA.
DR PIR; T41395; T41395.
DR RefSeq; NP_587765.1; NM_001022758.2.
DR AlphaFoldDB; O74946; -.
DR SMR; O74946; -.
DR BioGRID; 275707; 8.
DR ComplexPortal; CPX-2092; DNA polymerase alpha:primase complex.
DR IntAct; O74946; 3.
DR STRING; 4896.SPCC553.09c.1; -.
DR MaxQB; O74946; -.
DR PaxDb; O74946; -.
DR EnsemblFungi; SPCC553.09c.1; SPCC553.09c.1:pep; SPCC553.09c.
DR GeneID; 2539135; -.
DR KEGG; spo:SPCC553.09c; -.
DR PomBase; SPCC553.09c; spb70.
DR VEuPathDB; FungiDB:SPCC553.09c; -.
DR eggNOG; KOG1625; Eukaryota.
DR HOGENOM; CLU_014923_1_0_1; -.
DR InParanoid; O74946; -.
DR OMA; PFLDIEH; -.
DR PhylomeDB; O74946; -.
DR Reactome; R-SPO-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-SPO-68952; DNA replication initiation.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR Reactome; R-SPO-69091; Polymerase switching.
DR Reactome; R-SPO-69166; Removal of the Flap Intermediate.
DR Reactome; R-SPO-69183; Processive synthesis on the lagging strand.
DR PRO; PR:O74946; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IPI:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0061806; P:regulation of DNA recombination at centromere; IMP:PomBase.
DR GO; GO:1902981; P:synthesis of RNA primer involved in mitotic DNA replication; IC:PomBase.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR InterPro; IPR016722; DNA_pol_alpha_bsu.
DR InterPro; IPR013627; Pol_alpha_B_N.
DR PANTHER; PTHR23061; PTHR23061; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
DR Pfam; PF08418; Pol_alpha_B_N; 1.
DR PIRSF; PIRSF018300; DNA_pol_alph_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..574
FT /note="DNA polymerase alpha subunit B"
FT /id="PRO_0000194040"
FT MUTAGEN 450
FT /note="F->L: Loss of interaction with orc2; when associated
FT with H-527."
FT /evidence="ECO:0000269|PubMed:15314153"
FT MUTAGEN 527
FT /note="N->H: Loss of interaction with orc2; when associated
FT with L-450."
FT /evidence="ECO:0000269|PubMed:15314153"
SQ SEQUENCE 574 AA; 64185 MW; 18C17FCFA7AA098A CRC64;
MEFPIDDEEL LDERNKLLQI CNMDEQTMFY KWESWCLQRG NTPKLDLDTF KAFAKDMKFQ
MERQVKATLK QNPERKSIKQ IPGMNIDSIL GLPVKTTASG DSLMQESKPS TETFELNSSD
AGRVLEVLNK ELKIVTSKPS APSKLVIVAN FDLKAFNYRI MYQKLYDSSE VLDDRIELFS
ALTCRKYNIS DEDLANPSEL TQEPVVVVGR IVVESTNLGG RLNQNSILLE SSRRLGAGVR
VRLKVDDLPS YSIFPGQIVS VKGSNPSGNM FIAKEILPIP PLPFPSSSKQ EHATFVANTN
NQPISIYIAS GPWSLRDDLS FSPLKSMISY VNKNPVDLVI LCGPFLDINH ILIRTGNITG
TSATSLEELF KERVTPILSQ LTCPCILIPH INDAASDHPA WPQDAFNRVA LGLPSNFKCF
PNPCMFSIND VVFGVSTNDI LLHTSREELF RLPSHGNLFA RLVSHVLHQR HFYPLFPGGS
LEKCNPSNLD IAHLKLGEFL NTMPDILILP SDLRYFVKNV ENVVSLNPGK ATKGINLGTF
AKLTIAPLEL GDNGSSNHYS HRVWLRTKAE ILKL
