DPOA2_BOVIN
ID DPOA2_BOVIN Reviewed; 604 AA.
AC Q58D13;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=DNA polymerase alpha subunit B;
DE AltName: Full=DNA polymerase alpha 70 kDa subunit;
GN Name=POLA2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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 (By similarity).
CC During the S phase of the cell cycle, the DNA polymerase alpha complex
CC (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and
CC two primase subunits, the catalytic subunit PRIM1 and the regulatory
CC subunit PRIM2) is recruited to DNA at the replicative forks via direct
CC interactions with MCM10 and WDHD1 (By similarity). The primase subunit
CC of the polymerase alpha complex initiates DNA synthesis by
CC oligomerising short RNA primers on both leading and lagging strands.
CC These primers are initially extended by the polymerase alpha catalytic
CC subunit and subsequently transferred to polymerase delta and polymerase
CC epsilon for processive synthesis on the lagging and leading strand,
CC respectively (By similarity). {ECO:0000250|UniProtKB:P09884,
CC ECO:0000250|UniProtKB:P20664, ECO:0000250|UniProtKB:Q14181}.
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 POLA1, the regulatory subunit POLA2, and the
CC primase complex subunits PRIM1 and PRIM2 respectively (By similarity).
CC Within the complex, POLA1 directly interacts with PRIM2 (By
CC similarity). {ECO:0000250|UniProtKB:P20664,
CC ECO:0000250|UniProtKB:Q14181}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The N-terminal 240 amino acids are sufficient to mediate
CC complex formation.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner, in G2/M phase.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC {ECO:0000305}.
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DR EMBL; BT021784; AAX46631.1; -; mRNA.
DR RefSeq; NP_001019713.2; NM_001024542.2.
DR AlphaFoldDB; Q58D13; -.
DR SMR; Q58D13; -.
DR CORUM; Q58D13; -.
DR STRING; 9913.ENSBTAP00000015221; -.
DR BindingDB; Q58D13; -.
DR ChEMBL; CHEMBL5259; -.
DR PaxDb; Q58D13; -.
DR GeneID; 514793; -.
DR KEGG; bta:514793; -.
DR CTD; 23649; -.
DR eggNOG; KOG1625; Eukaryota.
DR InParanoid; Q58D13; -.
DR PRO; PR:Q58D13; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.530; -; 1.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR InterPro; IPR043034; DNA_pol_alpha_B_N_sf.
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 2: Evidence at transcript level;
KW DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..604
FT /note="DNA polymerase alpha subunit B"
FT /id="PRO_0000371218"
FT REGION 109..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
SQ SEQUENCE 604 AA; 66955 MW; 2AB9B8FDB4B821F5 CRC64;
MAVSAQLLVE ELQIFGLECE EAVIEKLVEL CILYGQNEEG MASELIAFCT STRKDCFTLE
TLNSFEHEFL SKRVSKTRHG ASKDKGLRHA GARDIVSIQE LIEVEEEEET LLNSYTTPSK
GSQKRTITTP ETPLTKRSVS ARSPHQLLSP SSFSPSATPP QKYSSRSNRG EVVTSFGSAQ
GVSWSGRGGA SPLSLKVLGH PEPLTGSYKY MFQKLPDIRE VLTCKIEELG SELKEHYKIE
AFAPILVPAQ EPVTLLGQIG CDSNGKLNHK SVILEGDLEH SSGAQIPVDL SELKEYSLFP
GQVVVMEGIN TTGRKLVATR LYEGVPLPFH QPDEEDGDSE QFMVLVACGP YTTSDSITFD
PLLDLITIIN RDRPDVCILF GPFLDAKHEQ VESCLLTSSF EDVFKQCLRT IIEGTRSSGS
HLIIVPSLRD VHHEPVYPQP PFSCSDLLRE DKKRVRLVSE PCTLSINGVI FGLTSTDLLF
HMGAEEISSS SGTSDRFSRI LRHILTQRSY YPLYPPQEDM AIDYENFYLY AQLPVTPDVF
IAPSELRYFV KVGLNSAISL QCQNQFLSGA LALNSSRVCW WGQWPRSFGG GVGVENKSVS
IMLK
