ID GLD2_BOVIN Reviewed; 484 AA. AC Q2HJ44; Q1JPF9; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 19. DE RecName: Full=Poly(A) RNA polymerase GLD2; DE EC=2.7.7.19; DE AltName: Full=PAP-associated domain-containing protein 4; GN Name=PAPD4; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=Hereford; TISSUE=Uterus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive CC AMP monomers to the 3'-end of specific RNAs, forming a poly(A) CC tail. In contrast to the canonical nuclear poly(A) RNA polymerase, CC it only adds poly(A) to selected cytoplasmic mRNAs (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1). CC -!- SUBUNIT: Interacts with CPEB1, CPEB2, CPSF1 and PABPC1 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q2HJ44-1; Sequence=Displayed; CC Name=2; CC IsoId=Q2HJ44-2; Sequence=VSP_034322, VSP_034323; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2 CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BT025394; ABF57350.1; -; mRNA. DR EMBL; BC113319; AAI13320.1; -; mRNA. DR IPI; IPI00702849; -. DR IPI; IPI00843674; -. DR RefSeq; NP_001039826.1; -. DR UniGene; Bt.92095; -. DR Ensembl; ENSBTAG00000006751; Bos taurus. DR GeneID; 533862; -. DR KEGG; bta:533862; -. DR HOVERGEN; Q2HJ44; -. DR OMA; Q2HJ44; NQKTEAR. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0043631; P:RNA polyadenylation; ISS:UniProtKB. DR InterPro; IPR002058; PAP_assoc. DR Pfam; PF03828; PAP_assoc; 1. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Cytoplasm; mRNA processing; KW Nucleotide-binding; Nucleus; Transferase. FT CHAIN 1 484 Poly(A) RNA polymerase GLD2. FT /FTId=PRO_0000341548. FT MOTIF 76 92 Nuclear localization signal (Potential). FT ACT_SITE 215 215 By similarity. FT VAR_SEQ 157 163 SQQILEL -> NKRTLTW (in isoform 2). FT /FTId=VSP_034322. FT VAR_SEQ 164 484 Missing (in isoform 2). FT /FTId=VSP_034323. SQ SEQUENCE 484 AA; 56051 MW; EA2345615C844818 CRC64; MFPNSILGRP PFTPNHQQHN NFFALSPSLY SHQQLIDAQF SFHNADLSRA VSLQQLTYGN VSPIQTSTSP LFRGRKRLSD EKNLPLDGKR QRFHSPHQEP TIVNHIVPLS DERRYSMSPL FHTHYVPDIV RCVPPFREIS ILEPREITLP EAKDKLSQQI LELFEACQQQ VSDLKKKELC RTELQREIQL LFPQSRLFLV GSSLNGFGTR SSDGDLCLVV KEEPCFFQVN QKTEARHILT LVHKHFCTRL SGYIERPQLI RAKVPIVKFR DKVSCVEFDL NVNNIVGIRN TFLLRTYAYL ENRVRPLVLV IKKWASHHDI NDASRGTLSS YSLVLMVLHY LQTLPEPILP SIQKIYPESF SPSIQLHLVH QAPCNVPPYL SKNESNLGDL LLGFLKYYAT EFDWNSQMIS VREAKAIPRP DGIEWRNKYI CVEEPFDGTN TARAVHEKQK FDMIKDQFLK SWHRLKNRKD LNSILPLRAA ILKR //