ID F7GW04_CALJA Unreviewed; 312 AA.
AC F7GW04; F7H026;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Regulation of nuclear pre-mRNA domain-containing protein {ECO:0000256|RuleBase:RU369021};
GN Name=RPRD1A {ECO:0000313|EMBL:JAB06288.1,
GN ECO:0000313|Ensembl:ENSCJAP00000039171.2};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB06288.1};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000039171.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB06288.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB06288.1}, Cerebellum
RC {ECO:0000313|EMBL:JAB47689.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB32090.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB18803.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB35341.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000039171.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat
CC domain (CTD) of the largest RNA polymerase II subunit POLR2A, and
CC participates in dephosphorylation of the CTD by RPAP2. May act as a
CC negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the
CC cell cycle. {ECO:0000256|ARBA:ARBA00035622}.
CC -!- SUBUNIT: Associates with the RNA polymerase II complex.
CC {ECO:0000256|RuleBase:RU369021}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family.
CC {ECO:0000256|ARBA:ARBA00034310, ECO:0000256|RuleBase:RU369021}.
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DR EMBL; GAMT01005574; JAB06287.1; -; mRNA.
DR EMBL; GAMT01005573; JAB06288.1; -; mRNA.
DR EMBL; GAMS01004333; JAB18803.1; -; mRNA.
DR EMBL; GAMS01004332; JAB18804.1; -; mRNA.
DR EMBL; GAMR01001842; JAB32090.1; -; mRNA.
DR EMBL; GAMR01001841; JAB32091.1; -; mRNA.
DR EMBL; GAMQ01006510; JAB35341.1; -; mRNA.
DR EMBL; GAMP01005066; JAB47689.1; -; mRNA.
DR EMBL; GAMP01005065; JAB47690.1; -; mRNA.
DR RefSeq; XP_008977964.1; XM_008979716.1.
DR STRING; 9483.ENSCJAP00000039171; -.
DR Ensembl; ENSCJAT00000041380.4; ENSCJAP00000039171.2; ENSCJAG00000021044.5.
DR GeneID; 100392118; -.
DR KEGG; cjc:100392118; -.
DR CTD; 55197; -.
DR eggNOG; KOG2669; Eukaryota.
DR GeneTree; ENSGT00950000183094; -.
DR HOGENOM; CLU_055523_1_0_1; -.
DR OMA; LWMQRLK; -.
DR OrthoDB; 1989419at2759; -.
DR TreeFam; TF320926; -.
DR Proteomes; UP000008225; Chromosome 13.
DR Bgee; ENSCJAG00000021044; Expressed in frontal cortex and 6 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0097550; C:transcription preinitiation complex; IEA:Ensembl.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IEA:InterPro.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR GO; GO:0001111; P:RNA polymerase II promoter clearance; IEA:Ensembl.
DR CDD; cd17011; CID_RPRD1A; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 6.10.250.2560; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR032337; RPRD1A/B_C.
DR InterPro; IPR047884; RPRD1A_CID.
DR PANTHER; PTHR12460; CYCLIN-DEPENDENT KINASE INHIBITOR-RELATED PROTEIN; 1.
DR PANTHER; PTHR12460:SF2; REGULATION OF NUCLEAR PRE-MRNA DOMAIN-CONTAINING PROTEIN 1A; 1.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF16566; CREPT; 1.
DR SMART; SM00582; RPR; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR PROSITE; PS51391; CID; 1.
PE 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|RuleBase:RU369021};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|RuleBase:RU369021};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT DOMAIN 1..133
FT /note="CID"
FT /evidence="ECO:0000259|PROSITE:PS51391"
FT COILED 248..282
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 312 AA; 35720 MW; 61785281F31CB328 CRC64;
MSAFSEAALE KKLSELSNSQ QSVQTLSLWL IHHRKHSRPI VTVWERELRK AKPNRKLTFL
YLANDVIQNS KRKGPEFTKD FAPVIVEAFK HVSSETDESC KKHLGRVLSI WEERSVYEND
VLEQLKQALY GDKKPRKRTY EQIKVDENEN CSSLGSPSEP PQTLDLVRAL QDLENAASGD
AAVHQRIASL PVEVQEVSLL DKITDKESGE RLSKMVEDAC MLLADYNGRL AAEIDDRKQL
TRMLADFLRC QKEALAEKEH KLEEYKRKLA RVSLVRKELR SRIQSLPDLS RLPNVTGSHM
HLPFAGDIYS ED
//
