ID   RPR1A_CHICK             Reviewed;         268 AA.
AC   Q5ZM30;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Regulation of nuclear pre-mRNA domain-containing protein 1A;
DE   AltName: Full=Cyclin-dependent kinase inhibitor 2B-related protein;
DE   AltName: Full=p15INK4B-related protein;
GN   Name=RPRD1A; Synonyms=P15RS; ORFNames=RCJMB04_3f10;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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:0000250|UniProtKB:Q96P16}.
CC   -!- SUBUNIT: May form a heterodimer with RPRD1B. Associates with the RNA
CC       polymerase II subunit POLR2A (via CTD phosphorylated at 'Ser-2' and
CC       'Ser-7' of the heptad repeats). {ECO:0000250|UniProtKB:Q96P16}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96P16}.
CC   -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family. {ECO:0000305}.
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DR   EMBL; AJ719554; CAG31213.1; -; mRNA.
DR   RefSeq; NP_001026176.1; NM_001031005.2.
DR   AlphaFoldDB; Q5ZM30; -.
DR   SMR; Q5ZM30; -.
DR   STRING; 9031.ENSGALP00000021401; -.
DR   PaxDb; Q5ZM30; -.
DR   PRIDE; Q5ZM30; -.
DR   GeneID; 420953; -.
DR   KEGG; gga:420953; -.
DR   CTD; 55197; -.
DR   VEuPathDB; HostDB:geneid_420953; -.
DR   eggNOG; KOG2669; Eukaryota.
DR   InParanoid; Q5ZM30; -.
DR   PhylomeDB; Q5ZM30; -.
DR   PRO; PR:Q5ZM30; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISS:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR   GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IBA:GO_Central.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR006569; CID_dom.
DR   InterPro; IPR032337; CREPT.
DR   InterPro; IPR008942; ENTH_VHS.
DR   Pfam; PF04818; CID; 1.
DR   Pfam; PF16566; CREPT; 1.
DR   SMART; SM00582; RPR; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   PROSITE; PS51391; CID; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..268
FT                   /note="Regulation of nuclear pre-mRNA domain-containing
FT                   protein 1A"
FT                   /id="PRO_0000311347"
FT   DOMAIN          1..133
FT                   /note="CID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
SQ   SEQUENCE   268 AA;  30836 MW;  9E066A613F247AB2 CRC64;
     MSAFSEAALE RKLSELSNSQ QSVQTLSLWL IHHRKHSALI VSVWERELRK AKPNRKLTFL
     YLANDVIQNS KRKGPEFTKD FAPVIVEAFK HVSSESDESC KKHPGRVLSI WEERSVYEND
     VLEQLRQALY GDRKVRKRTY EQIKVDENNC SPRSSPTDPP QTMDLIRALQ ELENAASGDA
     AVHQRIASLP IEVQDVSLLD RITDKESGEQ LSKMVDDACM LLADYNGRLA AEIDDRKQLT
     RMLSDFLRCQ KEFLAEKEHK LEVRIVLF