ID   RPR1A_BOVIN             Reviewed;         312 AA.
AC   Q0P5J9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 90.
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;
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 GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0P5J9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0P5J9-2; Sequence=VSP_029529, VSP_029530;
CC   -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC119944; AAI19945.1; -; mRNA.
DR   RefSeq; NP_001068624.1; NM_001075156.1. [Q0P5J9-2]
DR   RefSeq; XP_005224014.1; XM_005223957.3. [Q0P5J9-1]
DR   RefSeq; XP_010816978.1; XM_010818676.2. [Q0P5J9-1]
DR   AlphaFoldDB; Q0P5J9; -.
DR   SMR; Q0P5J9; -.
DR   STRING; 9913.ENSBTAP00000007226; -.
DR   PaxDb; Q0P5J9; -.
DR   PRIDE; Q0P5J9; -.
DR   Ensembl; ENSBTAT00000007226; ENSBTAP00000007226; ENSBTAG00000005497. [Q0P5J9-1]
DR   Ensembl; ENSBTAT00000056481; ENSBTAP00000048688; ENSBTAG00000005497. [Q0P5J9-2]
DR   GeneID; 504355; -.
DR   KEGG; bta:504355; -.
DR   CTD; 55197; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005497; -.
DR   eggNOG; KOG2669; Eukaryota.
DR   GeneTree; ENSGT00950000183094; -.
DR   HOGENOM; CLU_055523_1_0_1; -.
DR   InParanoid; Q0P5J9; -.
DR   OMA; MAYNDDA; -.
DR   OrthoDB; 1091009at2759; -.
DR   TreeFam; TF320926; -.
DR   Proteomes; UP000009136; Chromosome 24.
DR   Bgee; ENSBTAG00000005497; Expressed in occipital lobe and 108 other tissues.
DR   ExpressionAtlas; Q0P5J9; baseline and differential.
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   Acetylation; Alternative splicing; Coiled coil; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96P16"
FT   CHAIN           2..312
FT                   /note="Regulation of nuclear pre-mRNA domain-containing
FT                   protein 1A"
FT                   /id="PRO_0000311343"
FT   DOMAIN          2..133
FT                   /note="CID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT   COILED          244..286
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96P16"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96P16"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96P16"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96P16"
FT   VAR_SEQ         264..270
FT                   /note="EYKRKLA -> VRNLFLI (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_029529"
FT   VAR_SEQ         271..312
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_029530"
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