RPR1A_PONAB
ID RPR1A_PONAB Reviewed; 312 AA.
AC Q5R8Y3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family. {ECO:0000305}.
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DR EMBL; CR859614; CAH91777.1; -; mRNA.
DR RefSeq; NP_001126030.1; NM_001132558.1.
DR AlphaFoldDB; Q5R8Y3; -.
DR SMR; Q5R8Y3; -.
DR STRING; 9601.ENSPPYP00000010232; -.
DR Ensembl; ENSPPYT00000033804; ENSPPYP00000024540; ENSPPYG00000009111.
DR GeneID; 100172978; -.
DR KEGG; pon:100172978; -.
DR CTD; 55197; -.
DR eggNOG; KOG2669; Eukaryota.
DR GeneTree; ENSGT00950000183094; -.
DR HOGENOM; CLU_055523_1_0_1; -.
DR InParanoid; Q5R8Y3; -.
DR OMA; MAYNDDA; -.
DR OrthoDB; 1091009at2759; -.
DR TreeFam; TF320926; -.
DR Proteomes; UP000001595; Chromosome 18.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISS:UniProtKB.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
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; Coiled coil; Nucleus; Phosphoprotein; 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_0000311346"
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"
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