RPAP2_MOUSE
ID RPAP2_MOUSE Reviewed; 614 AA.
AC Q8VC34; Q3TLC8; Q3TSP8; Q3UKX0; Q8C7M5; Q8CBW8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Putative RNA polymerase II subunit B1 CTD phosphatase Rpap2;
DE EC=3.1.3.16;
DE AltName: Full=RNA polymerase II-associated protein 2;
GN Name=Rpap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Diencephalon, Hippocampus, Medulla oblongata, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Protein phosphatase that displays CTD phosphatase activity
CC and regulates transcription of snRNA genes. Recognizes and binds
CC phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain
CC (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates
CC dephosphorylation of 'Ser-5' of the CTD, thereby promoting
CC transcription of snRNA genes. {ECO:0000250|UniProtKB:Q8IXW5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Associates with the RNA polymerase II complex. Interacts with
CC transcribing RNA polymerase II phosphorylated on 'Ser-7' on CTD (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Shuttles between the cytoplasm and the nucleus in a CRM1-dependent
CC manner. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8VC34-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VC34-2; Sequence=VSP_020686, VSP_020687;
CC Name=3;
CC IsoId=Q8VC34-3; Sequence=VSP_020685;
CC Name=4;
CC IsoId=Q8VC34-4; Sequence=VSP_020682, VSP_020685;
CC Name=5;
CC IsoId=Q8VC34-5; Sequence=VSP_020683, VSP_020684;
CC -!- SIMILARITY: Belongs to the RPAP2 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00812, ECO:0000305}.
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DR EMBL; AK034418; BAC28703.1; -; mRNA.
DR EMBL; AK049889; BAC33973.1; -; mRNA.
DR EMBL; AK145830; BAE26681.1; -; mRNA.
DR EMBL; AK161901; BAE36627.1; -; mRNA.
DR EMBL; AK166574; BAE38864.1; -; mRNA.
DR EMBL; BC021895; AAH21895.1; -; mRNA.
DR CCDS; CCDS19506.1; -. [Q8VC34-1]
DR CCDS; CCDS51588.1; -. [Q8VC34-3]
DR CCDS; CCDS51589.1; -. [Q8VC34-4]
DR CCDS; CCDS71630.1; -. [Q8VC34-2]
DR CCDS; CCDS71631.1; -. [Q8VC34-5]
DR RefSeq; NP_001156933.1; NM_001163461.2. [Q8VC34-3]
DR RefSeq; NP_001156934.1; NM_001163462.2. [Q8VC34-4]
DR RefSeq; NP_001276498.1; NM_001289569.1. [Q8VC34-5]
DR RefSeq; NP_001276499.1; NM_001289570.1. [Q8VC34-2]
DR RefSeq; NP_659160.2; NM_144911.3. [Q8VC34-1]
DR RefSeq; XP_006534963.1; XM_006534900.3. [Q8VC34-5]
DR AlphaFoldDB; Q8VC34; -.
DR SMR; Q8VC34; -.
DR IntAct; Q8VC34; 1.
DR MINT; Q8VC34; -.
DR STRING; 10090.ENSMUSP00000070209; -.
DR iPTMnet; Q8VC34; -.
DR PhosphoSitePlus; Q8VC34; -.
DR EPD; Q8VC34; -.
DR MaxQB; Q8VC34; -.
DR PaxDb; Q8VC34; -.
DR PeptideAtlas; Q8VC34; -.
DR PRIDE; Q8VC34; -.
DR ProteomicsDB; 300470; -. [Q8VC34-1]
DR ProteomicsDB; 300471; -. [Q8VC34-2]
DR ProteomicsDB; 300472; -. [Q8VC34-3]
DR ProteomicsDB; 300473; -. [Q8VC34-4]
DR ProteomicsDB; 300474; -. [Q8VC34-5]
DR Antibodypedia; 46923; 64 antibodies from 20 providers.
DR DNASU; 231571; -.
DR Ensembl; ENSMUST00000065422; ENSMUSP00000070209; ENSMUSG00000033773. [Q8VC34-1]
DR Ensembl; ENSMUST00000112650; ENSMUSP00000108269; ENSMUSG00000033773. [Q8VC34-4]
DR Ensembl; ENSMUST00000112651; ENSMUSP00000108270; ENSMUSG00000033773. [Q8VC34-5]
DR Ensembl; ENSMUST00000112654; ENSMUSP00000108273; ENSMUSG00000033773. [Q8VC34-3]
DR Ensembl; ENSMUST00000112655; ENSMUSP00000108274; ENSMUSG00000033773. [Q8VC34-2]
DR GeneID; 231571; -.
DR KEGG; mmu:231571; -.
DR UCSC; uc008ymn.3; mouse. [Q8VC34-1]
DR UCSC; uc008ymq.3; mouse. [Q8VC34-5]
DR UCSC; uc033iky.1; mouse. [Q8VC34-2]
DR CTD; 79871; -.
DR MGI; MGI:2141142; Rpap2.
DR VEuPathDB; HostDB:ENSMUSG00000033773; -.
DR eggNOG; KOG4780; Eukaryota.
DR GeneTree; ENSGT00390000017965; -.
DR HOGENOM; CLU_019258_1_0_1; -.
DR InParanoid; Q8VC34; -.
DR OMA; KYVLDEQ; -.
DR OrthoDB; 1506260at2759; -.
DR PhylomeDB; Q8VC34; -.
DR TreeFam; TF331431; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 231571; 22 hits in 77 CRISPR screens.
DR ChiTaRS; Rpap2; mouse.
DR PRO; PR:Q8VC34; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VC34; protein.
DR Bgee; ENSMUSG00000033773; Expressed in animal zygote and 248 other tissues.
DR ExpressionAtlas; Q8VC34; baseline and differential.
DR Genevisible; Q8VC34; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043175; F:RNA polymerase core enzyme binding; IEA:InterPro.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; ISS:UniProtKB.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; ISS:UniProtKB.
DR GO; GO:0009301; P:snRNA transcription; ISS:UniProtKB.
DR Gene3D; 1.25.40.820; -; 1.
DR InterPro; IPR039693; Rtr1/RPAP2.
DR InterPro; IPR007308; Rtr1/RPAP2_dom.
DR InterPro; IPR038534; Rtr1/RPAP2_sf.
DR PANTHER; PTHR14732; PTHR14732; 1.
DR Pfam; PF04181; RPAP2_Rtr1; 1.
DR PROSITE; PS51479; ZF_RTR1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Hydrolase;
KW Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IXW5"
FT CHAIN 2..614
FT /note="Putative RNA polymerase II subunit B1 CTD
FT phosphatase Rpap2"
FT /id="PRO_0000250649"
FT ZN_FING 77..160
FT /note="RTR1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..68
FT /evidence="ECO:0000255"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXW5"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXW5"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5I0E6"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IXW5"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020682"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020683"
FT VAR_SEQ 78
FT /note="C -> M (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020684"
FT VAR_SEQ 569..614
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020685"
FT VAR_SEQ 569..570
FT /note="LT -> IL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020686"
FT VAR_SEQ 571..614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020687"
FT CONFLICT 201
FT /note="E -> D (in Ref. 2; AAH21895)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="K -> T (in Ref. 2; AAH21895)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="I -> V (in Ref. 1; BAE26681)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="G -> V (in Ref. 1; BAE38864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 614 AA; 68530 MW; 3029373A246478D7 CRC64;
MADSAVPCSL GPSTRASSTH RDATGTKQTR ALKRGDASKR QAELEAAIQR KVEFERKAVR
IVEQLLEENI TEEFLKECGM FITPAHYSDV VDERSIIKLC GYPLCQKKLG VIPKQKYRIS
TKTNKVYDIT ERKSFCSNFC YRASKFFETQ IPKTPVWVRE EERPPDFQLL KKGQSGSSGE
VVQFFRDAVT AADVDGSGAL EAQCDPASSS SWSERASDEE EQGFVSSLLP GNRPKAVDTR
PQPHTKSSIM RKKAAQNVDS KEGEQTVSEV TEQLDNCRLD SQEKVATCKR PLKKESTQIS
SPGPLCDRFN TSAISEHKHG VSQVTLVGIS KKSAEHFRSK FAKSNPGSGS ASGLVHVRPE
VAKANLLRVL SDTLTEWKTE ETLKFLYGQN HDSVCLKPSS ASEPDEELDE DDISCDPGSC
GPALSQAQNT LDATLPFRGS DTAIKPLPSY ESLKKETEML NLRVREFYRG RCVLNEDTTK
SQDSKESVLQ RDPSFPLIDS SSQNQIRRRI VLEKLSKVLP GLLGPLQITM GDIYTELKNL
IQTFRLSNRN IIHKPVEWTL IAVVLLLLLT PILGIQKHSP KNVVFTQFIA TLLTELHLKF
EDLEKLTMIF RTSC
