ID A0A1S3A9S7_ERIEU Unreviewed; 934 AA.
AC A0A1S3A9S7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Regulation of nuclear pre-mRNA domain-containing protein 2 isoform X3 {ECO:0000313|RefSeq:XP_007531621.1};
GN Name=RPRD2 {ECO:0000313|RefSeq:XP_007531621.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007531621.1};
RN [1] {ECO:0000313|RefSeq:XP_007531621.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_007531621.1; XM_007531559.2.
DR AlphaFoldDB; A0A1S3A9S7; -.
DR CTD; 23248; -.
DR OrthoDB; 1989419at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IEA:InterPro.
DR CDD; cd17001; CID_RPRD2; 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; IPR047885; RPRD2_CID.
DR PANTHER; PTHR12460; CYCLIN-DEPENDENT KINASE INHIBITOR-RELATED PROTEIN; 1.
DR PANTHER; PTHR12460:SF40; REGULATION OF NUCLEAR PRE-MRNA DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF04818; CID; 1.
DR SMART; SM00582; RPR; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR PROSITE; PS51391; CID; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT DOMAIN 19..149
FT /note="CID"
FT /evidence="ECO:0000259|PROSITE:PS51391"
FT REGION 286..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 100309 MW; 53805EE630171304 CRC64;
MAAGGGGGSG KASSSSASSA GALESSLDRK FQSVTNTMES IQGLSSWCIE NKKHHGTIVY
HWMKWLRRSA YPHRLNLFYL ANDVIQNCKR KNAIIFRESF ADVLPEAAAL VKDPSVSKSV
ERIFKIWEDR NVYPEEMIMA LREALTSTNP KAALKSKIVA EFRSQALIEE LLLYKRSEDQ
IELKEKQLST MRVDVCSTET LKCLKDKTGG KKFSKEFEEA SSKLEEFVNG LDKQVKNGPS
LTEALENAGI FYEAQYKEVK VVANAYKTFA NRVNNLKKKL DQLKATLPDP EESPVPSPSM
DAPSPTGSES PFQGMGGEES RSPAMESEKS ATPEPATDNR DVEDMELSDV EDDGSKIIVE
DRKEKPVEKS AVSTSVPTKP TESVSKTPSS TPVPVTVTAT PPPPKSVNTT LLSPSPALTL
PNLANVDLAK ISSILSSLTS VMKNTGVSPA PRPPGTPTSP SNLTTGAKTP APATTTSHNP
LANILSKVEI TPESILSALS KTQTQSAPTL QGLSSLLQSV TGNPVPTSEA APQSTSASPA
NTTVSSVKGR SLPSNTQTFM PKSFNYSPNS STSEVSSTSA SKTSVGQSPG LPSTTFKLPS
NSLGFTGTHN TSSAVPPAEV AMCQPSDISK PKLESESTSP SLEMKIHNFL KGNPGFSGLN
LNIPILSSLG SSTPAESHSS DFQRGPTSTS VDNVDGTPVR DERSGTPTQD EMMDKPTSSS
VDTMSLLSKI ISPGSSTPSS TRSPPPGREE NYPRELSNSV STYRPFGLGS DSPYKQPSEG
VERPSSLMES SQEKFFPDTS FQEDEDYRDF EYSGPPPSAM MNLEKKPAKS ILKSSKLSDA
TEFQPILSSY SHRAQDFSVK SAFPPSVRSL LDATENCDRL SSSPGLFGTF NIRGTEPGPD
RSPSPKHPCH SHGPPTHIGR GESPGLRHFY YINN
//