ID A0A1S3F3N8_DIPOR Unreviewed; 934 AA.
AC A0A1S3F3N8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Regulation of nuclear pre-mRNA domain-containing protein 2 isoform X3 {ECO:0000313|RefSeq:XP_012870719.1};
GN Name=Rprd2 {ECO:0000313|RefSeq:XP_012870719.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012870719.1};
RN [1] {ECO:0000313|RefSeq:XP_012870719.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012870719.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family.
CC {ECO:0000256|ARBA:ARBA00034310}.
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DR RefSeq; XP_012870719.1; XM_013015265.1.
DR AlphaFoldDB; A0A1S3F3N8; -.
DR GeneID; 105984913; -.
DR CTD; 23248; -.
DR OrthoDB; 1989419at2759; -.
DR Proteomes; UP000081671; 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; IPR032337; RPRD1A/B_C.
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 Pfam; PF16566; CREPT; 1.
DR SMART; SM00582; RPR; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR PROSITE; PS51391; CID; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT DOMAIN 19..149
FT /note="CID"
FT /evidence="ECO:0000259|PROSITE:PS51391"
FT REGION 285..392
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 523..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..332
FT /note="Polar residues"
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 370..392
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..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 100325 MW; 44425D55B2ACE966 CRC64;
MAAGGGGGSS KASSSSASSA GALESSLDRK FQSVTNTMES IQGLSSWCIE NKKHHSTIVY
HWMKWLRRSA YPHRLNLFYL ANDVIQNCKR KNAIIFRESF ADVLPEAAAL VKDPSVSKSI
ERIFKIWEDR NVYPEEMIVA LREALTSSNP KAALKSKIVA EFRSQALIEE LLLYKRSEDQ
IELKEKQLST MRVDVCSTET LKCLKDKTGG KKFSKEFEEA SSKLEEFVNG LDKQVKNGPS
LTEALENAGI FYEAQYKEVK VVANAYKTFA NRVNNLKKKL DQLKSTLPDP EESPVPSPSM
DAPSPTGSES PFQGMGGEES QSPTMESEKS ATPEPVTDNR DVEDMELSDV EDDGSKIIVE
DRKEKPMEKS VSTSVPTKPT ESTSKASSCA PVPVTMTATP PLAKPVNTTL LPSSPALALP
NLANVDLAKI SSILSSLTSV MKNTGVSPAS RPSPGTPTSP SNITSGLKPP APATTTSHNP
LANILSKVEI TPESILSALS KTQTQSAPAL QGLSSLLQSV TGNPVPATEA ASQNISSSPA
NTTVSTIKGR NLPSNAQSFI PKSFSYSPNS STSEVSSTSA NKASIGHNPG LPSTTFKLPA
NSLGFTGTHN SSPAAPPTEV AICQSSEVSK PKLESESTSP SLEMKIHNFL KGNPGFSGLN
LNIPILSSLG SSASTESHPS DMQRGPTSTS MDNIDGTPVR DERSGTPTQD EMMDKPTSSS
VDTMSLLSKI ISPGSSTPSS TRSPPPGREE SYSRELSNSS STYRPFGLGS ESPYKQSSDG
MERPSSLMDS SQEKFFPDTS FQEDEDYRDF EYSGPPPSAM MNLEKKPAKS ILKSSKLADA
TEYQPILSSY SHRAQEFGVK SAFPPSVRAL LDSSENCDRL SSSPGLFGAF NIRGNEPGSD
RSPSPKYPCS SHGPPTRIRH GESPGLHHFY HLDD
//