ID A0A1S3EP08_DIPOR Unreviewed; 1008 AA.
AC A0A1S3EP08;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=Rnf111 {ECO:0000313|RefSeq:XP_012865695.1};
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_012865695.1};
RN [1] {ECO:0000313|RefSeq:XP_012865695.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012865695.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the Arkadia family.
CC {ECO:0000256|ARBA:ARBA00007622}.
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DR RefSeq; XP_012865695.1; XM_013010241.1.
DR AlphaFoldDB; A0A1S3EP08; -.
DR GeneID; 105981176; -.
DR KEGG; dord:105981176; -.
DR CTD; 54778; -.
DR InParanoid; A0A1S3EP08; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16681; RING-H2_RNF111; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029306; RNF111_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16200:SF1; E3 UBIQUITIN-PROTEIN LIGASE PLR-1-RELATED; 1.
DR PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR Pfam; PF15303; RNF111_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 956..997
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 64..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..521
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..757
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 110289 MW; 18336E9774E3F0E5 CRC64;
MCQWTPECNK LFILNVAMKS EVPADAPKTQ ESLKGILLPP QPIGAAKSFP SGVEMIHSKV
GNEFSHLCDD PQKQEKDMNG NQQEREKSVR KKRKSQQAGP SYMQNCVKEN QGILGLRQHL
ETASEDDHDS SFSDCLSSPS SSLHFGDSDT VTSDEDKEVS VRHSQPVLNT KTRSHSARSQ
KWPRTETETV SGLLMKRPCF HSSSLRRLPC RKRFIKSNSS QRTQKQKERI LMQRKKREVL
ARKKYALLPS SSSSSENDLS SESSSSSSTE GEEDLFVSAS ENHQNNPAAP SGSIDEDVVV
IETSFAPQVT ANEEINVTST DSEVEIVTVG ESYRSRSTLG HSRSHWSQGS SSHTGRTQEP
RNRSRISTVI QPLRQNAAEV VDLTVDEDEP TVVPTTSARA DSQTTSASIT NSNPSTSEQA
SDTAPAVSSS QPSTAAETSA TLTSNSTAGS SAGDDSRRTA SSAVTEPGPP AMPRLPSCCP
QHSPCGGSSQ NHHALGHPHT SCFQQHSHHF QHHHHHHHTP HPAVPVSPSF SDPTCPVERP
PQVPAPCGAN SSSSSSYHDQ QALPVDLSSS GIRSHGSGGF HGASAFDPCC PVSSSRAAIF
GHQAAAAAPS QPLSIDGYGS SMVAQPQPQP PPQPSLSSCR HYMPPPWVAP VYTPHWGSVN
ENEDASLTRP LHHQASACPH SHGNPPPQTQ PPPPVDYVIP HPVHAFHSQI SSHATSHPVA
PPPPTHLSTA AAPVPQHLPP THQPISHHLP APAPPAQRLH PHEMMQRMEV QRRRMMQHPT
RAHERPPPHP HRMHPNYGHG HHIHVPQTMS SHPRQAPERS AWELGIEAGV TAATYTPGAL
HPHLAHYHAP PRLHHLQLGA LPLMVPDMAG YPHIRYISSG LDGTSFRGPF RGNFEELIHL
EERLGNVNRG ASQGTIERCT YPHKYKKVTT DWFSQRKLHC KQDGEEGTEE DTEEKCTICL
SILEEGEDVR RLPCMHLFHQ VCVDQWLITN KKCPICRVDI EAQLPSES
//
