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Database: UniProt
Entry: W5QI47_SHEEP
LinkDB: W5QI47_SHEEP
Original site: W5QI47_SHEEP 
ID   W5QI47_SHEEP            Unreviewed;       986 AA.
AC   W5QI47;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
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|Ensembl:ENSOARP00000022398.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000022398.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000022398.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000022398.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000022398.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AMGL01103234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5QI47; -.
DR   SMR; W5QI47; -.
DR   STRING; 9940.ENSOARP00000022398; -.
DR   PaxDb; 9940-ENSOARP00000022398; -.
DR   Ensembl; ENSOART00000022704.1; ENSOARP00000022398.1; ENSOARG00000020839.1.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_309031_0_0_1; -.
DR   OMA; FGHQATA; -.
DR   Proteomes; UP000002356; Chromosome 7.
DR   Bgee; ENSOARG00000020839; Expressed in thymus and 54 other cell types or tissues.
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:UP000002356};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          934..975
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          66..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..523
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..545
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   986 AA;  108277 MW;  3393DC130A3D37D8 CRC64;
     MSQWTPEYNK LYTLKVDMKS EIPSDAPKTQ ESLKGILLHP EPIGAAKSFP AGVEMINSKV
     GNEFSHLCDD SQKQEKDMNG NQQEQEKSVV VRKKRKSQQA GPSYMQNCAK ENQGILGLRQ
     HLETPSDEDN DSSFSDCLSS PSSSLHFGDS DTVTSDEDKE VSVRHSQAIL SAKSRTHSSR
     SHKWPRTETE SVSGLLMKRP CFHSSSLRRL PCRKRFVKNN SSQRTQKQKE RILMQRKKRE
     VLARRKYALL PSSSSSSEND LSSESSSSSS TEGEEDLFVS TSENHQNNPT VASGNIDEDV
     VVIEASSTPQ ITANEEINVT STDSEVEIVT VGESYRSRSA LGHNRSHWNQ GSSSHTSRPQ
     EPRNRNRMST VIQPLRQNAA EVVDLTVDED EPTVVPTTSA RMESQTTSAS INNSNPSTSE
     QASDTAAAVT SSQPSTVSET STTLTSNSMT GTSAGDDSRR TASNAVTETG PPAMPRLPSC
     CPQHSPCGGS SQNHHALGHP HTSCFQQHGH HFQHHHHHHH TPHPAVPVSP SFSDPTCPVE
     RPPQVQPPCG ANSTSSTSYH DQQALPVDLS SSGIRSHGSA GFHGASAFDP CCPVSSSRAA
     IFGHQAAAAA APSQPLSIDG YGSSMVAQPQ PQPPPQASLS SCRHYMPPPY ASLTRPLHHQ
     TSACPHSHGN PPPQTQPPPQ VDYVIPHPVH AFHSQISSHA TSHPVAPPPP THLASTAAPI
     PQHLPPTHQP ISHHIPTTAP PAQRLHPHEM MQRMEVQRRR MMQHPTRAHE RPPPHPHRMH
     PNYGHGHHIH VPQTMSSHPR QAPERSAWEL GIEAGVTAAT YTPGALHPHL AHYHAPPRLH
     HLQLGALPLM VPDMAGYPHI RYISSGLDGT SFRGPFRGNF EELIHLEERL GNVNRGASQG
     TIERCTYPHK YKKRKLHCKQ DGEEGTEEDT EEKCTICLSI LEEGEDVRRL PCMHLFHQVC
     VDQWLITNKK CPICRVDIEA QLPSES
//
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