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Database: UniProt
Entry: A0A2Y9K2S9_ENHLU
LinkDB: A0A2Y9K2S9_ENHLU
Original site: A0A2Y9K2S9_ENHLU 
ID   A0A2Y9K2S9_ENHLU        Unreviewed;       992 AA.
AC   A0A2Y9K2S9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=LOC111153203 {ECO:0000313|RefSeq:XP_022367787.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022367787.1};
RN   [1] {ECO:0000313|RefSeq:XP_022367787.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022367787.1};
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_022367787.1; XM_022512079.1.
DR   AlphaFoldDB; A0A2Y9K2S9; -.
DR   Proteomes; UP000248482; 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:UP000248482};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          940..981
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          76..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..530
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..690
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  108872 MW;  0F2F2E2E1811463E CRC64;
     MPSLKFLMSQ WTPEYNKLYT LKVDMKSEIP SDAPKTQESL KGILLHPEPI GAAKSFPAGV
     EMINSKVGNE FSHLCDDSQK QEKDMNGNQQ EQEKSVVVRK KRKSQQAGPS YMQNCVKENQ
     GILGLRQHLE TPSDEDNDSS FSDCLSSPSS SLHFGDSDTV TSDEDKEVSV RHSQAILSAK
     SRTHSARSQK WPRTETESVS GLLMKRPCFH SSSLRRLPCR KRFVKNNSSQ RTQKQKERIL
     MQRKKREVLA RRKYALLPTS SSSSENDLSS ESSSSSSTEG EEDLFVSTSE NHQNNPTVPS
     GSIDEDVVVI EASSTPQVTA NEEINVTSTD SEVEIVTVGE SYRSRSTLGH SRSHWSQGSN
     SHTSRPQEPR NRSRISTVIQ PLRQNAAEVV DLTVDEDEPT VVPTTSARME SQTTSTSINN
     SNPSTSEQAS DAASAVTGSQ PSIVSETSAT LTSNSMTGTS IGDDSRRTSS SAVTETGPPA
     MPRLPSCCPQ HSPCGGSSQN HHALGHPHTS CFQQHGHHFQ HHHHHHHTPH PPVPVSPSFS
     DSTCPVERPP QVQAPCGANS SSGTSYHDQQ ALPVDLSNNG IRSHGNGGFH GASAFDPCCP
     VSSSRAAIFG HQAAAAAPSQ PLSIDGYGSS MVAQPQPQPP PQASLSSCRH YMPPPYASLT
     RPLHHQASAC PHSHGNPPPP TQPPPQVDYV IPHPVHAFHS QISSHATSHP VAPPPPTHLA
     STAAPIPQHL PPTHQPISHH IPATAPPAQR LHPHEVMQRM EVQRRRMMQH PTRAHERPPP
     HPHRMHPNYG HGHHIHVPQT MSSHPRQAPE RSAWELGIEA GVTAATYTPG ALHPHLAHYH
     APPRLHHLQL GALPLMVPDM AGYPHIRYIS SGLDGTSFRG PFRGNFEELI HLEERLGNVN
     RGASQGTIER CTYPHKYKKR KLHCKQDGEE GTEEDTEEKC TICLSILEEG EDVRRLPCMH
     LFHQVCVDQW LITNKKCPIC RVDIEAQLPS ES
//
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