ID A0A1S3PTG2_SALSA Unreviewed; 242 AA.
AC A0A1S3PTG2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=E3 ubiquitin-protein ligase RNF166 {ECO:0000256|ARBA:ARBA00039320};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING finger protein 166 {ECO:0000256|ARBA:ARBA00041621};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF166 {ECO:0000256|ARBA:ARBA00041350};
GN Name=LOC106587267 {ECO:0000313|RefSeq:XP_014030983.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014030983.1};
RN [1] {ECO:0000313|RefSeq:XP_014030983.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014030983.1};
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}.
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DR RefSeq; XP_014030983.1; XM_014175508.1.
DR AlphaFoldDB; A0A1S3PTG2; -.
DR GeneID; 106587267; -.
DR OrthoDB; 26661at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000087266; Chromosome ssa26.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16549; RING-HC_RNF166; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR034734; ZF_C2HC_RNF.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46016:SF4; E3 UBIQUITIN-PROTEIN LIGASE RNF166; 1.
DR PANTHER; PTHR46016; ZINC FINGER, RING/FYVE/PHD-TYPE; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF18574; zf_C2HC_14; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS51803; ZF_C2HC_RNF; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 38..78
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 103..122
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000259|PROSITE:PS51803"
SQ SEQUENCE 242 AA; 26846 MW; 73296A10989FA69E CRC64;
MMAMFRSFVS ATHQLRQHQQ NGAAAAATGE SLESQFSCPI CLEVYHKPVI IGSCAHTFCG
ECLQPCLQVT SPLCPLCRMP FDPKKVDKSS SVEKQLSNYK APCRGCSKKV SLVKMRSHIS
SCAKVQEQMA NCPKFVPVVP TSQPIPSNIP NRSTFSCPFC GARNLDQQEL VKHCMENHRN
DPNKVVCPVC SAMPWGDPSY KSSNFLQHLL HRHKFSYDTF VDYSIDEEAA LQAALALSMA
EN
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