ID A0A1U7SIT5_ALLSI Unreviewed; 338 AA.
AC A0A1U7SIT5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=E3 ubiquitin-protein ligase RNF170 {ECO:0000256|ARBA:ARBA00014068};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING finger protein 170 {ECO:0000256|ARBA:ARBA00031107};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF170 {ECO:0000256|ARBA:ARBA00030110};
GN Name=RNF170 {ECO:0000313|RefSeq:XP_006036511.2};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006036511.2};
RN [1] {ECO:0000313|RefSeq:XP_006036511.2}
RP IDENTIFICATION.
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: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_006036511.2; XM_006036449.3.
DR AlphaFoldDB; A0A1U7SIT5; -.
DR STRING; 38654.A0A1U7SIT5; -.
DR GeneID; 102384645; -.
DR KEGG; asn:102384645; -.
DR CTD; 81790; -.
DR eggNOG; KOG2164; Eukaryota.
DR InParanoid; A0A1U7SIT5; -.
DR OrthoDB; 154493at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR CDD; cd16553; RING-HC_RNF170; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR010652; DUF1232.
DR InterPro; IPR038896; RNF170.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22894:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF170; 1.
DR PANTHER; PTHR22894; UNCHARACTERIZED; 1.
DR Pfam; PF06803; DUF1232; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 169..212
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 38627 MW; 2E6821ACBBD1B1FE CRC64;
MQRLSRRAPD RRHLGDTEGS WVRPPSRAPL PFAASPFSAS LPHGFAKVFA SWSVGFGWQT
GKNVPWRLLT SDFPKTYFTR PGMASQQAEV QSLKLSNDSI IEGVSDQVLV AVVLSFSFIA
ALVYMLLRNE HQNIHPENQE LVRALRQQLQ TEQDESAGDR HHFYTDMSCP VCLQQATFPI
ETNCGHLFCG ACIIAYWRYG SWLGAIRCPI CRQTVTLFLP LFGEDQPDAA QVLQDVSDYN
RRFSGQPRSI MERIMDLPTL LRHAFREMFS VGGLFWMFRI RIFLCLLGAL LYLASPLDFL
PEALFGILGF LDDFFVIFLL LIYISIMYRE VVTQRLNR
//
