ID I3KLX1_ORENI Unreviewed; 424 AA.
AC I3KLX1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=E3 ubiquitin-protein ligase RNFT1 {ECO:0000256|ARBA:ARBA00039413};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING finger and transmembrane domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042946};
GN Name=rnft1 {ECO:0000313|Ensembl:ENSONIP00000022116.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000022116.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000022116.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts in the endoplasmic
CC reticulum (ER)-associated degradation (ERAD) pathway, which targets
CC misfolded proteins that accumulate in the endoplasmic reticulum (ER)
CC for ubiquitination and subsequent proteasome-mediated degradation.
CC Protects cells from ER stress-induced apoptosis.
CC {ECO:0000256|ARBA:ARBA00037172}.
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_003458098.2; XM_003458050.4.
DR AlphaFoldDB; I3KLX1; -.
DR Ensembl; ENSONIT00000022135.2; ENSONIP00000022116.1; ENSONIG00000017540.2.
DR GeneID; 100690418; -.
DR KEGG; onl:100690418; -.
DR CTD; 51136; -.
DR eggNOG; KOG4638; Eukaryota.
DR GeneTree; ENSGT00940000156740; -.
DR HOGENOM; CLU_039460_2_1_1; -.
DR InParanoid; I3KLX1; -.
DR OMA; GCIHSRL; -.
DR OrthoDB; 4593171at2759; -.
DR TreeFam; TF331930; -.
DR Proteomes; UP000005207; Linkage group LG10.
DR GO; GO:0016020; C: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 GO; GO:1904294; P:positive regulation of ERAD pathway; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044235; RNFT1/2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR15860:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNFT1; 1.
DR PANTHER; PTHR15860; UNCHARACTERIZED RING FINGER-CONTAINING PROTEIN; 1.
DR Pfam; PF13639; zf-RING_2; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 146..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 364..402
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..125
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"
FT COMPBIAS 19..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 47360 MW; 759A6BA2D13E8AD0 CRC64;
MKLRVQNDRS DSRRVQKLRE SPTVMQPNST ERGGHAGNGL SLTLQPELFT RAPVSGAAAS
SPESGEVRVP MTGGPGESSG GAPSRRCRIN SHSHSHSHSH AHNRAPPSSS EPELDPAESD
LDSGEPSASL SELRCLFRWL QKSLPFLVIL CAKLVIQHAL GLAVGIGLFT TFLYVNKNIQ
TQVFLQDRHS KLQCIWLLLF LISSTLLLYY TFLTETLYHC LILLSPAIEP LGFWETLWAV
GITNFVIKFL CMGIKCLILL LPSSLVSYRT QGRWLMLTEE LGQVHQAIAP VPLWFRYLVT
YQETEGTPGL TLGVLLALLY LILKLLGLYG QWTSLMKTGR LFLRVECTGT AATRSQCNEA
GDVCPICQGE YREPRALLCQ HIFCDECIAL WFNREKSCPL CRTVITEKVY KWRDGATSPH
LQIY
//
