RNFT1_DANRE
ID RNFT1_DANRE Reviewed; 419 AA.
AC Q6NZ21;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=E3 ubiquitin-protein ligase RNFT1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q5M7Z0};
DE AltName: Full=RING finger and transmembrane domain-containing protein 1;
GN Name=rnft1; ORFNames=zgc:77306;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q5M7Z0}.
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:0000250|UniProtKB:Q5M7Z0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q5M7Z0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5M7Z0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5M7Z0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH66378.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC066378; AAH66378.1; ALT_INIT; mRNA.
DR RefSeq; NP_998393.2; NM_213228.2.
DR AlphaFoldDB; Q6NZ21; -.
DR STRING; 7955.ENSDARP00000013898; -.
DR PaxDb; Q6NZ21; -.
DR Ensembl; ENSDART00000022484; ENSDARP00000013898; ENSDARG00000015917.
DR Ensembl; ENSDART00000182807; ENSDARP00000148924; ENSDARG00000116783.
DR GeneID; 406509; -.
DR KEGG; dre:406509; -.
DR CTD; 51136; -.
DR ZFIN; ZDB-GENE-040426-2324; rnft1.
DR eggNOG; KOG4638; Eukaryota.
DR GeneTree; ENSGT00940000156740; -.
DR HOGENOM; CLU_039460_2_1_1; -.
DR InParanoid; Q6NZ21; -.
DR OMA; GCIHSRL; -.
DR OrthoDB; 1321151at2759; -.
DR PhylomeDB; Q6NZ21; -.
DR TreeFam; TF331930; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6NZ21; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000015917; Expressed in mature ovarian follicle and 24 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 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; PTHR15860; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..419
FT /note="E3 ubiquitin-protein ligase RNFT1"
FT /id="PRO_0000320637"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 359..397
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..403
FT /note="Required for ubiquitin ligase activity and for
FT protection against ER stress-induced cell death"
FT /evidence="ECO:0000250|UniProtKB:Q5M7Z0"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 47191 MW; C8111D26C817ABFB CRC64;
MKLRAQFDRG TYSESKGSFK LRDSLDPMQP EPSSREGNGL SLTLQPELLA RMPGAGSSSG
TETGEDVRVP MGSSSGSTNG RGATSRRMRT ASHSHSHTHG HGHSHEHESD SGESDLESGE
SSSSISELRY LLRWLKKSLP FIVILCAKLV IQHALGLAVA VGLFTTFMYV NKSIQTQVFL
HDRRTNLHCA WLLLFLTSSS LLVFYTFHTQ SLYRCLFFAN ATIDYHNFWE VLWSVGVTNF
ILKFIFMGFK CLILLVPCPL MTYRRRGQWY MLIEEVGQLY QVIAPVPLWF RYLVSYDEMD
TSVGLTLGIL LALLYLIMKL LALYGLSGSL QKTLRTFFSP EVNGAPASPA QIREAGDICP
ICQADFKQPR VLVCQHIFCE ECIAQWLNQE RTCPLCRTVI TDKVHKWKDG ATSAHLQIY
