RNFT1_XENTR
ID RNFT1_XENTR Reviewed; 416 AA.
AC Q28GL3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=TEgg046i15.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) 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}.
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DR EMBL; CR761344; CAJ81809.1; -; mRNA.
DR RefSeq; NP_001016349.1; NM_001016349.2.
DR RefSeq; XP_012812416.1; XM_012956962.1.
DR AlphaFoldDB; Q28GL3; -.
DR SMR; Q28GL3; -.
DR STRING; 8364.ENSXETP00000055374; -.
DR PaxDb; Q28GL3; -.
DR Ensembl; ENSXETT00000055374; ENSXETP00000055374; ENSXETG00000026210.
DR GeneID; 549103; -.
DR KEGG; xtr:549103; -.
DR CTD; 51136; -.
DR Xenbase; XB-GENE-984035; rnft1.
DR eggNOG; KOG4638; Eukaryota.
DR HOGENOM; CLU_039460_2_1_1; -.
DR InParanoid; Q28GL3; -.
DR OMA; RLHCKHI; -.
DR OrthoDB; 1321151at2759; -.
DR TreeFam; TF331930; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000026210; Expressed in egg cell and 12 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 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..416
FT /note="E3 ubiquitin-protein ligase RNFT1"
FT /id="PRO_0000320639"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 356..394
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 27..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..400
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 27..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 47030 MW; E1DABF8C58953179 CRC64;
MKHRPVHERQ CSTETKNWKE NTQLIMQSSS GHTHHQPGSN DSPSVCMSLP VPQLSAEGSC
TAGDVTIDLS SPESHHGARS SSRRVRPGNG RSLSRHGHTH SHDANGPEDA NDADSREQSN
SISEVFHFYK WLEKSFPYIL IFSAKLVVQH ITGISVGIGL LTTFLYANKC IVNQVFLRDK
CSKLQCLWIL VFLLFSSLLL YYTFSSQALY YSLVFMNPSL GPLHFFDALW VVGITDFIGK
FFFMGLKCII LLVPSFVMSH KSKGYWYMAL EEVAQCYCML VSTPVWFRYL IDYGNQNSGA
EWHFGILLAL LYLILKLLII FGQRKTSSNS LRLFLTQPNY GAAATKSQCS EVDGMCAICQ
AEFIKPIVLV CQHVFCEECI SLWFNKEKTC PLCRTVISNQ SHKWKDGATS LQLRIF
