RNFT1_XENLA
ID RNFT1_XENLA Reviewed; 416 AA.
AC Q6NTV1; Q6DDF3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 73.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-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=AAH77617.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC068853; AAH68853.1; -; mRNA.
DR EMBL; BC077617; AAH77617.1; ALT_INIT; mRNA.
DR RefSeq; NP_001084648.1; NM_001091179.1.
DR RefSeq; XP_018100454.1; XM_018244965.1.
DR AlphaFoldDB; Q6NTV1; -.
DR SMR; Q6NTV1; -.
DR DNASU; 414607; -.
DR GeneID; 414607; -.
DR KEGG; xla:414607; -.
DR CTD; 414607; -.
DR Xenbase; XB-GENE-984040; rnft1.L.
DR OMA; GCIHSRL; -.
DR OrthoDB; 1321151at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 414607; Expressed in egg cell and 19 other tissues.
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; IEA:InterPro.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; IEA:InterPro.
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..416
FT /note="E3 ubiquitin-protein ligase RNFT1"
FT /id="PRO_0000320638"
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 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..117
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 16..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 86
FT /note="R -> G (in Ref. 1; AAH68853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 47122 MW; 299BE3822FFBAB17 CRC64;
MKHRPVHERQ SSTESKNLKE TTQLIMQSSS DHTHHQLGSN DSPSACMSLP VPQLSAEGSC
TVGDVTVDLS SQDSQHVARS NSRRVRPSTH GRSPSRHGHT HSHDASGPED ANDDSREQSN
SISEVFHLYK WLEKSFPYIL IFSAKLVVQH ITGISVGIGL LTTFLYANKC IVNQVFLRDK
CSKLQCLWVL VFLLFSSFLL YYTFSSQALY YSLVFMNPSL GPLHFFDALW VVGITDFIGK
FFFMGLKCII LLVPSFVMSH KSKGYWYMAL EELAQCYCTL VSTPVWFRYL IDYGNLDSGA
EWHFGILLAL LYLILKILII FGQRKTSSDC LRLFLSQPNY GTTATKRQCS EADGMCAICQ
AEFTKPIALI CQHVFCEECI SSWFNKEKTC PLCRTLISNH SHKWKDGATS LQLRIF
