ID A0A2K6LI81_RHIBE Unreviewed; 782 AA.
AC A0A2K6LI81;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RNF43 {ECO:0000313|Ensembl:ENSRBIP00000023236.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000023236.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000023236.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000023236.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the ZNRF3 family.
CC {ECO:0000256|ARBA:ARBA00008759}.
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DR RefSeq; XP_017717081.1; XM_017861592.1.
DR RefSeq; XP_017717082.1; XM_017861593.1.
DR AlphaFoldDB; A0A2K6LI81; -.
DR STRING; 61621.ENSRBIP00000023236; -.
DR Ensembl; ENSRBIT00000047129.1; ENSRBIP00000023236.1; ENSRBIG00000035536.1.
DR GeneID; 108521641; -.
DR KEGG; rbb:108521641; -.
DR CTD; 54894; -.
DR GeneTree; ENSGT00940000154006; -.
DR OrthoDB; 5474929at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0038018; P:Wnt receptor catabolic process; IEA:Ensembl.
DR CDD; cd16798; RING-H2_RNF43; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045907; RNF43_Znf_RING.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR040700; ZNRF-3_ecto.
DR PANTHER; PTHR16200:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF43; 1.
DR PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF18212; ZNRF_3_ecto; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Signal {ECO:0000256|SAM:SignalP};
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}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..782
FT /note="RING-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014401974"
FT TRANSMEM 199..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 272..312
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 363..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..588
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 85838 MW; BAB070406ED1C6AD CRC64;
MSGGHQLQLA ALWPWLLMAT LQAGFGRTGL VLAAAVESER SAEQKAIIRV IPLKMDPTGK
LNLTLEGVFA GVAEVTPAEG KLMQSHPLYL CNASDDDNLE PGFISIVKLE SPRRAPRPCL
SLASKARMAG ERGASAVLFD ITEDRAAAEQ LQQPLGLTWP VVLIWGNDAE KLMEFVYKNQ
KAHVRIELKE PPAWPDYDVW ILLTVVGTIF VIILASVLRI RCRPRHSRPD PLQQRTAWAI
SQLATRRYQA SCRQARGEWP DSGSSCSSAP VCAICLEEFS EGQELRIISC LHEFHRNCVD
PWLHQHRTCP LCMFNIIEGD SFSQSLGPSR SYQEPGRRLH LIHQHPGHAH YHLPAAYLLG
PSQSAVARPP RPGPFLPSQE PGMGPRHHRL PRAAHPWAPG EQQRLAGAQH PYAQGWGLSH
LQSTSQHPAA RPVPLRRARP PDSSGSGESY CTERSGYLAD GPASDSSSGP CHGSSSDSVV
NCTDISLQGV HGSSSTFCSS LSSDFDSLVY CSPEGDPQRV DMHPSVTSRP RSFDSVVPTG
ETQVSSHVQY HRHRHHHYKK RFQWHGRKPG PETGVPPSRP PIPRTQPQPE PASDQHVTRS
NSAAPSGRLC NPQRPRALPE PAPGLVEASS MCLNTSSLFN LQKSSLSARH PQRKRRGCPS
EPTPGSRPQD ATVHPACQIV PHFTPSVAYS WSPEAHPLIF GPPGLDRRLI PETPGPYYSN
SQPVWLCLTP RRSPEPHPPG EGPSEWSSDT AEGRPCPHPH CQVLSAQPGS EEELEELCEQ
AV
//