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Database: UniProt
Entry: A0A2K6LI81_RHIBE
LinkDB: A0A2K6LI81_RHIBE
Original site: A0A2K6LI81_RHIBE 
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
//
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