ID A0A3B3U9S7_9TELE Unreviewed; 732 AA.
AC A0A3B3U9S7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000009668.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000009668.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B3U9S7; -.
DR STRING; 48699.ENSPLAP00000009668; -.
DR Ensembl; ENSPLAT00000000824.1; ENSPLAP00000009668.1; ENSPLAG00000012478.1.
DR GeneTree; ENSGT00940000154006; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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 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 TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..275
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 347..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 79867 MW; 0CC505178CA68E12 CRC64;
MEPCSLCRLS HPDVEPTCFQ NGKVESEGSV SQPALSPRAH FSAKGRQCLL YPVCLCLLQY
HPVSLCNTSE DERQDSGFIT IVKLEQLGPH CSPLASSHPL HLTDQRTNSR PQLKNADSLP
HPVVLIKGAD AKKLMNLVNH NEEATVVIEA KVEPKWPHYD VSILLTIVLV ILTIVLIFAF
RYKCKSNRTW DSVHQQTVRA IGRLETRIYR SQSCSGSQRH RGAWGSASSS NSSPVCAICL
EEFQEGQNLR IISCAHEFHR DCVDPWLMQH RTCPLYFFFL SVLALSVFLR NGASASEKQK
PADCGFHLPV DVPGRPHRLG AGCRTSAHHY ASRRSCHTYR SSCPAQRNAS GSRLQHGTSA
AAQSRGVAGN GRQDDGSCSG GSYHTERSGY LADGPASDSS SGPWHGSSSD SVLNCTDVSL
QGVYGSWSTF RSSLSSDYDP FGYFGAAPVA GVGSGHAPRR NSLEAAAQNR PKSLDSVVNK
AGCLEEQPQT VFSHIHYHRH RHHHYEEGEH GQGPSRGSDE EQGPAAASAS GQDKDSPACP
PKHSPCHCPK PEPTDRPSPG TERQDLDQTG PPVIVPPISL QLQPHCCHQG HGHPPAPLVG
GCLLDGPSVH FHQSLDLQDD RSIHIHYGQS PAYCCPPPEL HPALLPVPLI LDSAGIEEWP
CCGGAHVVWQ RQVQQAHSEP QLMGPGTSMD RPPCRFHQGP SAERNTDICL YCQSMHHNQG
EDPFCFLLAR PA
//