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Database: UniProt
Entry: A0A3B3U9S7_9TELE
LinkDB: A0A3B3U9S7_9TELE
Original site: A0A3B3U9S7_9TELE 
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}.
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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
//
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