ID   G3PLF3_GASAC            Unreviewed;       522 AA.
AC   G3PLF3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369081};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU369081};
DE   AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|RuleBase:RU369081};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000018434.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000018434.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000018434.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin ligase. {ECO:0000256|RuleBase:RU369081}.
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         ECO:0000256|RuleBase:RU369081};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369081}.
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DR   AlphaFoldDB; G3PLF3; -.
DR   Ensembl; ENSGACT00000018470.1; ENSGACP00000018434.1; ENSGACG00000013960.1.
DR   GeneTree; ENSGT00390000009925; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000013960; Expressed in intestinal epithelial cell and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd16817; mRING-HC-C3HC5_RNF157; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045194; MGRN1/RNF157-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22996:SF2; E3 UBIQUITIN-PROTEIN LIGASE MGRN1; 1.
DR   PANTHER; PTHR22996; MAHOGUNIN; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|RuleBase:RU369081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU369081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Transferase {ECO:0000256|RuleBase:RU369081};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU369081};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369081};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          276..315
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          388..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  57426 MW;  68D819B6D17FF31A CRC64;
     MGSVLSRRIA GVEDIDIQAN SAYRFPPKSG NYFASHFFMG GEKFDTPHPE GYLFGENMDL
     NFLGNRPVQF PYVTPAPHEP VKTLRSLVNI RKDSLRLVRY KDDSDAPVEE GEKPKVQYGV
     EFTFDADARV AITLYCQAFE EFSNGMAVYS AKNPSLVSET VHYKRGVSQQ FSMPSFKIDL
     TEWKEEDLNF DLDRGVFPMV IQAVVDEGDD CLGHAHVLLA AFERHVDGSF SVKPLKQKQI
     VDRVSYLLQE IYGIENKNNQ ETKPSDDENS DNSNECVVCL SDLRDTLILP CRHLCLCNSC
     ADTLRYQANN CPICRLPFRA LLQIRAVRKK PGALSPVSFS PVLAQTMDHD EHSSTDSVPP
     GFEPISLLEA LNGLQSVSPA IPPAPLYDDI NFSGGPGGEG RQLSSPEHLS DGSLQKGKVS
     KSPDSTLRSP SSPIQEEDEE KLSEVSDAQP HTQLSSSPAP TDVNPPLHQP TSKLLQKMHS
     GGDHLQDCSS EHSSLTKTES EPAGVLSLPG SSESTESLKS QS
//