UniProt: G3TIK3

Database: UniProt
Entry: G3TIK3_LOXAF

LinkDB:  G3TIK3_LOXAF 
Original site:  G3TIK3_LOXAF

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Ontology (11)   
   GO (11)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (6)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
   SMART (1)   
All databases (21)   

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ID   G3TIK3_LOXAF            Unreviewed;       503 AA.
AC   G3TIK3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
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};
GN   Name=MGRN1 {ECO:0000313|Ensembl:ENSLAFP00000014486.4};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000014486.4, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000014486.4, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014486.4,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000014486.4}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014486.4};
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; G3TIK3; -.
DR   STRING; 9785.ENSLAFP00000014486; -.
DR   Ensembl; ENSLAFT00000017275.4; ENSLAFP00000014486.4; ENSLAFG00000017274.4.
DR   eggNOG; KOG4265; Eukaryota.
DR   GeneTree; ENSGT00390000009925; -.
DR   HOGENOM; CLU_016631_1_1_1; -.
DR   InParanoid; G3TIK3; -.
DR   OMA; CAQSGPP; -.
DR   TreeFam; TF314969; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
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:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR   GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IEA:Ensembl.
DR   GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
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:UP000007646};
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          251..290
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          390..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  55502 MW;  308F6C2C518E6B86 CRC64;
     TGNYFASHFF MGGEKFDTPH PEGYLFGENM DLNFLGNRPV QFPYVTPAPH EPVKTLRSLV
     NIRKDSLRLV SRYKDDADSP TEENEKPRVL YSLEFTFDAD TRVAITIYCQ ATEEFLNGMA
     VYSPKSTALQ SETIHYKRGV GQQFSLPSFK IDFSEWKDDE LNFDLDRGMF PVVVQAVVDE
     GDVVEVTGHA HVLLAAFEKH MDGSFSVKPL KQKQIVDRVS YLLQEIYGIE NKNNQDTKPS
     DDENSDNSNE CVVCLSDLRD TLILPCRHLC LCNSCADTLR YQANNCPICR LPFRALLQIR
     AVRKKPGALS PVSFSPVLAQ SVDHDEHSSP DSIPPGYEPI SLLEALNGLR AISPAIPSAP
     LYEEITYSGA SDALSQASCP LAGISQVVDS SHLKGKPRNR SPDSTLRSPS SPIREEDEEK
     LSEDSDAPPP QSSVELAQRE SSSPESFITE EVDEMSSLKQ GSQAPSVESV LQDSSPEHRG
     LGPPADIYLP ALGPDSCSIG IEE
//

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