GOLI_DROME
ID GOLI_DROME Reviewed; 461 AA.
AC Q06003; E1JGX0; Q8T0M7; Q9W0W3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=E3 ubiquitin-protein ligase goliath {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305|PubMed:23353890};
DE Flags: Precursor;
GN Name=gol; Synonyms=g1 {ECO:0000303|PubMed:8462875}, GL; ORFNames=CG2679;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-461 (ISOFORM C), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8462875; DOI=10.1016/0378-1119(93)90330-6;
RA Bouchard M.L., Cote S.;
RT "The Drosophila melanogaster developmental gene g1 encodes a variant zinc-
RT finger-motif protein.";
RL Gene 125:205-209(1993).
RN [5]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 323-HIS--HIS-326.
RX PubMed=23353890; DOI=10.1038/emboj.2013.1;
RA Yamazaki Y., Schoenherr C., Varshney G.K., Dogru M., Hallberg B.,
RA Palmer R.H.;
RT "Goliath family E3 ligases regulate the recycling endosome pathway via
RT VAMP3 ubiquitylation.";
RL EMBO J. 32:524-537(2013).
CC -!- FUNCTION: Endosomal E3 ubiquitin-protein ligase that regulates the
CC recycling endosome pathway (PubMed:23353890). May play an indirect role
CC in regulation of gene expression during embryonic mesoderm formation
CC (PubMed:8462875). {ECO:0000269|PubMed:23353890,
CC ECO:0000269|PubMed:8462875}.
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:0000305|PubMed:23353890};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23353890}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:23353890};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B;
CC IsoId=Q06003-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q06003-3; Sequence=VSP_012171;
CC Name=D;
CC IsoId=Q06003-4; Sequence=VSP_042121;
CC -!- TISSUE SPECIFICITY: Embryonic visceral mesoderm and primordia of
CC somatic musculature. {ECO:0000269|PubMed:8462875}.
CC -!- DISRUPTION PHENOTYPE: Flies are viable and fertile.
CC {ECO:0000269|PubMed:23353890}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28582.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA28582.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF47316.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68328.1; -; Genomic_DNA.
DR EMBL; AE013599; ACZ94572.1; -; Genomic_DNA.
DR EMBL; AY069169; AAL39314.1; -; mRNA.
DR EMBL; M97204; AAA28582.1; ALT_SEQ; mRNA.
DR PIR; JC1495; JC1495.
DR RefSeq; NP_001163300.1; NM_001169829.3. [Q06003-4]
DR RefSeq; NP_001246517.1; NM_001259588.2. [Q06003-3]
DR RefSeq; NP_523864.3; NM_079140.5. [Q06003-3]
DR RefSeq; NP_726508.1; NM_166705.3. [Q06003-1]
DR AlphaFoldDB; Q06003; -.
DR SMR; Q06003; -.
DR IntAct; Q06003; 3.
DR MINT; Q06003; -.
DR STRING; 7227.FBpp0289416; -.
DR PaxDb; Q06003; -.
DR PRIDE; Q06003; -.
DR DNASU; 38006; -.
DR EnsemblMetazoa; FBtr0072459; FBpp0072361; FBgn0004919. [Q06003-1]
DR EnsemblMetazoa; FBtr0300178; FBpp0289415; FBgn0004919. [Q06003-3]
DR EnsemblMetazoa; FBtr0300179; FBpp0289416; FBgn0004919. [Q06003-4]
DR EnsemblMetazoa; FBtr0306330; FBpp0297426; FBgn0004919. [Q06003-3]
DR GeneID; 38006; -.
DR KEGG; dme:Dmel_CG2679; -.
DR UCSC; CG2679-RB; d. melanogaster. [Q06003-1]
DR CTD; 38006; -.
DR FlyBase; FBgn0004919; gol.
DR VEuPathDB; VectorBase:FBgn0004919; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000156171; -.
DR HOGENOM; CLU_029735_1_0_1; -.
DR InParanoid; Q06003; -.
DR OMA; APATMPH; -.
DR PhylomeDB; Q06003; -.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-5689896; Ovarian tumor domain proteases.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q06003; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 38006; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38006; -.
DR PRO; PR:Q06003; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004919; Expressed in spermathecum and 24 other tissues.
DR ExpressionAtlas; Q06003; baseline and differential.
DR Genevisible; Q06003; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0001707; P:mesoderm formation; IEP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IMP:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Endosome;
KW Membrane; Metal-binding; Reference proteome; Signal; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..461
FT /note="E3 ubiquitin-protein ligase goliath"
FT /id="PRO_0000030721"
FT TOPO_DOM 26..234
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 98..207
FT /note="PA"
FT ZN_FING 303..344
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 355..461
FT /note="FLGSEESILEYQPDPPQGLALVEARDESADLNRSRDFVVDFPRVFVLDSGCV
FT VGAREMLFPCRIPERSQSSLSLRQARDWVSLMSNKLEEQQGLRSMRNDEMQQVIK ->
FT VGDQIYQTPSPQHTAPIASIEEVPVIVVAVPHGPQPLQPLQASNMSSFAPSHYFQSSRS
FT PSSSVQQQLAPLTYQPHPQQAASERGRRNSAPATMPHAITASHQVTDV (in
FT isoform C)"
FT /evidence="ECO:0000303|PubMed:8462875"
FT /id="VSP_012171"
FT VAR_SEQ 459..461
FT /note="VIK -> QLLSARESARHRRSRSADGRYSTGCFGGRQRQPSVLVSSLGQPQL
FT HSEVAQMQRSNSSQALKHLTDAAHAQSRQRQRESFDFARTRRRFMRRESDEISLRSLPR
FT RGATSAAHRQLHREREPDDSVHTDQITIQVNGKGVDLNQ (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_042121"
FT MUTAGEN 323..326
FT /note="HEFH->REFR: Abolished E3 ubiquitin-protein ligase
FT activity and ability to generate large endosomes when
FT overexpressed."
FT /evidence="ECO:0000269|PubMed:23353890"
FT CONFLICT 245..251
FT /note="LMIISLV -> DDILC (in Ref. 1; AAA28582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 52623 MW; 309F41D935BD78B7 CRC64;
MYIRKTLLLA CLVLLFGGLP PLTFPATTTT LVAAMSIANQ DLERYFRPGN GTHSFSGMED
RIAVDVYNYA FLNWSYVEHG NMLCNMEFAQ EQARYGEGKV LNVTGRLIHI TATDNFSDDY
ACTPYIRGTL GAPIPDKGET WIALVRRGRC TFEEKVKHVY QQNAAGVIIY NDKQVMQLEK
MQIKGKTRNI AAVITYQNIG QDLSLTLDKG YNVTISIIEG RRGVRTISSL NRTSVLFVSI
SFIVLMIISL VWLIFYYIQR FRYMQAKDQQ SRNLCSVTKK AIMKIPTKTG KFSDEKDLDS
DCCAICIEAY KPTDTIRILP CKHEFHKNCI DPWLIEHRTC PMCKLDVLKF YGYVFLGSEE
SILEYQPDPP QGLALVEARD ESADLNRSRD FVVDFPRVFV LDSGCVVGAR EMLFPCRIPE
RSQSSLSLRQ ARDWVSLMSN KLEEQQGLRS MRNDEMQQVI K
