GZL_DROME
ID GZL_DROME Reviewed; 536 AA.
AC Q9VI20; Q8T089;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=E3 ubiquitin-protein ligase Godzilla {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:23353890, ECO:0000269|PubMed:26974662};
DE Flags: Precursor;
GN Name=gzl {ECO:0000303|PubMed:23353890, ECO:0000312|FlyBase:FBgn0037442};
GN ORFNames=CG10277 {ECO:0000312|FlyBase:FBgn0037442};
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.
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].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-536.
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 255-HIS--HIS-258.
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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 255-HIS--HIS-258.
RX PubMed=26974662; DOI=10.1038/ncb3325;
RA Yamazaki Y., Palmer L., Alexandre C., Kakugawa S., Beckett K., Gaugue I.,
RA Palmer R.H., Vincent J.P.;
RT "Godzilla-dependent transcytosis promotes Wingless signalling in Drosophila
RT wing imaginal discs.";
RL Nat. Cell Biol. 18:451-457(2016).
CC -!- FUNCTION: Endosomal E3 ubiquitin-protein ligase that regulates the
CC recycling endosome pathway by mediating ubiquitination of Synaptobrevin
CC (Syb) (PubMed:23353890). Also acts as a regulator of transcytosis in
CC wing imaginal disks by catalyzing ubiquitination of Syb: ubiquitination
CC of Syb promotes transcytosis of wingless (wg) to the basolateral
CC surface (PubMed:26974662). {ECO:0000269|PubMed:23353890,
CC ECO:0000269|PubMed:26974662}.
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:0000269|PubMed:23353890,
CC ECO:0000269|PubMed:26974662};
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 -!- DISRUPTION PHENOTYPE: Larval lethality. {ECO:0000269|PubMed:23353890}.
CC -!- SIMILARITY: Belongs to the Godzilla family. {ECO:0000305}.
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DR EMBL; AE014297; AAF54124.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13375.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13376.1; -; Genomic_DNA.
DR EMBL; AE014297; ABW08609.1; -; Genomic_DNA.
DR EMBL; BT133094; AEX98014.1; -; mRNA.
DR EMBL; AY069479; AAL39624.1; -; mRNA.
DR RefSeq; NP_001097695.1; NM_001104225.2.
DR RefSeq; NP_649653.1; NM_141396.4.
DR RefSeq; NP_731079.1; NM_169139.2.
DR RefSeq; NP_731080.1; NM_169140.2.
DR SMR; Q9VI20; -.
DR IntAct; Q9VI20; 3.
DR MINT; Q9VI20; -.
DR STRING; 7227.FBpp0081218; -.
DR PeptideAtlas; Q8T089; -.
DR PRIDE; Q9VI20; -.
DR EnsemblMetazoa; FBtr0081720; FBpp0081217; FBgn0037442.
DR EnsemblMetazoa; FBtr0081721; FBpp0081218; FBgn0037442.
DR EnsemblMetazoa; FBtr0081722; FBpp0081219; FBgn0037442.
DR EnsemblMetazoa; FBtr0113198; FBpp0112110; FBgn0037442.
DR GeneID; 40791; -.
DR KEGG; dme:Dmel_CG10277; -.
DR UCSC; CG10277-RA; d. melanogaster.
DR CTD; 40791; -.
DR FlyBase; FBgn0037442; gzl.
DR VEuPathDB; VectorBase:FBgn0037442; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000159671; -.
DR HOGENOM; CLU_035275_5_0_1; -.
DR OMA; HERINPF; -.
DR OrthoDB; 1487241at2759; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 40791; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 40791; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037442; Expressed in oviduct (Drosophila) and 25 other tissues.
DR ExpressionAtlas; Q9VI20; baseline and differential.
DR GO; GO:0005768; C:endosome; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0016197; P:endosomal transport; IMP:FlyBase.
DR GO; GO:1904300; P:positive regulation of transcytosis; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IMP:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd02123; PA_C_RZF_like; 1.
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 InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
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 Endosome; Glycoprotein; Membrane; Metal-binding; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..536
FT /note="E3 ubiquitin-protein ligase Godzilla"
FT /evidence="ECO:0000255"
FT /id="PRO_5015100278"
FT TOPO_DOM 22..174
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 89..151
FT /note="PA"
FT /evidence="ECO:0000255"
FT ZN_FING 235..277
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 255..258
FT /note="HPYH->RPYR: Abolished E3 ubiquitin-protein ligase
FT activity and ability to ubiquitinate Syb. Impaired ability
FT to promote transcytosis of wg."
FT /evidence="ECO:0000269|PubMed:23353890,
FT ECO:0000269|PubMed:26974662"
SQ SEQUENCE 536 AA; 58824 MW; 90E787655D4746A0 CRC64;
MSKRSCQILT LLGLCLVCHE ATLVGGHVLV YRKATSQLIE EFNDLPAQFG PNLPSNGLKV
YVVPARRPYY GCDSLDRPPH LKYPPSAKFV ALVARGECVF ERKIRVAQNA SYSAVIVYNN
EGDDLEQMSA ENITGIRIPS VFVGHTTGKA LATYFTTEVV LIINDELPFN INTQLILPFS
ILIGMCFIIM VIYMIYKCIR EQRRLRRHRL PKSMLKKLPV LRYTKNNANN KYDTCVICLE
DFIEDDKLRV LPCSHPYHTH CIDPWLTENR RVCPICKRKV FTKGEARASR SRQPSLDNVT
DTDDDTTPLL QQQQSNGRQV GQVSSASSAG GAAGSSSSVA AAAVAGTTRH GTFRRGHAGR
NPFEESQSSD DENALLASTV RPATSSGAHE RINPFDRAPN LPAHLAEQLT ESRRSVWSRI
NFASFFRRQP AVISVAAPPY LERVESGTSA MGLPVTGTIA VASPASNNIL NPNLSGSFKD
EDDMPPHRSI YEPIAISTPA ADSATVDDSA FLQTPTQGGI GVAALPHSAS DRQFLI
