GORAB_DROME
ID GORAB_DROME Reviewed; 338 AA.
AC Q8IQQ4; Q8SZQ5;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=RAB6-interacting golgin {ECO:0000305};
GN Name=Gorab {ECO:0000303|PubMed:29892014, ECO:0000312|FlyBase:FBgn0053052};
GN ORFNames=CG33052 {ECO:0000312|FlyBase:FBgn0053052};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAL48058.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48058.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL48058.1};
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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SAS-6, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, MUTAGENESIS OF 246-ALA--ALA-259; 246-ALA--SER-323;
RP 260-CYS--ASN-286; VAL-266 AND 287-ALA--SER-323, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=29892014; DOI=10.1038/s41588-018-0149-1;
RA Kovacs L., Chao-Chu J., Schneider S., Gottardo M., Tzolovsky G.,
RA Dzhindzhev N.S., Riparbelli M.G., Callaini G., Glover D.M.;
RT "Gorab is a Golgi protein required for structure and duplication of
RT Drosophila centrioles.";
RL Nat. Genet. 50:1021-1031(2018).
RN [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH SAS-6 AND RAB6, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 1-MET--ASP-194; 1-MET--GLN-222;
RP 1-MET--LEU-245; 197-GLN--ALA-259; 219-GLN--ASP-244; 224-THR--PRO-338;
RP 244-ASP--ALA-259; 247-VAL--PRO-338; 260-CYS--VAL-266; 260-CYS--ASN-286;
RP 261-ILE--PRO-338; 267-GLU--LYS-281; 271-VAL--PRO-338; 282-ILE--ASN-286;
RP 286-ASN--VAL-320; 288-SER--PRO-338; 303-ALA--VAL-320 AND 306-ALA--PRO-338.
RX PubMed=33704067; DOI=10.7554/elife.57241;
RA Fatalska A., Stepinac E., Richter M., Kovacs L., Pietras Z., Puchinger M.,
RA Dong G., Dadlez M., Glover D.M.;
RT "The dimeric Golgi protein Gorab binds to Sas6 as a monomer to mediate
RT centriole duplication.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Required for centriole duplication likely through its
CC interaction with Sas-6 (PubMed:29892014, PubMed:33704067). During
CC embryogenesis, maternally provided protein is required for centrosome
CC duplication and nuclear division cycles of the syncytial embryos
CC (PubMed:29892014). In femoral chordotonal organs, required for sensory
CC cilia structural integrity and functionality necessary for motor
CC coordination (PubMed:29892014). In male germline, has a role in
CC cytokinesis which seems dependent on its localization to the Golgi
CC (PubMed:29892014). {ECO:0000269|PubMed:29892014,
CC ECO:0000269|PubMed:33704067}.
CC -!- SUBUNIT: Homodimer (via C-terminus); dimerization appears to be
CC required for its trans-Golgi localization but not for its function and
CC centriolar localization (PubMed:33704067). Interacts (via C-terminus)
CC with Rab6; binds Rab6 as a homodimer, this interaction seems to be
CC required for trans-Golgi localization (PubMed:33704067). Interacts (via
CC C-terminus) with Sas-6; binds as a monomer to a Sas-6 homodimer
CC (PubMed:29892014, PubMed:33704067). {ECO:0000269|PubMed:29892014,
CC ECO:0000269|PubMed:33704067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:29892014}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:29892014, ECO:0000269|PubMed:33704067}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:29892014,
CC ECO:0000269|PubMed:33704067}. Note=Co-localizes with the centriole in
CC interphase and mitosis (PubMed:29892014). Mostly found in the Golgi,
CC with a small amount detected in centrosomes (PubMed:29892014,
CC PubMed:33704067). In spermatocytes, localizes to the trans-Golgi and
CC inside the Golgi cisternae (PubMed:33704067).
CC {ECO:0000269|PubMed:29892014, ECO:0000269|PubMed:33704067}.
CC -!- DISRUPTION PHENOTYPE: Viable (PubMed:29892014). Loss of daughter
CC centrioles and asymmetrical mother centriole-derived basal body results
CC in defective nine-fold symmetry of cilia in neurosensory organs and
CC therefore motor coordination defects (PubMed:29892014,
CC PubMed:33704067). Plp-associated structures are also disorganized but
CC ciliary structures are still present in the scolopale rods
CC (PubMed:29892014). Males are fertile, whereas female are sterile
CC (PubMed:29892014). Results in failure to duplicate centrosomes in
CC embryos and diploid larval tissues (PubMed:29892014).
CC {ECO:0000269|PubMed:29892014, ECO:0000269|PubMed:33704067}.
CC -!- SIMILARITY: Belongs to the GORAB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48058.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAN11712.1; -; Genomic_DNA.
DR EMBL; AY070587; AAL48058.1; ALT_FRAME; mRNA.
DR RefSeq; NP_788523.1; NM_176345.3.
DR AlphaFoldDB; Q8IQQ4; -.
DR SMR; Q8IQQ4; -.
DR IntAct; Q8IQQ4; 5.
DR STRING; 7227.FBpp0074991; -.
DR PaxDb; Q8IQQ4; -.
DR PRIDE; Q8IQQ4; -.
DR EnsemblMetazoa; FBtr0075229; FBpp0074991; FBgn0053052.
DR GeneID; 326245; -.
DR KEGG; dme:Dmel_CG33052; -.
DR UCSC; CG33052-RA; d. melanogaster.
DR CTD; 92344; -.
DR FlyBase; FBgn0053052; Gorab.
DR VEuPathDB; VectorBase:FBgn0053052; -.
DR eggNOG; ENOG502R60M; Eukaryota.
DR GeneTree; ENSGT00390000014886; -.
DR HOGENOM; CLU_075655_0_0_1; -.
DR InParanoid; Q8IQQ4; -.
DR OMA; TEHLCTV; -.
DR OrthoDB; 1277705at2759; -.
DR PhylomeDB; Q8IQQ4; -.
DR SignaLink; Q8IQQ4; -.
DR BioGRID-ORCS; 326245; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 326245; -.
DR PRO; PR:Q8IQQ4; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0053052; Expressed in ovary and 10 other tissues.
DR Genevisible; Q8IQQ4; DM.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0031985; C:Golgi cisterna; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR GO; GO:0046601; P:positive regulation of centriole replication; IMP:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR InterPro; IPR007033; GORAB.
DR PANTHER; PTHR21470; PTHR21470; 1.
DR Pfam; PF04949; Transcrip_act; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Reference proteome.
FT CHAIN 1..338
FT /note="RAB6-interacting golgin"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445701"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..260
FT /note="Essential for Sas-6 binding"
FT /evidence="ECO:0000269|PubMed:33704067"
FT REGION 246..323
FT /note="Necessary for localization to the Golgi"
FT /evidence="ECO:0000269|PubMed:29892014"
FT REGION 246..286
FT /note="Necessary for localization to the centrosome"
FT /evidence="ECO:0000269|PubMed:29892014"
FT REGION 260..286
FT /note="Necessary for interaction with Sas-6 and essential
FT for homodimerization"
FT /evidence="ECO:0000269|PubMed:29892014,
FT ECO:0000269|PubMed:33704067"
FT COILED 192..244
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1..245
FT /note="Missing: Abolishes binding with Rab6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 1..222
FT /note="Missing: Decreased binding with Rab6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 1..194
FT /note="Missing: No effect on binding with Rab6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 197..259
FT /note="Missing: Abolishes binding with Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 219..244
FT /note="Missing: Decreased binding with Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 224..338
FT /note="Missing: Abolishes binding with Sas-6 and Rab6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 244..259
FT /note="Missing: Abolishes binding with Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 246..323
FT /note="Missing: Loss of localization to the Golgi and
FT centrosomes. Results in female sterility and loss of
FT coordination."
FT /evidence="ECO:0000269|PubMed:29892014"
FT MUTAGEN 246..259
FT /note="Missing: Loss of localization to the Golgi and
FT centrosomes. Results in female sterility and loss of
FT coordination."
FT /evidence="ECO:0000269|PubMed:29892014"
FT MUTAGEN 247..338
FT /note="Missing: Abolishes binding with Sas-6 and Rab6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 260..286
FT /note="Missing: Decreased binding with Sas-6 and abolishes
FT homodimerization. Loss of localization to the Golgi and
FT centrosomes. Results in female sterility and loss of
FT coordination."
FT /evidence="ECO:0000269|PubMed:29892014,
FT ECO:0000269|PubMed:33704067"
FT MUTAGEN 260..266
FT /note="Missing: Decreased binding with Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 261..338
FT /note="Missing: Abolishes binding with Rab6 and decreased
FT binding with Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 266
FT /note="V->P: Loss of localization to the Golgi while
FT retaining localization to the centrosomes."
FT /evidence="ECO:0000269|PubMed:29892014"
FT MUTAGEN 267..281
FT /note="Missing: Decreased binding with Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 271..338
FT /note="Missing: Abolishes binding with Rab6. No effect on
FT binding to Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 282..286
FT /note="Missing: Loss of localization to the Golgi while
FT retaining localization to the centrosomes. No effect on
FT binding with Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 286..320
FT /note="Missing: No effect on binding with Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 287..323
FT /note="Missing: Loss of localization to the Golgi while
FT retaining localization to the centrosomes."
FT /evidence="ECO:0000269|PubMed:29892014"
FT MUTAGEN 288..338
FT /note="Missing: Abolishes binding with Rab6. No effect on
FT binding to Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 303..320
FT /note="Missing: No effect on binding with Sas-6."
FT /evidence="ECO:0000269|PubMed:33704067"
FT MUTAGEN 306..338
FT /note="Missing: Abolishes binding with Rab6."
FT /evidence="ECO:0000269|PubMed:33704067"
SQ SEQUENCE 338 AA; 37707 MW; CC327FFC83E90FD2 CRC64;
MTEKFNGFSH DEILKITGVK EGGVGKRPAS LEAAKPALRI QPGIRRMPDK IFRQADQLRK
QQQQQPQQPI QKPDVAKKTK SGTATPTEKP PTPTPAAEDD VANGSLNLDR PLSDSLIEAL
YHGNATARDK KTPATYADAE TTSTDDSSIL KISGGDSQTT SSTDDGSILP STQDTSPRER
LNTDSPFKGI SLKDFEQHRR MIEEQNKQKK QMLYQAIEQH TQKTAAESRK IEEIRHELSK
LESDLAVDVA LLRKQIDNAC IHFANVEKQY VKIEAQFLRA KIELHNASEK KELLTEHLCT
VIAHNEDRKA QKLTELMQKV GLSPTDDCQP IDLTQQSP
