CEG1A_DROME
ID CEG1A_DROME Reviewed; 995 AA.
AC Q9NGC3; B7FNK5; I0C0M3; Q6IDF7; Q86P12; Q8MR30; Q95SF3; Q9NKE5; Q9VJV4;
AC Q9VJV5; Q9VJV7;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Centaurin-gamma-1A;
GN Name=CenG1A; ORFNames=CG31811;
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|EMBL:AAF66064.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA Hendrick A.G., Harrington L.S.;
RT "Identification of novel ARF-GTPase activating protein (GAP)-like proteins
RT in the Drosophila genome.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [3] {ECO:0000305}
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
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 [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; B AND C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Booth B., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B;
CC IsoId=Q9NGC3-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9NGC3-2; Sequence=VSP_000312, VSP_000313;
CC Name=C;
CC IsoId=Q9NGC3-3; Sequence=VSP_000314;
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28369.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAT27272.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform A]:
CC Sequence=AAF66064.1; Type=Miscellaneous discrepancy; Note=a duplication of 79 residues inserted in position 130.; Evidence={ECO:0000305};
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DR EMBL; AF254741; AAF66064.1; ALT_SEQ; mRNA.
DR EMBL; AE014134; AAF53343.2; -; Genomic_DNA.
DR EMBL; AE014134; AAF53349.2; -; Genomic_DNA.
DR EMBL; AE014134; AAF53350.2; -; Genomic_DNA.
DR EMBL; AY122158; AAM52670.1; -; mRNA.
DR EMBL; AY060821; AAL28369.1; ALT_SEQ; mRNA.
DR EMBL; BT003538; AAO39542.1; -; mRNA.
DR EMBL; BT014648; AAT27272.1; ALT_FRAME; mRNA.
DR EMBL; BT053695; ACK77612.1; -; mRNA.
DR EMBL; BT133428; AFH68352.1; -; mRNA.
DR RefSeq; NP_523562.2; NM_078838.3. [Q9NGC3-2]
DR RefSeq; NP_723849.1; NM_165067.2. [Q9NGC3-1]
DR RefSeq; NP_723850.1; NM_165068.2. [Q9NGC3-3]
DR AlphaFoldDB; Q9NGC3; -.
DR SMR; Q9NGC3; -.
DR BioGRID; 60833; 51.
DR DIP; DIP-21141N; -.
DR IntAct; Q9NGC3; 41.
DR STRING; 7227.FBpp0080123; -.
DR PaxDb; Q9NGC3; -.
DR PRIDE; Q9NGC3; -.
DR DNASU; 34803; -.
DR EnsemblMetazoa; FBtr0080546; FBpp0080123; FBgn0028509. [Q9NGC3-1]
DR EnsemblMetazoa; FBtr0080547; FBpp0080124; FBgn0028509. [Q9NGC3-2]
DR EnsemblMetazoa; FBtr0080548; FBpp0080125; FBgn0028509. [Q9NGC3-3]
DR GeneID; 34803; -.
DR KEGG; dme:Dmel_CG31811; -.
DR CTD; 34803; -.
DR FlyBase; FBgn0028509; CenG1A.
DR VEuPathDB; VectorBase:FBgn0028509; -.
DR eggNOG; KOG0705; Eukaryota.
DR GeneTree; ENSGT00940000169062; -.
DR InParanoid; Q9NGC3; -.
DR OMA; WYGANIK; -.
DR PhylomeDB; Q9NGC3; -.
DR SignaLink; Q9NGC3; -.
DR BioGRID-ORCS; 34803; 0 hits in 3 CRISPR screens.
DR ChiTaRS; CenG1A; fly.
DR GenomeRNAi; 34803; -.
DR PRO; PR:Q9NGC3; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0028509; Expressed in spermathecum and 62 other tissues.
DR Genevisible; Q9NGC3; DM.
DR GO; GO:0016020; C:membrane; ISS:FlyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IMP:FlyBase.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0072375; P:medium-term memory; IMP:FlyBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:FlyBase.
DR GO; GO:0043087; P:regulation of GTPase activity; ISM:FlyBase.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; GTP-binding; GTPase activation;
KW Metal-binding; Nucleotide-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..995
FT /note="Centaurin-gamma-1A"
FT /id="PRO_0000074221"
FT DOMAIN 453..682
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 679..822
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 866..898
FT /note="ANK"
FT ZN_FING 717..740
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..340
FT /note="Small GTPase-like"
FT REGION 308..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 193..197
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 249..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..232
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_000314"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.6"
FT /id="VSP_000312"
FT VAR_SEQ 69..125
FT /note="AHPPQPLISNSLAIRQEIQRFESVHPSIYAIYELIDLLPMADAQIAQSIRDH
FT VVCIE -> MLAVKNFFLPERAKAPETPQRFSRMPEAFLRSIRRRSLRVKRAKSLVVPD
FT RSEKRKS (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.6"
FT /id="VSP_000313"
FT CONFLICT 334
FT /note="N -> D (in Ref. 6; AAO39542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 995 AA; 108044 MW; E2376662937C328F CRC64;
MSNYHPHSHP HALSHPHPQQ VHNQLQNPHQ NQLPPPQRHN HAAPTAAASA SGAPSSSASA
SASASILVAH PPQPLISNSL AIRQEIQRFE SVHPSIYAIY ELIDLLPMAD AQIAQSIRDH
VVCIEDSFVN SQEWTISRSV PDLRLGIVGS LNSGKSALVH RYLTGSYMQE ESPEGGRFKK
EVFIDGQSYL LLIRDEGGAP EMQFAGWVDA VIFVFSLENE GSFNTVYNYY TKMAHFRNGQ
EIPMILVGTQ DAISERNPRV IDDTRARKLA SDLKRCSYYE TCATYGLNVE RVFQDACQKI
LSQRLPLPPQ VQPARPTTPQ GNRLGLAPYQ APTNGQRGQQ QLPLRMSADF AQAEQKLWSL
QAASSSTINE NNNITKYNPG AANSLQGDCS QVQLRDPRDL APPPGKELPT PTSTPTTSRK
SRRRSNLFIP SSSKKADKEK EPKSSELGSG RSIPIKQGYL YKRSSKSLNK EWKKKYVTLC
DDGRLTYHPS LHDYMDDVHG KEIPLQYVTV KVPGQKPRGS KSIITNSALT SSLMANGQRA
QNTLSDGIGC LTLAKDNQRK LSEKLSLLGA GSIAAGAGGE PLKSNSSQQT SGDEGIAMSN
SNSQTFIAGE VANAGNKLEA QTPNVKKRHR RMKSSSVKAN EADDNDGYEF YIVSLDSKQW
HFEAANSEER DEWVAAVEQE IFKSLQSIES SKTKQATSTD LAAMLAIRQR VPGNGFCVDC
GAPNPEWASL NLGVLMCIEC SGVHRNLGSH ISKVRSLGLD DWPSPHLSVM LAIGNSLANS
VWESNTRQRV KPTSQASRED KERWVRSKYE AKEFLTPLGN GSSAHPSPSP GQQLIEAVIR
ADIKSIVSIL ANCPSEVTNA NVSARDVRTP LLLACAIGNL AIAQLLIWNG ANIKHTDHEG
RTCLAYARAA QSLATAKSIK AAAAAQAGTT IPAPAPPTNG GIPAPQYNVE DTTALVELLE
GLGCPEAAPL TASGTLPRRR DTLGTPYEKS VSGVI
