GALL2_DROME
ID GALL2_DROME Reviewed; 156 AA.
AC Q9VTC4;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=MIP18 family protein galla-2 {ECO:0000303|PubMed:25065591};
GN Name=galla-2 {ECO:0000303|PubMed:25065591,
GN ECO:0000312|FlyBase:FBgn0036107};
GN ORFNames=CG7949 {ECO:0000312|FlyBase:FBgn0036107};
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 FUNCTION, INTERACTION WITH THE CGX COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=25065591; DOI=10.1038/onc.2014.202;
RA Yeom E., Hong S.T., Choi K.W.;
RT "Crumbs interacts with Xpd for nuclear division control in Drosophila.";
RL Oncogene 34:2777-2789(2015).
RN [4]
RP INTERACTION WITH XPD AND MMS19.
RX PubMed=29361561; DOI=10.1242/dev.156802;
RA Nag R.N., Niggli S., Sousa-Guimaraes S., Vazquez-Pianzola P., Suter B.;
RT "Mms19 is a mitotic gene that permits Cdk7 to be fully active as a Cdk-
RT activating kinase.";
RL Development 145:0-0(2018).
CC -!- FUNCTION: Component of the crb-galla-Xpd (CGX) complex which is
CC essential for proper mitotic chromosome segregation in early embryos.
CC The CGX complex is also required for cell proliferation in developing
CC wing disks. In the CGX complex, acts with crb to recruit Xpd thus
CC forming the functional complex. {ECO:0000269|PubMed:25065591}.
CC -!- SUBUNIT: Component of the CGX complex composed of crb, galla (galla-1
CC or galla-2) and Xpd (PubMed:25065591). Interacts with crb (via
CC intracellular domain) (PubMed:25065591). Also able to interact with Xpd
CC in the absence of crb (PubMed:25065591). Interacts with Mms19
CC (PubMed:29361561). {ECO:0000269|PubMed:25065591,
CC ECO:0000269|PubMed:29361561}.
CC -!- INTERACTION:
CC Q9VTC4; Q7K1Y4: Ciao1; NbExp=3; IntAct=EBI-100085, EBI-175932;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. In 0-2 hr embryos, mutants
CC display signs of incomplete chromosome segregation during mitotic
CC divisions likely due to defective organization of spindle microtubules.
CC {ECO:0000269|PubMed:25065591}.
CC -!- MISCELLANEOUS: The name 'galla' means splitting in Korean and is
CC derived from its role in chromosome segregation.
CC {ECO:0000303|PubMed:25065591}.
CC -!- SIMILARITY: Belongs to the MIP18 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF50128.1; -; Genomic_DNA.
DR RefSeq; NP_648416.1; NM_140159.2.
DR PDB; 6TBL; X-ray; 2.65 A; C/D=2-156.
DR PDB; 6TBN; X-ray; 2.00 A; A=2-156.
DR PDB; 6TC0; X-ray; 3.60 A; B/E=2-156.
DR PDBsum; 6TBL; -.
DR PDBsum; 6TBN; -.
DR PDBsum; 6TC0; -.
DR AlphaFoldDB; Q9VTC4; -.
DR SMR; Q9VTC4; -.
DR BioGRID; 64598; 10.
DR DIP; DIP-20907N; -.
DR IntAct; Q9VTC4; 1.
DR STRING; 7227.FBpp0075999; -.
DR PaxDb; Q9VTC4; -.
DR PRIDE; Q9VTC4; -.
DR EnsemblMetazoa; FBtr0076270; FBpp0075999; FBgn0036107.
DR GeneID; 39221; -.
DR KEGG; dme:Dmel_CG7949; -.
DR UCSC; CG7949-RA; d. melanogaster.
DR CTD; 39221; -.
DR FlyBase; FBgn0036107; galla-2.
DR VEuPathDB; VectorBase:FBgn0036107; -.
DR eggNOG; KOG3381; Eukaryota.
DR GeneTree; ENSGT00390000017697; -.
DR HOGENOM; CLU_075876_3_1_1; -.
DR InParanoid; Q9VTC4; -.
DR OMA; NQCISAR; -.
DR OrthoDB; 1408004at2759; -.
DR PhylomeDB; Q9VTC4; -.
DR SignaLink; Q9VTC4; -.
DR BioGRID-ORCS; 39221; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39221; -.
DR PRO; PR:Q9VTC4; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036107; Expressed in adult abdomen and 28 other tissues.
DR ExpressionAtlas; Q9VTC4; baseline and differential.
DR Genevisible; Q9VTC4; DM.
DR GO; GO:0097361; C:CIA complex; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IEA:InterPro.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR039796; MIP18.
DR InterPro; IPR002744; MIP18-like.
DR PANTHER; PTHR12377; PTHR12377; 1.
DR Pfam; PF01883; FeS_assembly_P; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome partition; Mitosis;
KW Reference proteome.
FT CHAIN 1..156
FT /note="MIP18 family protein galla-2"
FT /id="PRO_0000212694"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:6TBN"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:6TBN"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:6TBN"
FT TURN 55..59
FT /evidence="ECO:0007829|PDB:6TBN"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:6TBN"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6TBN"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:6TBN"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6TBN"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:6TBN"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6TBN"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:6TBN"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:6TBN"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:6TBN"
SQ SEQUENCE 156 AA; 17587 MW; F545ED448765C3A0 CRC64;
MPTEIENINP NVYDRIKERV LTANEEDENV PDPFDKREIF DLIRNINDPE HPLTLEELHV
VQEDLIRIND SQNSVHISFT PTIPHCSMAT LIGLSIRVKL LRSLPPRFKV TVEITPGTHA
SELAVNKQLA DKERVAAALE NNHLAEVINQ CIAAKG
