GCP2_DROME
ID GCP2_DROME Reviewed; 852 AA.
AC Q9XYP7; Q95RT7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Gamma-tubulin complex component 2 homolog;
DE AltName: Full=Gamma-ring complex protein 84 kDa;
DE Short=d84p;
DE Short=dGrip84;
GN Name=Grip84; ORFNames=CG3917;
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 [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF 39-56;
RP 95-106; 166-173; 237-248; 340-347; 358-370; 391-396; 406-412; 418-435;
RP 438-444; 515-519 AND 570-588.
RX PubMed=10037793; DOI=10.1083/jcb.144.4.721;
RA Oegema K., Wiese C., Martin O.C., Milligan R.A., Iwamatsu A.,
RA Mitchison T.J., Zheng Y.;
RT "Characterization of two related Drosophila gamma-tubulin complexes that
RT differ in their ability to nucleate microtubules.";
RL J. Cell Biol. 144:721-733(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-852 (ISOFORM 1).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- SUBUNIT: Gamma-tubulin small complex (Gamma TuSC) is a heterotetrameric
CC complex which contains two molecules of gamma-tubulin, and one molecule
CC each of Dgrip84 and Dgrip91. The gamma-tubulin in this complex binds
CC preferentially to GDP over GTP.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=B;
CC IsoId=Q9XYP7-1; Sequence=Displayed;
CC Name=2; Synonyms=C;
CC IsoId=Q9XYP7-2; Sequence=VSP_001619;
CC -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28696.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF118379; AAD27816.1; -; mRNA.
DR EMBL; AE014298; AAF48971.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09502.1; -; Genomic_DNA.
DR EMBL; AY061148; AAL28696.1; ALT_INIT; mRNA.
DR RefSeq; NP_001285444.1; NM_001298515.1. [Q9XYP7-2]
DR RefSeq; NP_523409.1; NM_078685.3. [Q9XYP7-2]
DR RefSeq; NP_728265.1; NM_167663.2. [Q9XYP7-1]
DR AlphaFoldDB; Q9XYP7; -.
DR SMR; Q9XYP7; -.
DR BioGRID; 59246; 16.
DR IntAct; Q9XYP7; 1.
DR MINT; Q9XYP7; -.
DR STRING; 7227.FBpp0074544; -.
DR iPTMnet; Q9XYP7; -.
DR PaxDb; Q9XYP7; -.
DR PRIDE; Q9XYP7; -.
DR EnsemblMetazoa; FBtr0074776; FBpp0074545; FBgn0026430. [Q9XYP7-1]
DR EnsemblMetazoa; FBtr0074777; FBpp0074546; FBgn0026430. [Q9XYP7-2]
DR EnsemblMetazoa; FBtr0343590; FBpp0310187; FBgn0026430. [Q9XYP7-2]
DR GeneID; 32946; -.
DR KEGG; dme:Dmel_CG3917; -.
DR CTD; 32946; -.
DR FlyBase; FBgn0026430; Grip84.
DR VEuPathDB; VectorBase:FBgn0026430; -.
DR eggNOG; KOG2001; Eukaryota.
DR GeneTree; ENSGT00940000156697; -.
DR InParanoid; Q9XYP7; -.
DR OMA; SKLMTCC; -.
DR PhylomeDB; Q9XYP7; -.
DR SignaLink; Q9XYP7; -.
DR BioGRID-ORCS; 32946; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32946; -.
DR PRO; PR:Q9XYP7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0026430; Expressed in secondary oocyte and 30 other tissues.
DR ExpressionAtlas; Q9XYP7; baseline and differential.
DR Genevisible; Q9XYP7; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0008275; C:gamma-tubulin small complex; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:FlyBase.
DR GO; GO:0030953; P:astral microtubule organization; IMP:FlyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:FlyBase.
DR GO; GO:0007020; P:microtubule nucleation; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR Gene3D; 1.20.120.1900; -; 1.
DR InterPro; IPR007259; GCP.
DR InterPro; IPR040457; GCP_C.
DR InterPro; IPR042241; GCP_C_sf.
DR InterPro; IPR041470; GCP_N.
DR PANTHER; PTHR19302; PTHR19302; 1.
DR Pfam; PF04130; GCP_C_terminal; 1.
DR Pfam; PF17681; GCP_N_terminal; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..852
FT /note="Gamma-tubulin complex component 2 homolog"
FT /id="PRO_0000078115"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 747..779
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10037793"
FT /id="VSP_001619"
FT CONFLICT 171
FT /note="H -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 98505 MW; 38BE28083FE3E92B CRC64;
MYALLVFVER YSECKPVSES SSSTSLSAMG LPHGNKTSDV NSAAGSVPTT LAIASTSTIL
TTSQNVSGST RLSLTQSQDF PTSTPVNCKK ATESDTTPVV FVRRGPMDRN RGAGKDERND
LSVIKERVLN AVSDQSLSGY RSVTNKTGNS PKSMPNDLVT LTDVPDEYRT HLLWEYYKVD
GDKVPRAEIA AMPLLSQESM LLDELLHCLT GIRESLLVPQ KPIISAVGLA KYDTDFDIHT
HLDRSLTHQV REILPLASYF MGVQKIIAAT DGLGQVMNSL NEALQELTHD FYLIIVQAEQ
ELRHNRLTLQ KLLYYLQPTM WVMHEVWSSL VIIQLSDSRD AEVLTYLHER IKRLEGNKDA
QQLIIGLVRK AAKPYMRMLQ MWIQKGVIVD RHREFLVVDN EVIHRDELPE HYSDDYWERR
YTLRDEQIPS FLAKYSDKIL RTGKYLNVIR QCGKRVMPTQ EMNLEFDPTS ERHVSVINDA
YYFAARMLLD VLLTENDLMG HLQSVKRYLL LNQGDFTMQF MDACEDELTK NVDHVLPMTL
ENLLGLTLRI SSARNDPYKD DLHCELLPYD LVTQMSKIMK KEENWQAQPR LDLSGLECFA
FTYEVKWPCS LVLNHISISK YQMLFRQLFY CKHVERQLCK IWKENSIARQ FEPQAASLYR
AAFTLRQRMM NAIQNLEYYM MIEIIEPNWH IFIEKMKTVE NVDNVLRLHQ DFLDSCLKNC
MLTESSHLNR SIFKLCKICL KYCEFIQITQ RYFQDAELRS MVRDSADSSE SEQESLHCPQ
IETPLDPTDT FSERVRRFDL EFTQLLISFL KQINSMAKKN TADCFMNLVH RINFNAFYTD
QMDKMCVEDA IG
