GCP6_MOUSE
ID GCP6_MOUSE Reviewed; 1769 AA.
AC G5E8P0; Q6PFC6; Q6ZPK3; Q8BWI2;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Gamma-tubulin complex component 6;
DE Short=GCP-6;
GN Name=Tubgcp6; Synonyms=Kiaa1669;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-656 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 921-1769.
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation
CC at the centrosome. {ECO:0000250|UniProtKB:Q96RT7}.
CC -!- SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2,
CC TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. {ECO:0000250|UniProtKB:Q96RT7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q96RT7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=G5E8P0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=G5E8P0-2; Sequence=VSP_058269, VSP_058270;
CC -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98230.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129420; BAC98230.1; ALT_INIT; mRNA.
DR EMBL; AC113069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466550; EDL04376.1; -; Genomic_DNA.
DR EMBL; AK052441; BAC34992.1; -; mRNA.
DR EMBL; BC057626; AAH57626.1; -; mRNA.
DR CCDS; CCDS49697.1; -. [G5E8P0-1]
DR RefSeq; NP_001156791.1; NM_001163319.1. [G5E8P0-1]
DR AlphaFoldDB; G5E8P0; -.
DR SMR; G5E8P0; -.
DR IntAct; G5E8P0; 10.
DR MINT; G5E8P0; -.
DR STRING; 10090.ENSMUSP00000104977; -.
DR iPTMnet; G5E8P0; -.
DR PhosphoSitePlus; G5E8P0; -.
DR jPOST; G5E8P0; -.
DR MaxQB; G5E8P0; -.
DR PaxDb; G5E8P0; -.
DR PRIDE; G5E8P0; -.
DR ProteomicsDB; 265736; -. [G5E8P0-1]
DR ProteomicsDB; 265737; -. [G5E8P0-2]
DR Antibodypedia; 52528; 123 antibodies from 24 providers.
DR Ensembl; ENSMUST00000109353; ENSMUSP00000104977; ENSMUSG00000051786. [G5E8P0-1]
DR GeneID; 328580; -.
DR KEGG; mmu:328580; -.
DR UCSC; uc007xfh.2; mouse. [G5E8P0-1]
DR UCSC; uc056yzw.1; mouse.
DR CTD; 85378; -.
DR MGI; MGI:2146071; Tubgcp6.
DR VEuPathDB; HostDB:ENSMUSG00000051786; -.
DR eggNOG; KOG2000; Eukaryota.
DR GeneTree; ENSGT00940000157810; -.
DR HOGENOM; CLU_002518_0_0_1; -.
DR InParanoid; G5E8P0; -.
DR OMA; HIRVGEN; -.
DR OrthoDB; 110079at2759; -.
DR PhylomeDB; G5E8P0; -.
DR TreeFam; TF106321; -.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR BioGRID-ORCS; 328580; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Tubgcp6; mouse.
DR PRO; PR:G5E8P0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; G5E8P0; protein.
DR Bgee; ENSMUSG00000051786; Expressed in embryonic post-anal tail and 172 other tissues.
DR ExpressionAtlas; G5E8P0; baseline and differential.
DR Genevisible; Q6PFC6; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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:0000931; C:gamma-tubulin large complex; ISO:MGI.
DR GO; GO:0008275; C:gamma-tubulin small complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; ISO:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR Gene3D; 1.20.120.1900; -; 1.
DR InterPro; IPR007259; GCP.
DR InterPro; IPR045818; GCP6_N.
DR InterPro; IPR040457; GCP_C.
DR InterPro; IPR042241; GCP_C_sf.
DR InterPro; IPR041470; GCP_N.
DR PANTHER; PTHR19302; PTHR19302; 1.
DR Pfam; PF19340; GCP6_N; 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; Microtubule;
KW Reference proteome.
FT CHAIN 1..1769
FT /note="Gamma-tubulin complex component 6"
FT /id="PRO_0000436164"
FT REGION 809..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 249..281
FT /note="PQIVDQWEDEGFQSASNLTPDSQSEPSMTPDLD -> VFLSLSVTLEVWKIL
FT LPGTVGKLLSKPQVSRQS (in isoform 2)"
FT /id="VSP_058269"
FT VAR_SEQ 282..1769
FT /note="Missing (in isoform 2)"
FT /id="VSP_058270"
SQ SEQUENCE 1769 AA; 197192 MW; 556E139E9CAE51EE CRC64;
MASITQLFDD LCEALLPAAQ ARPGQRSVNR KRAKRSLKRV AYNALFANLF QEDTHQRQPD
SSKLPVKNKV LMLSFDLRVG GLGPEADRLE ELVEKLEAAP DCPFVEVASV LDLLVQLAGS
GPPQVLRRKR DYFFNNKHAG RNIPYSGYDC YDLSVFEMDV RSFISGEENL CHHTVQEALQ
VMEAAPGTGL PTVGLFSIGD SCGDRFERDT RVSLFGALVH SRTYDMDVRL DLPPVPDSAD
FSGLAIKVPQ IVDQWEDEGF QSASNLTPDS QSEPSMTPDL DLWEAVLTYE ASKRRCWERI
GCPPGHREEP YLTEAGRDAF DRFCRLRHGE LQALSGGLLQ APKPVLVEES ELVKDSLNVL
LGVVSATFSL CRPTQAFVVE PGVHVSGASP ESISSILSEV AEYGTCYTRL SHFSLQPVVG
SLCSRGLVFQ AFTSGLRRYL QYYRACVLST PPTLSLLTIG FLFKKLGRQL RYLAELCGVG
TVSLATSGEP RAVFPTGVKL LSYLYQEALD NCSNEHYPVL LSLLKTSCEP YTRFIHDWVY
SGVFRDVYGE FMIQVNHEYL SFRDKFYWTH GYVLISKEVE DCVPVFLKHI AHDVYVCGKT
INLLKLCCPR HYLCWSDVPV PRISVIFSLE ELKEIEKDCA VYVGRMERVA RHSCISKEEK
ELRMEIAKQE LIVHAREAAS RVLSELSDRQ MAEQIAQDTR KREQFQRLKE QFVKDQERRL
AARQEELDDD FSYARELRDR EKRLKALEEE LERKARQALV DHYSKLSAEA ARREQKALWR
IQRHRLESAR LRFLLEDQKC IQEMLRDMEA QQPQEPPSVF PSTGSQVTST GPEHAGEGHS
CDPGFTELHW GCPSLPCAST PSVPKSATEG ADDSGAGPFS TGLSITDFLP VDSGEEQPVE
NTGVPFLEVA LQTICSDLSP VAPEPAALTA GGPQATQSEY DFNTILRPAM ATSLSPGPFQ
DVQNSVDSDK QHLLGDMSTK VDSYIHDMQE TLPCPHPLSH ATPVEGSLQP VGQLLEHMSE
TTVSTESHAS GMAPCQQLSI SRHVSDANIK VGDYMSDVAL PRPRWNVHGH VSEASIGVGE
NMAEVAPSRP RWNVHGHVSD ASIKIGENMS DVAPSRTRWN IHGHVSDASI KVGENVSDVT
PSRPRWNVHG HVSEASIKVG ENVSDVTPSR PRWNVHGHVS EASIKVGENV SDVTPSRPRW
NVHGHVSDAS IRIGENVSDT DLDLQQRGCA QPPLILEEPL PEAEADLKPH QCPPAHVSEA
VLGVEAQSPA LECGPQLPEK TKPTVCSGFG RTEEGSLQTK TLVAEPSMLG SGIPEEKGPG
KSRDAEDLSP CLPSSSQEDT AVPSSPGPSD EVSNTEAEAR RWGKEQAYLT DLTKLYHLEQ
YPDSYDSMSE PPVAHLVHHM LPRAFAFPVD PQVQSAVDES AVQLSELLTL PVLMKRSLMA
PLAAHVSLVS KAAVDYFFVE LHLETHFEAL RHFLLMEDGE FAQSLSDLLF EKLGAGQTPG
ELLNPLVLNS ILSKALQYSL HGDTPHASNL SFALKYLPEV FAPNAPDVLS CLELRYKVDW
PLNIVITESC LNKYSGIFSF LLQLKLMMWT LKDICFHLKR TALVSHTAGS VQFRQLQLFK
HEMQHFVKVI QGYIANQILH VSWCEFRARL AVVGDLEEIQ RAHAEYLHRA VFRGLLTEKA
APVMNIIHSI FSLVLKFRSQ LISQNWGPAT GPRGAEHPNF PLMQQSYSTF KYYSHFLFKV
VTKLVNRGYQ PHLEDFLLRI NFNNYYQDS
