ID   TBG1_EUPCR              Reviewed;         462 AA.
AC   P54403;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Tubulin gamma-1 chain;
DE   AltName: Full=Gamma-1-tubulin;
OS   Euplotes crassus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Hypotrichia; Euplotida; Euplotidae; Moneuplotes.
OX   NCBI_TaxID=5936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=9524221; DOI=10.1016/s0378-1119(98)00068-7;
RA   Tan M., Heckmann K.;
RT   "The two gamma-tubulin-encoding genes of the ciliate Euplotes crassus
RT   differ in their sequences, codon usage, transcription initiation sites and
RT   poly(A) addition sites.";
RL   Gene 210:53-60(1998).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC       chain is found at microtubule organizing centers (MTOC) such as the
CC       spindle poles or the centrosome, suggesting that it is involved in the
CC       minus-end nucleation of microtubule assembly.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X85234; CAA59489.1; -; Genomic_DNA.
DR   EMBL; Y09550; CAA70741.1; -; mRNA.
DR   PIR; S53084; S53084.
DR   AlphaFoldDB; P54403; -.
DR   SMR; P54403; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000930; C:gamma-tubulin complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   CDD; cd02188; gamma_tubulin; 1.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 1.
DR   InterPro; IPR002454; Gamma_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; PTHR11588; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01164; GAMMATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..462
FT                   /note="Tubulin gamma-1 chain"
FT                   /id="PRO_0000048460"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   462 AA;  51959 MW;  773A5DE377DF53F6 CRC64;
     MPREIITCQV GQCGNQIGME FWKQLCMEHG INPEGILEEY AQNGEDRKDV FFYQADDEHY
     VPRAVLIDLE PRVINGIQKS PYASLYNPEN IFISKHGGGA GNNWGRGYCD AEKVQEEIIE
     MIDREADGSD SLEGFVLTHS IAGGTGSGFG SYLLERLNDH YPKKLIQTYS VFPNENDVVV
     QPYNCLLSMK RLILNADCVV VLDNTALTSI AVDRLKLLQP TFPQINSIVS TVMAASTTTL
     RYPGYMNNDL VGLIASLVPT PRCHFLMTGY TPLSLIDQKV TSVRKTTVLD VMRRLLQTKN
     IMATGAIKKG AYMSILNIIQ GDVDPTQVHK SLQRIRERKL ANFIPWGPAS IQVALSKKSP
     YMESGHKVSG LMLANHTGIR SIFKVIYDQY RTFRKRDAYM NIFKQTKIFE DNLDEFDSSD
     EVVKSLIEDS AAAEKMDYIN WGNDDDDMGY DPRAPPNFSS MQ