ID   TBG2_EUPOC              Reviewed;         461 AA.
AC   P90548;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Tubulin gamma-2 chain;
DE   AltName: Full=Gamma-2-tubulin;
OS   Euplotoides octocarinatus (Freshwater ciliate) (Euplotes octocarinatus).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX   NCBI_TaxID=2716877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tan M., Liang A., Heckmann K.;
RT   "The two gamma tubulin genes of Euplotes octocarinatus code for a slightly
RT   different protein.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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; Y09553; CAA70744.1; -; Genomic_DNA.
DR   EMBL; Y17254; CAA76714.1; -; Genomic_DNA.
DR   AlphaFoldDB; P90548; -.
DR   SMR; P90548; -.
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   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..461
FT                   /note="Tubulin gamma-2 chain"
FT                   /id="PRO_0000048463"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   461 AA;  51952 MW;  DBED624C4B824A46 CRC64;
     MPREIITCQV GQCGNQIGME FWKQLCMEHG INPEGILEDF AVNGEDRKDV FFYQADDEHY
     VPRAVLIDLE PRVINGIQKS AYSSLYNPEN IYIAKHGGGA GNNWGRGYTD AEKVQDEILE
     MIDREADGSD SLEGFVLTHS IAGGTGSGFG SYLLERLNDH YPKKLIQTYS VFPIENDVVV
     QPYNCLLSIK RLTLNADCVV VLDNNALTSI AVDRLKILQP TFSQINSIVS TVMAASTTTL
     RYPGYMNNDM VGLIASLVPT PRCHFLMTGY TPLSLDQKFT SVRKTTVLDV MRRLLQTKNI
     MVTGAVKKGA YMSILNVIQG DVDPTQVHKS LQRIRERKLA NFIPWGPASI QVALSKKSPY
     IDSGHKVSGL MLANHTGIRS IFKVLYDQYR TFRKRDAYMN IFKQTKIFED NLDEFDSSDE
     VVKSLIDEYA AAEKMDYINW GSDDDDMQFD PREPPKFSNI Q