TBG2_EUPCR
ID TBG2_EUPCR Reviewed; 462 AA.
AC P54404;
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-2 chain;
DE AltName: Full=Gamma-2-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; X85235; CAA59490.1; -; Genomic_DNA.
DR EMBL; Y09551; CAA70742.1; -; mRNA.
DR AlphaFoldDB; P54404; -.
DR SMR; P54404; -.
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-2 chain"
FT /id="PRO_0000048461"
FT REGION 441..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 462 AA; 52117 MW; FF63B755E9AC4846 CRC64;
MPREIITCQV GQCGNQIGME FWKQLCMEHG ISPEGILEEY ALDGEDRKDV FFYQADDEHY
VPRAVLIDLE PGVIKQIQNS PYSNLYNPEN FFVSKTMDGA GNNWAKGYCE GAKYEEEIIE
MIDREADGSD SLEGFVLTHS IAGGTGSGFG SYLLEKLNDH YPKKLVQTYS VFPNDNDIVV
QPYNCILSMK RLVLNADCVV VLDNTAITSI AVDRLKLLHP TISQVNSIVS TVMAASTTTL
RYPGYMNNDL VGLIASLVPT PRCHFLMTGY TPLSLNDQKV SSIRKTTVLD VMRRLLQTRN
IMTSGAIKKG AYMSILNIIQ GDVDPTQVHK SLQRIRERNV ANFIPWGPAS IQVALSKKSP
YIESDNKVSG LMLANHTGIR SIFQVLYGQY RQFRKRDAFL GTYRETKIFQ DNLDEFDSSE
EVVKDLIDEY AAAEKMDYIN RGKDDEDMDY DPRAPPNFRP IE
