ID   TBG_ANEPH               Reviewed;         472 AA.
AC   P34785;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
GN   Name=TUBG;
OS   Anemia phyllitidis (Fern) (Osmunda phyllitidis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Schizaeales; Anemiaceae; Anemia.
OX   NCBI_TaxID=12940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8219092; DOI=10.1007/bf00019306;
RA   Fuchs U., Moepps B., Maucher H.P., Schraudolf H.;
RT   "Isolation, characterization and sequence of a cDNA encoding gamma-tubulin
RT   protein from the fern Anemia phyllitidis L. Sw.";
RL   Plant Mol. Biol. 23:595-603(1993).
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, suggesting that it is involved in the minus-end
CC       nucleation of microtubule assembly.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center {ECO:0000250|UniProtKB:P38557}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X69188; CAA48932.1; -; mRNA.
DR   PIR; S39553; S39553.
DR   AlphaFoldDB; P34785; -.
DR   SMR; P34785; -.
DR   PRIDE; P34785; -.
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; 2.
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..472
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048444"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   472 AA;  53138 MW;  F1E76F51BCC2DA09 CRC64;
     MPREIITLQV GQCGNQIGME FWKQLCLEHG ISKEGMLEDF ATQGGDRKDV FFYQADDEHY
     IPRALLLDLE PRVINGIQNS EYRNLYNHEN VFVADHGGGA GNNWASGYHQ GEQVEEDIMD
     MIDREADGSD SLEGFVLCHS IAGGTGSGMG SYLLEALNDR YSKKLVQTYS VFPNQMETSD
     VVVQPYNSLL TLNKRLTINA DCVVVLDNTA LNRIAVDRLH IPNPTFAQTN SLVSTVMSAS
     TTTLRYPGYM NNDLVGLVAS LIPTPRCHFL MTGYTPLTVE RQANAIRKTT VLDVMRRLLQ
     AKNIMVSSYA RTKEASQAKY ISILNIIQGE VDPTQVHKSL QRIRERKLAN FIEWGPASIQ
     VALSRKSPYV QTAHRVSGLM LASHTSIRHL FSKCINQYEK LRKKQAFLDN YRKFPMFADN
     DLTEFDESRE IVQSLVDEYK ACESADYIKW GMEDRSKTLS ADGTMDLSLP SS