ID   TBG_RETFI               Reviewed;         478 AA.
AC   P54405;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Tubulin gamma chain;
DE   AltName: Full=Gamma-tubulin;
OS   Reticulomyxa filosa.
OC   Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC   Reticulomyxidae; Reticulomyxa.
OX   NCBI_TaxID=46433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9127728;
RA   Kube-Granderath E., Schliwa M.;
RT   "Unusual distribution of gamma-tubulin in the giant fresh water amoeba
RT   Reticulomyxa filosa.";
RL   Eur. J. Cell Biol. 72:287-296(1997).
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; X97250; CAA65885.1; -; mRNA.
DR   AlphaFoldDB; P54405; -.
DR   SMR; P54405; -.
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..478
FT                   /note="Tubulin gamma chain"
FT                   /id="PRO_0000048478"
FT   REGION          451..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         141..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   478 AA;  53559 MW;  4702908E7AEBB98C CRC64;
     MPREIITLQV GQCGNQIGTE FWGRLIAEHG IGPDGIVKEF ATEGTDRKDV FFYQADDQHY
     IPRALLIDLE PRVINSLQES EFKNLWNPEN VYIDSQGGGA GNNWAVGYTH ATEKYEHIMD
     MIDREDNSDS LEGFVLTHSI AGGTGSGFGS HMLEQLTDRY PKKIIQTYSV FPNDSERSSV
     VVHPYNSVLA LKRLILNADA VVVIDNTSLH RIADERLQLD FASFKETNSI ISTVMAASTT
     TLRYPGYMNN DLVGLIASLV PTPRAHFLMT SFTPLVIKGA QRRIQKTSVL DVMRRLLQPK
     NIMVSCGTKK GVYVSILDII RGDVDPTDIH KSLQRIREKK IVNFIPWGPA SIQVALSKQS
     PYANVPYRVS GCMMANHSNL GNLFARIIRT YDILRKRNAF LNVYKETPVF SENLDEFEDA
     KETITNLIEE YKAIQTSDYI NWGMKQQQSQ ISQKESSSLA NENGNGANNK PGKSAMAL