ID   TBG1_XENLA              Reviewed;         451 AA.
AC   P23330;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Tubulin gamma-1 chain;
DE   AltName: Full=Gamma-1-tubulin;
DE            Short=xGAM;
GN   Name=tubg1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1840506; DOI=10.1016/0092-8674(91)90390-k;
RA   Stearns T., Evans L., Kirschner M.;
RT   "Gamma-tubulin is a highly conserved component of the centrosome.";
RL   Cell 65:825-836(1991).
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}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:P23258}. Note=Localizes to mitotic spindle
CC       microtubules. {ECO:0000250|UniProtKB:P23258}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M63446; AAA49720.1; -; mRNA.
DR   PIR; A39528; UBXLG.
DR   PDB; 6TF9; EM; 4.80 A; TP1/hP1/iP1/kP1/lP1/mP1/nP1/oP1/pP1/qP1/rP1/sP1/tP1/wP1=1-451.
DR   PDBsum; 6TF9; -.
DR   AlphaFoldDB; P23330; -.
DR   SMR; P23330; -.
DR   IntAct; P23330; 1.
DR   PRIDE; P23330; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000930; C:gamma-tubulin complex; IEA:InterPro.
DR   GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR   GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Tubulin gamma-1 chain"
FT                   /id="PRO_0000048470"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   451 AA;  51168 MW;  52195DA5921EF246 CRC64;
     MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
     IPRAVLLDLE PRVIHSILNS PYANLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD
     IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSH
     VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST
     TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
     KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL
     SRKSPYLPSA HRVSGLMMAN HTNISSLFER TCRQYDKLRK REAFLEQFRK EDIFKDNFDE
     LDNSREIVQQ LIDEYHAATR PDYISWGTQD K