TBG_YEAST
ID TBG_YEAST Reviewed; 473 AA.
AC P53378; D6VYL3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Tubulin gamma chain;
DE AltName: Full=Gamma-tubulin;
GN Name=TUB4; OrderedLocusNames=YLR212C; ORFNames=L8167.21;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CHARACTERIZATION.
RC STRAIN=Y270;
RX PubMed=8557744; DOI=10.1083/jcb.131.6.1775;
RA Sobel S.G., Snyder M.;
RT "A highly divergent gamma-tubulin gene is essential for cell growth and
RT proper microtubule organization in Saccharomyces cerevisiae.";
RL J. Cell Biol. 131:1775-1788(1995).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8707827; DOI=10.1083/jcb.134.2.429;
RA Spang A., Geissler S., Grain K., Schiebel E.;
RT "Gamma-tubulin-like Tub4p of Saccharomyces cerevisiae is associated with
RT the spindle pole body substructures that organize microtubules and is
RT required for mitotic spindle formation.";
RL J. Cell Biol. 134:429-441(1996).
RN [5]
RP INTERACTION WITH SPC72.
RX PubMed=9670012; DOI=10.1093/emboj/17.14.3952;
RA Knop M., Schiebel E.;
RT "Receptors determine the cellular localization of a gamma-tubulin complex
RT and thereby the site of microtubule formation.";
RL EMBO J. 17:3952-3967(1998).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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. TUB4 is an important
CC spindle pole body component that organizes both cytoplasmic and nuclear
CC microtubule arrays.
CC -!- SUBUNIT: Interacts with SPC72, SPC97 and SPC98.
CC {ECO:0000269|PubMed:9670012}.
CC -!- INTERACTION:
CC P53378; P38863: SPC97; NbExp=8; IntAct=EBI-19013, EBI-17786;
CC P53378; P53540: SPC98; NbExp=4; IntAct=EBI-19013, EBI-17794;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body.
CC -!- MISCELLANEOUS: Present with 7200 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; U14913; AAB67442.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09529.1; -; Genomic_DNA.
DR PIR; S48563; S48563.
DR RefSeq; NP_013313.1; NM_001182099.1.
DR PDB; 5FLZ; EM; 6.90 A; C/D=1-473.
DR PDB; 5FM1; EM; 8.00 A; C/D=1-473.
DR PDB; 7M2W; EM; 3.00 A; A/B/C/D=1-473.
DR PDB; 7M2X; EM; 3.60 A; A/B=1-473.
DR PDB; 7M2Y; EM; 4.03 A; A/B=1-473.
DR PDB; 7M2Z; EM; 3.70 A; A/B=1-473.
DR PDBsum; 5FLZ; -.
DR PDBsum; 5FM1; -.
DR PDBsum; 7M2W; -.
DR PDBsum; 7M2X; -.
DR PDBsum; 7M2Y; -.
DR PDBsum; 7M2Z; -.
DR AlphaFoldDB; P53378; -.
DR SMR; P53378; -.
DR BioGRID; 31480; 1071.
DR ComplexPortal; CPX-1198; Gamma tubulin small complex.
DR DIP; DIP-821N; -.
DR IntAct; P53378; 9.
DR MINT; P53378; -.
DR STRING; 4932.YLR212C; -.
DR iPTMnet; P53378; -.
DR MaxQB; P53378; -.
DR PaxDb; P53378; -.
DR PRIDE; P53378; -.
DR EnsemblFungi; YLR212C_mRNA; YLR212C; YLR212C.
DR GeneID; 850909; -.
DR KEGG; sce:YLR212C; -.
DR SGD; S000004202; TUB4.
DR VEuPathDB; FungiDB:YLR212C; -.
DR eggNOG; KOG1374; Eukaryota.
DR GeneTree; ENSGT00940000174463; -.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; P53378; -.
DR OMA; EHGINKE; -.
DR BioCyc; YEAST:G3O-32329-MON; -.
DR PRO; PR:P53378; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P53378; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0008275; C:gamma-tubulin small complex; IDA:SGD.
DR GO; GO:0005822; C:inner plaque of spindle pole body; IDA:SGD.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005824; C:outer plaque of spindle pole body; IDA:SGD.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; HDA:SGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:SGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0000212; P:meiotic spindle organization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IDA:SGD.
DR GO; GO:0051417; P:microtubule nucleation by spindle pole body; IMP:SGD.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:SGD.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IMP:SGD.
DR GO; GO:0010968; P:regulation of microtubule nucleation; IC:ComplexPortal.
DR CDD; cd02188; gamma_tubulin; 1.
DR DisProt; DP01513; -.
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..473
FT /note="Tubulin gamma chain"
FT /id="PRO_0000048481"
FT REGION 33..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 11..28
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 131..144
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 180..197
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 315..325
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:7M2W"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 416..440
FT /evidence="ECO:0007829|PDB:7M2W"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:7M2W"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:7M2W"
SQ SEQUENCE 473 AA; 52627 MW; 3EA6F89E4A9A12F8 CRC64;
MGGEIITLQA GQCGNHVGKF LWSQLAKEHA IGTDGLSQLP DSSTERDDDT KPFFRENSRN
KFTPRAIMMD SEPSVIADVE NTFRGFFDPR NTWVASDGAS AGNSWANGYD IGTRNQDDIL
NKIDKEIDST DNFEGFQLLH SVAGGTGSGL GSNLLEALCD RYPKKILTTY SVFPARSSEV
VVQSYNTILA LRRLIEDSDA TVVFDNASLL NISGKVFRNP NIDLQHTNQL ISTIISSVTN
SIRFPSYMYS SMSSIYSTLI PSPELHFLSP SFTPFTSDYI HDDIAHKGHS SYDVMLDLLD
PSNSLVSTAM NNPTYFNVYN TIIGNVEPRQ ISRAMTKLQQ RIKFPSWSSS AMHVNIGRRS
PYLPLQPNEN EVSGMMLSNM STVVNVFENA CNTFDKVFAK GAFLNNYNVG DLFQSMQNVQ
DEFAESREVV QSLMEDYVAA EQDSYLDDVL VDDENMVGEL EEDLDADGDH KLV
