TBG_SCHJP
ID TBG_SCHJP Reviewed; 446 AA.
AC Q9Y882;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Tubulin gamma chain;
DE AltName: Full=Gamma-tubulin;
GN Name=tug1; Synonyms=gtb1;
OS Schizosaccharomyces japonicus (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=4897;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Horio T., Shimizu M., Akashi T., Tanaka K.;
RT "Isolation and characterization of gamma-tubulin gene from
RT Schizosaccharomyces japonicus.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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, spindle pole body {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AF159163; AAD41900.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y882; -.
DR SMR; Q9Y882; -.
DR VEuPathDB; FungiDB:SJAG_01215; -.
DR OMA; EHGINKE; -.
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:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN 1..446
FT /note="Tubulin gamma chain"
FT /id="PRO_0000048479"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 446 AA; 50159 MW; B86BBE9E54A94A2C CRC64;
MGREIITLQA GQCGNQVGSQ FWQQLCLEHG ICPDGTLEDF ATEGLDRKDV FFYQSDDTRY
IPRAILLDLE PRVVNNILSD TYGSLYNPEN IFVATDGGGA GNNWAHGYAH AEKIFEDIVD
MIDREAEGSD SLEGFSLLHS IAGGTGSGLG SYLLERLNDR FPKKIVQTYS VFPNNRSVSD
VVVQPYNSLL TLKRLTLNAD AVVVLDNAAL AHIAADRLHI QNPTFHQQNQ LVSTVMSAST
TTLRYPGYMN NDLVSIIASL IPTPRCHFLS TSYTPFTSQQ VEDARTIRKT TVLDVMRRLL
QPKNRMVSVN PGKQSCFISI LNIIQGEADP NDVHKSLLRI RERKLATFIP WGPASIQVAL
SKKSPYIKTN HRVSGLMLAN HTSIASLFKR TLDQYDRLRK RNAFLDQYRK ESIFENSLDE
FDNSREVVAD LIREYEACEQ PEYLSM
