TBG1_CANLF
ID TBG1_CANLF Reviewed; 451 AA.
AC Q9GKK5;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Tubulin gamma-1 chain;
DE AltName: Full=Gamma-1-tubulin;
DE AltName: Full=Gamma-tubulin complex component 1;
DE Short=GCP-1;
GN Name=TUBG1; Synonyms=TUBG;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11683730; DOI=10.1046/j.1365-2052.2001.0730j.x;
RA Sidjanin D.J., Xue F., McElwee J., Johnson J.L., Holmgren C., Mellersh C.,
RA Ostrander E.A., Acland G.M., Aguirre G.D.;
RT "Cloning of canine gamma-tubulin (TUBG1) cDNA and mapping to CFA9.";
RL Anim. Genet. 32:328-329(2001).
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. Pericentriolar matrix component that
CC regulates alpha/beta chain minus-end nucleation, centrosome duplication
CC and spindle formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TUBGCP2, TUBGCP3 and B9D2 (By similarity).
CC Interacts with CDK5RAP2; the interaction is leading to centrosomal
CC localization of TUBG1 and CDK5RAP2. Interacts with PIFO. Interacts with
CC SAS6 and NUP62 at the centrosome (By similarity). Interacts with EML3
CC (phosphorylated form) and HAUS8 (By similarity).
CC {ECO:0000250|UniProtKB:P23258, ECO:0000250|UniProtKB:P83887}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:P23258}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:P23258}. Note=Localizes to
CC mitotic spindle microtubules. {ECO:0000250|UniProtKB:P23258}.
CC -!- PTM: Phosphorylation at Ser-131 by BRSK1 regulates centrosome
CC duplication, possibly by mediating relocation of gamma-tubulin and its
CC associated proteins from the cytoplasm to the centrosome.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AF212974; AAG43544.1; -; mRNA.
DR RefSeq; NP_001003105.1; NM_001003105.1.
DR AlphaFoldDB; Q9GKK5; -.
DR SMR; Q9GKK5; -.
DR DIP; DIP-29733N; -.
DR IntAct; Q9GKK5; 1.
DR STRING; 9615.ENSCAFP00000021979; -.
DR PaxDb; Q9GKK5; -.
DR GeneID; 403695; -.
DR KEGG; cfa:403695; -.
DR CTD; 7283; -.
DR eggNOG; KOG1374; Eukaryota.
DR InParanoid; Q9GKK5; -.
DR OrthoDB; 687389at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..451
FT /note="Tubulin gamma-1 chain"
FT /id="PRO_0000048464"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 131
FT /note="Phosphoserine; by BRSK1"
FT /evidence="ECO:0000250|UniProtKB:P83887"
SQ SEQUENCE 451 AA; 51202 MW; 7CAA59CF649E600C CRC64;
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD
IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD
VVVQPYNSLL TLKRLTQNAD CVVVLDNTTL NRIATNRLHI QNPSFFQINQ LVSTIMSAST
TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL
SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK REAFLEQFRK EDIFKENFDE
LDTSREVVHQ LIDEYHAATR PDYISWGAQE Q
