TBG3_MAIZE
ID TBG3_MAIZE Reviewed; 421 AA.
AC Q41874;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Tubulin gamma-3 chain;
DE AltName: Full=Gamma-3-tubulin;
DE Flags: Fragment;
GN Name=TUBG3; Synonyms=TUBC, TUBG;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Black Mexican Sweet;
RA Canaday J., Stoppin V., Endle M.C., Lambert A.M.;
RT "Identification of two maize cDNAs encoding gamma-tubulin.";
RL Submitted (JAN-1995) 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, suggesting that it is involved in the minus-end
CC nucleation of microtubule assembly.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center {ECO:0000250|UniProtKB:P38557}.
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; X83696; CAA58671.1; -; mRNA.
DR AlphaFoldDB; Q41874; -.
DR SMR; Q41874; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q41874; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; 2.
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 Reference proteome.
FT CHAIN <1..421
FT /note="Tubulin gamma-3 chain"
FT /id="PRO_0000048473"
FT BINDING 94..100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 421 AA; 47541 MW; 7C2BC3B91EC77523 CRC64;
DVFFYQADDQ HFIPRSLLID LEPRVINGIQ NSEYRNLYNH ENIFVAEHGG GAGNNWASGY
HQGEQFVDDI MDMVDREADG SDSLEGFVLC HSIAGGTGSG MGSYLLETLN DRYSKKLVQT
YSVFPNQVET SDVVVQPYNS LLTLKRLTLN ADCVVVLDNT ALNRIAVERL HLSNPTFAQT
NSLVSTVMSA STTTLRYPGY MNNDLVGLLA SLIPTPRCHF LMTGYTPLTV ERQVNMIRKT
TVLDVMRRLL QTKNIMVSSY ARTKEASQAK YISILNIIQG EVDPTQVHES LQRIRERKLV
NFIDWAPASI QVALSRKSPY VQTTHRVSGL MLANHTSIRH LFSKCLGQYE KLRKKQAFLD
NYRKFPMFAD NDLSEFDESR EIIESLVDEY KACESPDYIK WGMEDPGEAN VVAALDSKLV
V