ID A0A1D5NU82_CHICK Unreviewed; 452 AA.
AC A0A1D5NU82;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
GN Name=TUBG1 {ECO:0000313|Ensembl:ENSGALP00010030915.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010030915.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010030915.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010030915.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU000352}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC hollow water-filled tube with an outer diameter of 25 nm and an inner
CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC form protofilaments running lengthwise along the microtubule wall with
CC the beta-tubulin subunit facing the microtubule plus end conferring a
CC structural polarity. Microtubules usually have 13 protofilaments but
CC different protofilament numbers can be found in some organisms and
CC specialized cells. {ECO:0000256|ARBA:ARBA00011747}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR RefSeq; XP_015155126.1; XM_015299640.1.
DR AlphaFoldDB; A0A1D5NU82; -.
DR SMR; A0A1D5NU82; -.
DR STRING; 9031.ENSGALP00000043891; -.
DR PaxDb; 9031-ENSGALP00000004979; -.
DR Ensembl; ENSGALT00010051826.1; ENSGALP00010030915.1; ENSGALG00010021375.1.
DR VEuPathDB; HostDB:geneid_420025; -.
DR GeneTree; ENSGT00940000156957; -.
DR InParanoid; A0A1D5NU82; -.
DR Reactome; R-GGA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-GGA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-GGA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-GGA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-GGA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-GGA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-GGA-8854518; AURKA Activation by TPX2.
DR Proteomes; UP000000539; Chromosome 27.
DR Bgee; ENSGALG00000030003; Expressed in brain and 13 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
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:0007020; P:microtubule nucleation; IBA:GO_Central.
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; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF7; TUBULIN GAMMA CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D5NU82};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539}.
FT DOMAIN 48..247
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 249..393
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 452 AA; 50331 MW; 32FFBA764FE24C39 CRC64;
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
IPRAVLLDLE PRVIHSILNS PYANLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD
IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVETYS VFPNQDEMSD
VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST
TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL
SRKSPYLPSA HRVSGLMMAN HTNISSTHLL RLTKPQWPTD VGLVGSPSLQ HIGILDLLGW
GPIHLLCILW AHPHPLVPFS ESRTPSARPK AA
//
