ID F2Z562_PIG Unreviewed; 394 AA.
AC F2Z562;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
GN Name=TUBG1 {ECO:0000313|Ensembl:ENSSSCP00000018429.5};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000018429.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000018429.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000018429.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000018429.5}
RP IDENTIFICATION.
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. Pericentriolar matrix component that
CC regulates alpha/beta chain minus-end nucleation, centrosome duplication
CC and spindle formation. {ECO:0000256|ARBA:ARBA00025618}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR AlphaFoldDB; F2Z562; -.
DR SMR; F2Z562; -.
DR PeptideAtlas; F2Z562; -.
DR Ensembl; ENSSSCT00000018934.5; ENSSSCP00000018429.5; ENSSSCG00000036106.3.
DR GeneTree; ENSGT00940000156957; -.
DR HOGENOM; CLU_015718_1_0_1; -.
DR TreeFam; TF300477; -.
DR Proteomes; UP000008227; Chromosome 12.
DR Bgee; ENSSSCG00000036106; Expressed in prefrontal cortex and 45 other cell types or tissues.
DR ExpressionAtlas; F2Z562; baseline and differential.
DR Genevisible; F2Z562; SS.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000930; C:gamma-tubulin complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0007020; P:microtubule nucleation; IEA:InterPro.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR InterPro; IPR002454; Gamma_tubulin.
DR InterPro; IPR000217; Tubulin.
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 PRINTS; PR01164; GAMMATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 354..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..210
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT REGION 226..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 43523 MW; 10AF9CD7780549E9 CRC64;
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD
IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSV
HHHVGQHHHP ALPRLHEQRP HRPHRLAHPH TAAPLPHDRL HPAHHGPVGG QREEDHGPGR
HEAAAAAQER DGVHRPGSPD QPLLHRHPQH HPGGGGPHPG PQEPAADPGT EAGQLHPLGP
SQHPGGPVEE VALPAFCPQG QWAHDGQPHQ HLLRESHSLH LFSHSHCPGC ASPFSILTIS
ASGFFFFFFF FVFCFLGPHP QHMEVSRLGV KSEL
//
