ID A0A3Q1CDN5_AMPOC Unreviewed; 451 AA.
AC A0A3Q1CDN5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Tubulin gamma chain {ECO:0000256|RuleBase:RU000352};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000017966.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000017966.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR AlphaFoldDB; A0A3Q1CDN5; -.
DR STRING; 80972.ENSAOCP00000017966; -.
DR Ensembl; ENSAOCT00000032926.1; ENSAOCP00000017966.1; ENSAOCG00000023133.1.
DR GeneTree; ENSGT00940000156957; -.
DR OMA; FWKKLCA; -.
DR OrthoDB; 5476567at2759; -.
DR Proteomes; UP000257160; Unplaced.
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: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 CDD; cd02188; gamma_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 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; IPR023123; Tubulin_C.
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 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 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:UP000257160}.
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 451 AA; 50989 MW; 5D29D7CC492D2178 CRC64;
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
IPRAVLLDLE PRVIHSILNS PYANLYNPEN IYLSEHGGGA GNNWASGYSQ GKKIQEDIFD
IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLEKLNDR YPKKLVQTYS VFPNQDEMSD
VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST
TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
KNVMVSTGRE RQPSHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLASFIP WGPASIQVAL
SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK REAFLEQFRK EDIFKDNFDE
LDNSREVVQQ LVDEYSAATR PDYISWGTQE Q
//