ID A0A096M087_POEFO Unreviewed; 450 AA.
AC A0A096M087;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000024828.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000024828.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC consisting of laterally associated linear protofilaments composed of
CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC GTPase activity of alpha-tubulin. {ECO:0000256|RuleBase:RU000352}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
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|RuleBase:RU000352}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; AYCK01016441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007575085.1; XM_007575023.2.
DR AlphaFoldDB; A0A096M087; -.
DR STRING; 48698.ENSPFOP00000024828; -.
DR Ensembl; ENSPFOT00000030578.1; ENSPFOP00000024828.1; ENSPFOG00000022838.1.
DR GeneID; 103153931; -.
DR KEGG; pfor:103153931; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00950000182825; -.
DR OMA; CGINYQS; -.
DR OrthoDB; 3014531at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd02186; alpha_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; IPR002452; Alpha_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:SF462; TUBULIN ALPHA CHAIN; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000028760}.
FT DOMAIN 49..246
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 248..393
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
SQ SEQUENCE 450 AA; 50079 MW; 1F1522303131F6D9 CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDPVLD
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLTVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGVDSV EGEDEEGEEY
//
