ID Q8AWI2_ONCMY Unreviewed; 192 AA.
AC Q8AWI2;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
DE Flags: Fragment;
GN Name=alpha tubulin {ECO:0000313|EMBL:AAN86582.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:AAN86582.1};
RN [1] {ECO:0000313|EMBL:AAN86582.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:AAN86582.1};
RA Schwindt A.R., Alonso M., Leong J.C., Schreck C.B.;
RT "Stress-induced differential gene expression in the brains of juvenile
RT steelhead trout (Oncorhynchus mykiss).";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 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; AY150303; AAN86582.1; -; mRNA.
DR AlphaFoldDB; Q8AWI2; -.
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 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; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; TUBULIN; 1.
DR PANTHER; PTHR11588:SF417; TUBULIN ALPHA-4 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 SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 2: Evidence at transcript 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 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}.
FT DOMAIN 1..127
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAN86582.1"
FT NON_TER 192
FT /evidence="ECO:0000313|EMBL:AAN86582.1"
SQ SEQUENCE 192 AA; 21412 MW; B7E0FE2E6533A2B0 CRC64;
DRTRKLVDQC TGLQGFLIFH SFGGGTGSGF TSLLMERLSV DYGKKSKLEF AIYPAPQVST
AVVEPYNSIL TTHTTLEHSD CAFMVDNEAI YDICRRNLDI ERPTYTNLNR LIGQIVSSIT
ASLRFDGALN VDLTEFQTNL VPYPRIHFPL ATYAPVISAE KAYHEMLSVA EITNACFEPA
NQMVKCDPRH GK
//
