ID L7N0T5_CIOIN Unreviewed; 451 AA.
AC L7N0T5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352};
GN Name=LOC100181688 {ECO:0000313|Ensembl:ENSCINP00000015837.3};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000015837.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000015837.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; L7N0T5; -.
DR STRING; 7719.ENSCINP00000015837; -.
DR Ensembl; ENSCINT00000015837.3; ENSCINP00000015837.3; ENSCING00000007677.3.
DR GeneTree; ENSGT00950000182825; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; L7N0T5; -.
DR OMA; GEVTNAC; -.
DR Proteomes; UP000008144; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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:SF239; 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:UP000008144}.
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 451 AA; 50362 MW; E00AB99C23F93B1F CRC64;
MRECISIHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVVDEIRT GTYRQLFHPE QLITGKEDAA NNYARGHYTV GKEHVDTVLD
RIRKLSDQCS GLQGFLIFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFA IYPAPQISTA
VVEPYNSVLT THTTLEHSDC AFMVDNEATY DICRRNLDVE RPTYTNLNRM IGQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLV TYAPIISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIAAIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYKY VGEGMEEGEF
SEAREDLAAL EKDYEEVGID SAEDQEEEEE Y
//
