ID   TBA_OCTVU               Reviewed;         240 AA.
AC   P24635;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Tubulin alpha chain;
DE   Flags: Fragment;
OS   Octopus vulgaris (Common octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=6645;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens;
RA   Zinov'Eva R.D., Aleinikova K.S., Tomarev S.I.;
RT   "Isolation and structural characterization of cDNAs coding for alpha-
RT   tubulin of the octopus eye lens.";
RL   Dokl. Akad. Nauk SSSR 302:462-467(1988).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC       two moles of GTP, one at an exchangeable site on the beta chain and one
CC       at a non-exchangeable site on the alpha chain.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC       and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC       tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL),
CC       respectively. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X15845; CAA33844.1; -; mRNA.
DR   PIR; A61544; A61544.
DR   AlphaFoldDB; P24635; -.
DR   SMR; P24635; -.
DR   PRIDE; P24635; -.
DR   Proteomes; UP000515154; Genome assembly.
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-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   Gene3D; 1.10.287.600; -; 1.
DR   Gene3D; 3.30.1330.20; -; 1.
DR   Gene3D; 3.40.50.1440; -; 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   PANTHER; PTHR11588; PTHR11588; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           <1..240
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048203"
FT   SITE            240
FT                   /note="Involved in polymerization"
FT   NON_TER         1
SQ   SEQUENCE   240 AA;  26962 MW;  13BB3A1F740F2416 CRC64;
     ICKRNLDIER PSYTNLNRLI SQVVSSITAS LRFDGALNVD LTEFQTNLVP YPRIHFPLVT
     YAPIISAEKA YHEQLAVAEV TSACFEPANQ MVKCDPRHGK YMACCMLYRG DVVPKDVNAA
     IATIKTKRSI QFVDWCPTGF KVGINYQPPT VVLGGDLAKV QRAVCMLSNT TAVAEAWARL
     DHKFDLMYAK RAFVHWYVGE GMEEGEFSEA REDLAALEKD YEEVGLDTFE AEEEEGGDEY