ID   TBA_LYTPI               Reviewed;         161 AA.
AC   P02553;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Tubulin alpha chain;
DE   Flags: Fragment;
OS   Lytechinus pictus (Painted sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Temnopleuroida; Toxopneustidae; Lytechinus.
OX   NCBI_TaxID=7653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=6317873; DOI=10.1007/bf02102315;
RA   Alexandraki D., Ruderman J.V.;
RT   "Evolution of alpha q- and beta-tubulin genes as inferred by the nucleotide
RT   sequences of sea urchin cDNA clones.";
RL   J. Mol. Evol. 19:397-410(1983).
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   PIR; A02969; UBURAL.
DR   AlphaFoldDB; P02553; -.
DR   SMR; P02553; -.
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   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; 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; SSF55307; SSF55307; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           <1..161
FT                   /note="Tubulin alpha chain"
FT                   /id="PRO_0000048187"
FT   SITE            161
FT                   /note="Involved in polymerization"
FT   NON_TER         1
SQ   SEQUENCE   161 AA;  18024 MW;  771332C6FF61195E CRC64;
     ITNACFEPAN QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
     FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG
     EGMEEGEFSE AREDLAALEK DYEEVGVDSV EGEAEEEGEE Y