ID   TBA2_STYLE              Reviewed;         449 AA.
AC   P09243;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Tubulin alpha-2 chain;
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Dorum;
RX   PubMed=2841032; DOI=10.1007/bf00365664;
RA   Helftenbein E., Mueller E.;
RT   "Both alpha-tubulin genes are transcriptionally active in Stylonychia
RT   lemnae.";
RL   Curr. Genet. 13:425-432(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: Acetylation of alpha chains at Lys-40 stabilizes microtubules and
CC       affects affinity and processivity of microtubule motors. This
CC       modification has a role in multiple cellular functions, ranging from
CC       cell motility, cell cycle progression or cell differentiation to
CC       intracellular trafficking and signaling (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X12365; CAA30926.1; -; Genomic_DNA.
DR   PIR; S01053; S01053.
DR   AlphaFoldDB; P09243; -.
DR   SMR; P09243; -.
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   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; PTHR11588; 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; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding.
FT   CHAIN           1..449
FT                   /note="Tubulin alpha-2 chain"
FT                   /id="PRO_0000048229"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  49358 MW;  E48F2A1B513464F2 CRC64;
     MREVISIHVG QAGIQVGNAC WELFCLEHGI QPDGQMPSNK TIGGGDDAFN TFFSETGTGK
     HVPRCVFLDL GPTVIDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
     GIRKLADQCT GLQGFLVFNS VGGGTGSGLG SLLLERLSVD YGKKSKLGFT IYPSPQVSTA
     VVEPYNSVLS THSLLEHTDV AVMLDNEAVY DICRRNLDIE RPTYTNLNRL IAQVISSLTA
     SLRFDGALNV DVTEFQTNLV PYPRIHFMLS SAPVISAEKA YHEQLSVAEI TNSAFEPASM
     MAKCDPRHGK YMACCLMYRG DVVPKDVNAA VATIKTKRTI QFVDWCPTGF KCGINYQPPT
     VVPSGDLAKV MRAVCMISNS TAIAEVFSRI DHKFDLMYAK RAFVHWYVGE GMEEGEFSEA
     REDLAALEKD YEEVGIETAE GEGEEEGME