ID   TBA2_ANEPH              Reviewed;         364 AA.
AC   P33624;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Tubulin alpha-2 chain;
DE   Flags: Fragment;
GN   Name=TUBA2;
OS   Anemia phyllitidis (Fern) (Osmunda phyllitidis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Schizaeales; Anemiaceae; Anemia.
OX   NCBI_TaxID=12940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Moepps B., Maucher H.P., Bogenberger J.M., Schraudolf H.;
RT   "Characterization of the alpha and beta tubulin gene families from Anemia
RT   phyllitidis L.Sw.";
RL   Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
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; X69184; CAA48928.1; -; mRNA.
DR   PIR; S32667; S32667.
DR   AlphaFoldDB; P33624; -.
DR   SMR; P33624; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           <1..364
FT                   /note="Tubulin alpha-2 chain"
FT                   /id="PRO_0000048134"
FT   BINDING         57..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            364
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   364 AA;  40177 MW;  A001456B2D06AE83 CRC64;
     LFHPEQLISG KEDAANNFAR GHYTVGKEIV DLCLDRVRKL SDNCTGLQGF LVFNAVGGGT
     GSGLGSLLLE RLSVDYGKKS KLGFTIYPSP QVSTAVVEPY NSVLSTHSLL EHTDVAVLLD
     NEAIYDICRR SLLDIERPTY TNLNRLVSQI ISSLTTSLRF DGALNVDVTE FQTNLVPYPR
     IHFMLSSYAP VISAAKAYHE QLSVPEITNA VFEPSSMMAK CDPRHGKYMA CCLMYRGDVV
     PKDVNAAVAT IKTKRTVQFV DWCPTGFKCG INYQPPSVVP GGDLAKVQRA VCMISNNTAV
     AEVFSRIDHK FDLMYAKLAF VHWYVGEGME EGEFSEARED LAALEKDYEE VAAEGVDEPE
     GDDY