ID   TBA1_PELFA              Reviewed;         453 AA.
AC   Q40831;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Tubulin alpha-1 chain;
GN   Name=TUBA1;
OS   Pelvetia fastigiata (Brown alga) (Fucodium fastigiatum).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae; Fucales;
OC   Fucaceae; Pelvetia.
OX   NCBI_TaxID=48072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Coffman H.R., Kropf D.L.;
RT   "The brown alga, Pelvetia fastigiata, expresses two alpha-tubulin
RT   sequences.";
RL   (er) Plant Gene Register PGR97-019(1997).
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; U58641; AAB68031.1; -; mRNA.
DR   AlphaFoldDB; Q40831; -.
DR   SMR; Q40831; -.
DR   PRIDE; Q40831; -.
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..453
FT                   /note="Tubulin alpha-1 chain"
FT                   /id="PRO_0000048211"
FT   REGION          433..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..453
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   SITE            453
FT                   /note="Involved in polymerization"
SQ   SEQUENCE   453 AA;  49937 MW;  65DF46C1E2981ED4 CRC64;
     MRECISIHIG QAGIQVGNAC WELYCLEHGI QPNGQMPADN TTGGGDDAFN TFFSETGAGK
     HVPRAVYVDL EPTVCDEVRT GSYRQLYHPE QIISGKEDAA NNYARGHYTI GKEIVDIVLD
     RIRKLSDNCT GLQGFLVFHA TGGGTGSGLG SLLLERLSVD YGRKSKLSFA ITPAPQVATA
     VVEPYNSVLS THALLEHTDC TFCLDNEALY DVCRRNLDIE RPTYTNLNRL VAQVISSLTA
     SLRFDGALNV DVTEFQTNLV PYPRIHFMLT SYAPIISAEK AYHEQLSVAE ITNSVFEPAG
     MMTKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP
     TAVPGGDLAR VQRAVCMVAN TTAIAEALSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDLVALEK DYEEVGAETA DGDGEEEEFG EEY