ID   TBAD_PHYPO              Reviewed;         450 AA.
AC   P50258;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Tubulin alpha-1A chain;
GN   Name=ALTA;
OS   Physarum polycephalum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC   Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX   NCBI_TaxID=5791;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=LU352;
RX   PubMed=8450305; DOI=10.1099/00221287-139-1-137;
RA   Cunningham D.B., Buchschacher G.L. Jr., Burland T.G., Dove W.F.,
RA   Kessler D., Paul E.C.A.;
RT   "Cloning and characterization of the altA alpha-tubulin gene of Physarum.";
RL   J. Gen. Microbiol. 139:137-151(1993).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3586014; DOI=10.1016/0022-2836(86)90037-9;
RA   Singhofer-Wowra M., Little M., Clayton L., Dawson P., Gull K.;
RT   "Amino acid sequence data of alpha-tubulin from myxamoebae of Physarum
RT   polycephalum.";
RL   J. Mol. Biol. 192:919-923(1986).
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, spindle. Nucleus.
CC       Note=Mitosis in the slime mold Plasmodium differs from the process in
CC       many eukaryotes. The tubulin chains must be transported to the nuclei
CC       for intranuclear assembly of the spindle.
CC   -!- DEVELOPMENTAL STAGE: Expressed in flagellate > amoeba > plasmodium.
CC   -!- PTM: May be acetylated, giving rise to the alpha3-tubulin isoform found
CC       specifically in amoeba and flagellates.
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   -!- 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}.
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DR   EMBL; M98863; AAA29972.1; -; mRNA.
DR   PIR; A25601; A25601.
DR   PIR; A47707; A47707.
DR   AlphaFoldDB; P50258; -.
DR   SMR; P50258; -.
DR   PRIDE; P50258; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Microtubule; Nucleotide-binding; Nucleus.
FT   CHAIN           1..450
FT                   /note="Tubulin alpha-1A chain"
FT                   /id="PRO_0000048213"
FT   REGION          430..450
FT                   /note="Disordered"
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   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  49853 MW;  AD7A87E06B53EA7B CRC64;
     MREVISIHIG QAGTQVGNAC WELYCLEHGI QPDGQMPSDK SVGYGDDAFN TFFSETGAGK
     HVPRAVFLDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLCLD
     RVRKLADQCT GLQGFLVFHS VGGGTGSGFG SLLLERLSVD YGKKSKLDFC VYPSPQVSTA
     VVEPYNSVLS THSLLEHTDV AFMLDNEAIY DICKRALDID RPTYTNLNRL VAQVISSLTT
     SLRFDGALNV DITEFQTNLV PYPRIHFMLC SYAPVISAEK AYHEQLTVAE ITNSVFEPAN
     MMAKCDPRHG KYMACCLMYR GDVVPKDVNA SVAVIKTKRT IQFVDWCPTG FKCGINYQPP
     TVVPGGDLAK VQRAVCMLSN TTAIAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGAESS EAGGDEEGEY