ID   TBA13_NAEPR             Reviewed;         453 AA.
AC   Q25563;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Tubulin alpha-13 chain;
GN   Name=TUBA13;
OS   Naegleria pringsheimi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=234921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 30961 / NB-1;
RA   Choi Y.-J., Park H.-L., Lee J.-H.;
RT   "Cloning and sequence determination of alpha-tubulin, beta-tubulin and
RT   flagellar calmodulin.";
RL   Misainmurhag Hoiji 33:40-45(1995).
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}.
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DR   EMBL; X81049; CAA56939.1; -; mRNA.
DR   AlphaFoldDB; Q25563; -.
DR   SMR; Q25563; -.
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   Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW   Nucleotide-binding.
FT   CHAIN           1..453
FT                   /note="Tubulin alpha-13 chain"
FT                   /id="PRO_0000048197"
FT   REGION          429..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   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   453 AA;  49813 MW;  C6C12504DF7232B9 CRC64;
     MREVISIHIG QAGVQVGNAC WELYCLEHGI QPDGLMPSSK TIGVEDDAFN TFFSETGAGK
     HVPRAVFLDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLCLD
     RIRKLADNCT GLQGFLVFSS VGGGTGSGLG ALLLERLSVD YGKKSKLGFT VYPSPQVATA
     VVEPYNSVLS THALLEHTDV AVMLDNEAIY DICRRSLDIQ RPTYTNLNRL IAQVISSLTA
     SLRFDGALNV DVTEFQTNLV PYPRIHFMLC SYAPVISAEK AYHEQLSVAE ITNSAFEPAS
     MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWSPTG FKCGINYQPP
     TVVPGGDLAK VQRAVCMISN STAIAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDLAALEK DYEEVGTESQ EGDGEEGEDG GDQ