ID   TBAE_PHYPO              Reviewed;         449 AA.
AC   P11480;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tubulin alpha-2B chain;
DE   AltName: Full=Tubulin alpha-E chain;
GN   Name=ALTBE; Synonyms=ALTB2;
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 [GENOMIC DNA].
RC   STRAIN=M3CVIII;
RX   PubMed=2659344; DOI=10.1111/j.1432-1033.1989.tb14764.x;
RA   Walden P.D., Monteiro M.J., Gull K., Cox R.A.;
RT   "Structure and expression of an alpha-tubulin gene of Physarum
RT   polycephalum.";
RL   Eur. J. Biochem. 181:583-592(1989).
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: Plasmodium specific alpha 2-tubulin.
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; X14213; CAA32430.1; -; Genomic_DNA.
DR   PIR; S04474; S04474.
DR   AlphaFoldDB; P11480; -.
DR   SMR; P11480; -.
DR   PRIDE; P11480; -.
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; IPR013838; Beta-tubulin_BS.
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; Nucleus.
FT   CHAIN           1..449
FT                   /note="Tubulin alpha-2B chain"
FT                   /id="PRO_0000048214"
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;  49639 MW;  0B6C9148EB00A60F CRC64;
     MREILSIHIG QAGAQVGNAC WELYCLEHGI KPDGQMPSDK SVGGGDDAFN TFFSETSSGK
     HVPRAIFLDL EPTVIDEIRT GTYRQLFHPE QLITGKEDAA NNYARGHYTV GKELVDLCLD
     RVRKLADQCS GLQGFLVFHS VGGGTGSGFG SLLLERLSVD YGKKSKLDFC VYPSPQVSTA
     VVEPYNSVLS THGLLEHTDV AFMLDNEAIY DLCKRSLDIE RPSYANLNRL VAQVISSLTT
     SLRFDGALNV DITEFQTNLV PYPRIHFMLA SYAPVISAEK AFHEQLSVAE LTNTVFDPSS
     MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVAVIKTKRT IQFVDWCPTG FKCGINYQPP
     SVVPGGDLAK VQRALCMISN TTAIAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEVEFSE
     AREDLAALEK DYEEVGAETA EDDGADEEM