TBAN_PHYPO
ID TBAN_PHYPO Reviewed; 449 AA.
AC P04105;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Tubulin alpha-1B chain;
DE AltName: Full=Tubulin alpha-N chain;
GN Name=ALTBN; Synonyms=ALTB1;
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].
RX PubMed=3586027; DOI=10.1016/0022-2836(87)90257-9;
RA Monteiro M.J., Cox R.A.;
RT "Primary structure of an alpha-tubulin gene of Physarum polycephalum.";
RL J. Mol. Biol. 193:427-438(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-423.
RX PubMed=4020874; DOI=10.1016/0022-2836(85)90176-7;
RA Krammer G., Singhofer-Wowra M., Seedorf K., Little M., Schedl T.;
RT "A plasmodial alpha-tubulin cDNA from Physarum polycephalum. Nucleotide
RT sequence and comparative analysis.";
RL J. Mol. Biol. 183:633-638(1985).
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 1-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 -!- MISCELLANEOUS: The source of this protein was the multinucleated
CC Plasmodium of the slime mold. At least two alpha tubulin genes are
CC expressed in the plasmodium.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; X05039; CAA28712.1; -; Genomic_DNA.
DR EMBL; X05467; CAA28712.1; JOINED; Genomic_DNA.
DR EMBL; X05468; CAA28712.1; JOINED; Genomic_DNA.
DR EMBL; X05469; CAA28712.1; JOINED; Genomic_DNA.
DR EMBL; X02625; CAA26477.1; -; mRNA.
DR PIR; A02971; UBFYA.
DR PIR; S02130; S02130.
DR AlphaFoldDB; P04105; -.
DR SMR; P04105; -.
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-1B chain"
FT /id="PRO_0000048215"
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"
FT CONFLICT 188
FT /note="V -> M (in Ref. 2; CAA26477)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="A -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="E -> D (in Ref. 2; CAA26477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49587 MW; CDDDD2C5275C2CFA CRC64;
MREIISIHIG QAGAQVGNAC WELYCLEHGI NPDGQMPSDK SVGGGDDAFN TFFSETSSGK
HVPRAIYLDL EPTVIDEIRT GTYRQLFHPE QLITGKEDAA NNYARGHYTV GKEIVDLCLD
RVRKLADQCS GLQGFLVFHS VGGGTGSGFG SLLLERLSVD YGKKSKLDFC VYPSPQVSTA
VVEPYNSVLS THGLLEHTDV AFMLDNEAIY DLCKKSLDID RPSYANLNRL VAQVISSLTT
SLRFDGALNV DINEFQTNLV PYPRIHFMLA SYAPVISAEK AFHEQLSVAE LTNTVFEPSS
MMAKCDPRHG KYMACCLMYR GDVVPKDVTA AVAVIKTKRT IQFVDWCPTG FKCGINYQAP
SVVPGGDLAK VQRALCMISN TTAIAEVFSR IDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGAETV GDDEAEEEM
