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Tubulin alpha chain

 TBA_ENTDO               Reviewed;         451 AA.
Q06331;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
10-MAY-2017, entry version 83.
RecName: Full=Tubulin alpha chain;
Enteroctopus dofleini (North Pacific giant octopus) (Octopus
dofleini).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Cephalopoda; Coleoidea;
Neocoleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae;
Enteroctopus.
NCBI_TaxID=267067;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lens;
PubMed=8241265; DOI=10.1016/0167-4781(93)90151-3;
Tomarev S.I., Zinovieva R.D., Piatigorsky J.;
"Primary structure and lens-specific expression of genes for an
intermediate filament protein and a beta-tubulin in cephalopods.";
Biochim. Biophys. Acta 1216:245-254(1993).
-!- FUNCTION: Tubulin is the major constituent of microtubules. It
binds two moles of GTP, one at an exchangeable site on the beta
chain and one at a non-exchangeable site on the alpha chain.
-!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is
a hollow water-filled tube with an outer diameter of 25 nm and an
inner diameter of 15 nM. Alpha-beta heterodimers associate head-
to-tail to form protofilaments running lengthwise along the
microtubule wall with the beta-tubulin subunit facing the
microtubule plus end conferring a structural polarity.
Microtubules usually have 13 protofilaments but different
protofilament numbers can be found in some organisms and
specialized cells.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- TISSUE SPECIFICITY: Actively expressed in the lens but does not
seem to be lens-specific.
-!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic
removal and re-addition of a C-terminal tyrosine residue by the
enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin
tyrosine ligase (TTL), respectively. {ECO:0000250}.
-!- PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules
and affects affinity and processivity of microtubule motors. This
modification has a role in multiple cellular functions, ranging
from cell motility, cell cycle progression or cell differentiation
to intracellular trafficking and signaling (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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EMBL; L10110; AAA16610.1; -; mRNA.
PIR; S43425; S43425.
ProteinModelPortal; Q06331; -.
SMR; Q06331; -.
PRIDE; Q06331; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
Gene3D; 3.30.1330.20; -; 1.
Gene3D; 3.40.50.1440; -; 1.
InterPro; IPR002452; Alpha_tubulin.
InterPro; IPR008280; Tub_FtsZ_C.
InterPro; IPR000217; Tubulin.
InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
InterPro; IPR017975; Tubulin_CS.
InterPro; IPR003008; Tubulin_FtsZ_GTPase.
PANTHER; PTHR11588; PTHR11588; 1.
Pfam; PF00091; Tubulin; 1.
Pfam; PF03953; Tubulin_C; 1.
PRINTS; PR01162; ALPHATUBULIN.
PRINTS; PR01161; TUBULIN.
SMART; SM00864; Tubulin; 1.
SMART; SM00865; Tubulin_C; 1.
SUPFAM; SSF52490; SSF52490; 1.
SUPFAM; SSF55307; SSF55307; 1.
PROSITE; PS00227; TUBULIN; 1.
2: Evidence at transcript level;
Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
Nucleotide-binding.
CHAIN 1 451 Tubulin alpha chain.
/FTId=PRO_0000048202.
NP_BIND 142 148 GTP. {ECO:0000255}.
SITE 451 451 Involved in polymerization.
MOD_RES 40 40 N6-acetyllysine. {ECO:0000250}.
SEQUENCE 451 AA; 50194 MW; 8D98E87BD5F89094 CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPSGQMPSDK AVGGKDDSFN TFFSETGSGK
HVPRAVFVDL EPTVVDEIRT GLYRQLFHPE QLITGKEDAA NNYARGHYTI GKEHIDLVLD
RVRKLSDQCT GLQGFLIFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVATA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICKRNLDIE RPSYTNLNRL ISQVVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLV TYAPIISAEK AYHEQLAVAE VTSACFEPAN
QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAVAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGLDTF EAEEEEGGDE Y


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