TBA_TYRPU
ID TBA_TYRPU Reviewed; 450 AA.
AC Q52PV9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Tubulin alpha chain {ECO:0000255|RuleBase:RU000352, ECO:0000305};
DE AltName: Full=Alpha-tubulin {ECO:0000303|PubMed:16339071};
DE AltName: Allergen=Tyr p 33 {ECO:0000305};
OS Tyrophagus putrescentiae (Mold mite) (Acarus putrescentiae).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Acaroidea; Acaridae; Tyrophaginae;
OC Tyrophagus.
OX NCBI_TaxID=59818 {ECO:0000312|EMBL:AAX84656.1};
RN [1] {ECO:0000312|EMBL:AAX84656.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX PubMed=16339071; DOI=10.1128/cdli.12.12.1451-1454.2005;
RA Jeong K.Y., Lee H., Lee J.S., Lee J., Lee I.Y., Ree H.I., Hong C.S.,
RA Park J.W., Yong T.S.;
RT "Immunoglobulin E binding reactivity of a recombinant allergen homologous
RT to alpha-Tubulin from Tyrophagus putrescentiae.";
RL Clin. Diagn. Lab. Immunol. 12:1451-1454(2005).
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. {ECO:0000255,
CC ECO:0000255|RuleBase:RU000352}.
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. {ECO:0000255, ECO:0000255|RuleBase:RU000352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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.
CC {ECO:0000250|UniProtKB:P91910}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 29% of
CC 41 patients allergic to storage mite T.putrescentiae.
CC {ECO:0000269|PubMed:16339071}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU000352, ECO:0000305}.
CC -!- CAUTION: This protein lacks the Tyr in position 450 required for a
CC tyrosination/detyrosination cycle, the cyclic removal and re-addition
CC of a C-terminal tyrosine residue; it is replaced by a Phe.
CC {ECO:0000305}.
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DR EMBL; AY986760; AAX84656.1; -; mRNA.
DR AlphaFoldDB; Q52PV9; -.
DR SMR; Q52PV9; -.
DR Allergome; 2822; Tyr p 33.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
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; ISS:UniProtKB.
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; Allergen; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding.
FT CHAIN 1..450
FT /note="Tubulin alpha chain"
FT /id="PRO_0000447303"
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|UniProtKB:P91910"
SQ SEQUENCE 450 AA; 50037 MW; AEE18B3986F07AD3 CRC64;
MRECISVHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGTGDDSFN TFFSETGSGK
HVPRAVYVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDVVLD
RIRKLSDQCT GLQGFLIFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFA VYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA
SLRFDGALNV ELTEFQTNLV PYPRIHFPLV TYSPVISAEK AYHEQLTVAE ITNTCFEPQN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAGIKTKRS IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGLDST EAEGGDGEEF
