ID   TBA3_CHICK              Reviewed;         322 AA.
AC   P09642;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Tubulin alpha-3 chain;
DE   Flags: Fragment;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3267229; DOI=10.1002/j.1460-2075.1988.tb02898.x;
RA   Pratt L.F., Cleveland D.W.;
RT   "A survey of the alpha-tubulin gene family in chicken: unexpected sequence
RT   heterogeneity in the polypeptides encoded by five expressed genes.";
RL   EMBO J. 7:931-940(1988).
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: Some glutamate residues at the C-terminus are polyglycylated,
CC       resulting in polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into axonemes
CC       (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC       cells, centrioles, axonemes, and the mitotic spindle. Both
CC       modifications can coexist on the same protein on adjacent residues, and
CC       lowering polyglycylation levels increases polyglutamylation, and
CC       reciprocally. The precise function of polyglycylation is still unclear.
CC       {ECO:0000250|UniProtKB:P68369}.
CC   -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC       resulting in polyglutamate chains on the gamma-carboxyl group (By
CC       similarity). Polyglutamylation plays a key role in microtubule severing
CC       by spastin (SPAST). SPAST preferentially recognizes and acts on
CC       microtubules decorated with short polyglutamate tails: severing
CC       activity by SPAST increases as the number of glutamates per tubulin
CC       rises from one to eight, but decreases beyond this glutamylation
CC       threshold (By similarity). {ECO:0000250|UniProtKB:P68369,
CC       ECO:0000250|UniProtKB:Q71U36}.
CC   -!- MISCELLANEOUS: This tubulin does not have a C-terminal tyrosine.
CC   -!- MISCELLANEOUS: There are at least seven alpha tubulin genes (alpha-1 to
CC       alpha-6, and alpha-8), and a pseudogene (alpha-7) in chicken.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; X07442; CAA30324.1; -; Genomic_DNA.
DR   PIR; S00468; UBCHA3.
DR   AlphaFoldDB; P09642; -.
DR   SMR; P09642; -.
DR   PaxDb; P09642; -.
DR   VEuPathDB; HostDB:geneid_416694; -.
DR   PhylomeDB; P09642; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           <1..322
FT                   /note="Tubulin alpha-3 chain"
FT                   /id="PRO_0000048149"
FT   BINDING         17..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   322 AA;  36088 MW;  BB39B41C9E916204 CRC64;
     ADQCSGLQGF LVFHSFGGGT GSGFTSLLME RLSVEYSKKS KLEFSVYPDR QVSTAVVEPY
     NSILTTHTTL EHSDCSFMVD NEAIYDICNR NLDIERPTYT NLNRLIGQIV SSVTASLRFN
     GALNVDLIEF QTNLVPYPRI HFPLTTYARI ISAEKAYHEQ LSVPEITNAC FEFSNQMVKC
     DPRRGKYMAC CLLYRGDVVP KDVNAAIAAI KTRRSIQFVD WCPTGFKVGI NYQPPTVVPG
     GDLAKVQRAV CMLSNTTAIA EAWARLDHKF DLMYAKRAFV HWYVGEGMEE GEFSEAREDL
     AALEKDYEEV GRNSADGGEF EE