TBA5_CHICK
ID TBA5_CHICK Reviewed; 448 AA.
AC P09644;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Tubulin alpha-5 chain;
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 -!- DOMAIN: The MREC motif may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P68363}.
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 -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the
CC microtubule lumen. This modification has been correlated with increased
CC microtubule stability, intracellular transport and ciliary assembly.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30852.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X08061; CAA30852.1; ALT_INIT; Genomic_DNA.
DR PIR; S00470; UBCHA5.
DR AlphaFoldDB; P09644; -.
DR SMR; P09644; -.
DR STRING; 9031.ENSGALP00000037524; -.
DR PaxDb; P09644; -.
DR PRIDE; P09644; -.
DR VEuPathDB; HostDB:geneid_100857247; -.
DR eggNOG; KOG1376; Eukaryota.
DR PhylomeDB; P09644; -.
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 Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..448
FT /note="Tubulin alpha-5 chain"
FT /id="PRO_0000048151"
FT MOTIF 1..4
FT /note="MREC motif"
FT /evidence="ECO:0000250|UniProtKB:P68363"
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:P41351,
FT ECO:0000250|UniProtKB:Q71U36"
SQ SEQUENCE 448 AA; 49948 MW; 2E498A2B20D7CBA6 CRC64;
MRECISVHVG QAGVQMGNTC WELYCLEHGI QPDGQMPSDK TIGGGDDSFT TFFCETGAGK
HVPRAIFVDL EPTVIDEVRA GIYRQLFHPE QLITGKEDGA NNYARGHYTI GKEIIDQVLD
RIRKLADQCT GLQGFLCFHS FGGGTGSGFT SLLMERLSGD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNSCFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
TVVAGGDLAK VQRIVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDIAALEK DYEEVGLDSY EDEEEGEE
