ID TBA2_CHICK Reviewed; 446 AA.
AC P08070;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Tubulin alpha-2 chain;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68363};
DE AltName: Full=Testis-specific;
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 [MRNA].
RX PubMed=3561402; DOI=10.1128/mcb.7.1.552-555.1987;
RA Pratt L.F., Okamura S., Cleveland D.W.;
RT "A divergent testis-specific alpha-tubulin isotype that does not contain a
RT coded C-terminal tyrosine.";
RL Mol. Cell. Biol. 7:552-555(1987).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC consisting of laterally associated linear protofilaments composed of
CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC GTPase activity of alpha-tubulin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P68363};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P68363};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P68363};
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 -!- TISSUE SPECIFICITY: Testis specific.
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 -!- 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; M16030; AAA49122.1; -; mRNA.
DR PIR; A26724; A26724.
DR RefSeq; NP_990775.1; NM_205444.1.
DR AlphaFoldDB; P08070; -.
DR SMR; P08070; -.
DR BioGRID; 676675; 1.
DR STRING; 9031.ENSGALP00000036691; -.
DR PaxDb; 9031-ENSGALP00000036691; -.
DR GeneID; 396426; -.
DR KEGG; gga:396426; -.
DR CTD; 396426; -.
DR VEuPathDB; HostDB:geneid_396426; -.
DR eggNOG; KOG1376; Eukaryota.
DR InParanoid; P08070; -.
DR PhylomeDB; P08070; -.
DR PRO; PR:P08070; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR CDD; cd02186; alpha_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR PANTHER; PTHR11588:SF140; TUBULIN ALPHA-8 CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN 1..446
FT /note="Tubulin alpha-2 chain"
FT /id="PRO_0000048148"
FT MOTIF 1..4
FT /note="MREC motif"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT ACT_SITE 251
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 11
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 68
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
FT BINDING 225
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P68363"
SQ SEQUENCE 446 AA; 49798 MW; 2FD24D095B362549 CRC64;
MRECISVHIG QAGVQIGNAC WELFCLEHSI QPDGTFSDPP SSDDSFATFF RETSMSKYVP
RAIMVDLEPT VVDEVRTGTY RHLFHPEQLI TGKEDAANNY ARGHYTVGKD KVDMVSDRIR
KLADSCSGLQ GFLIFHSFGG GTGSGFTSLL MERLSVEYGK KSKLEFAIYP APQASSAVVE
PYNSVLTTHT TLEHSDCVFM VDNEAIYDIC HRNLDIERPT YTNLNRLISQ IVSSITASLR
FDGALNVDLT EFQTNLVPFP RIHFPLVTYA PIISSDRAYH EQLSVAEITS SCFEPNNQMV
KCDPQQGKYM ACCMLYRGDV VPKDVNVAIA AIKTNRSLQF VDWCPTGFKV GINYQPPIPT
PGGDLAQVQR AVCMLSNTTA IAEAWARLDH KFDLMYAKRA FVHWYVSEGM EEGEFAEARE
DLAALEKDYD EVATDLFEDE NEAGDS
//
