TBA1A_PIG
ID TBA1A_PIG Reviewed; 451 AA.
AC P02550;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Tubulin alpha-1A chain;
DE AltName: Full=Alpha-tubulin 1;
DE AltName: Full=Tubulin alpha-1 chain;
DE Contains:
DE RecName: Full=Detyrosinated tubulin alpha-1A chain;
GN Name=TUBA1A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=7019911; DOI=10.1073/pnas.78.5.2757;
RA Ponstingl H., Krauhs E., Little M., Kempf T.;
RT "Complete amino acid sequence of alpha-tubulin from porcine brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:2757-2761(1981).
RN [2]
RP BINDING SITE.
RX PubMed=6688710; DOI=10.1016/0003-9861(83)90056-5;
RA Zabrecky J.R., Cole R.D.;
RT "Localization of the ATP binding site on alpha-tubulin.";
RL Arch. Biochem. Biophys. 225:475-481(1983).
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. Cilia and flagella glycylation is required for their
CC stability and maintenance. Flagella glycylation controls sperm
CC motility. {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). Glutamylation is also involved in cilia
CC motility (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 -!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic
CC microtubules and is required for normal mitosis and cytokinesis
CC contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.
CC -!- PTM: Nitration of Tyr-451 is irreversible and interferes with normal
CC dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase
CC (TTL), respectively. {ECO:0000250|UniProtKB:P68369,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: [Tubulin alpha-1A chain]: Tyrosination promotes microtubule
CC interaction with CAP-Gly domain-containing proteins such as CLIP1,
CC CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation
CC of dynein-dynactin motility via interaction with DCTN1, which brings
CC the dynein-dynactin complex into contact with microtubules. In neurons,
CC tyrosinated tubulins mediate the initiation of retrograde vesicle
CC transport (By similarity). {ECO:0000250|UniProtKB:P68369,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: [Detyrosinated tubulin alpha-1A chain]: Detyrosination is involved
CC in metaphase plate congression by guiding chromosomes during mitosis:
CC detyrosination promotes interaction with CENPE, promoting pole-proximal
CC transport of chromosomes toward the equator (By similarity).
CC Detyrosination increases microtubules-dependent mechanotransduction in
CC dystrophic cardiac and skeletal muscle. In cardiomyocytes,
CC detyrosinated microtubules are required to resist to contractile
CC compression during contraction: detyrosination promotes association
CC with desmin (DES) at force-generating sarcomeres, leading to buckled
CC microtubules and mechanical resistance to contraction (By similarity).
CC {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
CC -!- MISCELLANEOUS: The highly acidic C-terminal region may bind cations
CC such as calcium.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR PIR; A93874; UBPGA.
DR PDB; 1FFX; X-ray; 3.95 A; A/C=1-451.
DR PDB; 1IA0; EM; 15.00 A; A=1-451.
DR PDB; 1TUB; X-ray; 3.70 A; A=1-440.
DR PDB; 2HXF; EM; 10.00 A; A=1-451.
DR PDB; 2HXH; EM; 11.00 A; A=1-451.
DR PDB; 2P4N; EM; 9.00 A; A=1-451.
DR PDB; 3EDL; EM; 28.00 A; A=1-451.
DR PDB; 3J6E; EM; 4.70 A; A/C/E/G/I/K/M/O/Q=1-439.
DR PDB; 3J6F; EM; 4.90 A; A/C/E/G/I/K/M/O/Q=1-439.
DR PDB; 3J6G; EM; 5.50 A; A/C/E/G/I/K/M/O/Q=1-439.
DR PDB; 3J6H; EM; 8.10 A; A=2-437.
DR PDB; 3J6P; EM; 8.20 A; A=1-451.
DR PDB; 3J7I; EM; 8.90 A; A=1-451.
DR PDB; 4ABO; EM; 8.60 A; B/D/F/H=1-451.
DR PDB; 5MM4; EM; 4.50 A; A=1-439.
DR PDB; 5MM7; EM; 5.10 A; A=1-439.
DR PDB; 5XXT; EM; 5.35 A; A/C/E/G/I/K/M/O/Q=2-439.
DR PDB; 5XXV; EM; 6.46 A; A/C/E/G/I/K/M/O/Q=2-439.
DR PDB; 5XXW; EM; 6.00 A; A/C/E/G/I/K/M/O/Q=2-439.
DR PDB; 5XXX; EM; 6.43 A; A/C/E/G/I/K/M/O/Q=2-439.
DR PDB; 6KIO; EM; 3.94 A; a=2-439.
DR PDB; 6KIQ; EM; 3.62 A; a=2-439.
DR PDB; 6MLQ; EM; 4.20 A; A=1-451.
DR PDB; 6MLR; EM; 4.20 A; A=1-451.
DR PDB; 6MZE; X-ray; 3.60 A; A/C/H/J/O/Q/V/X=1-451.
DR PDB; 6MZF; X-ray; 4.40 A; A/C/H/J/O/Q/V/X=1-451.
DR PDB; 6MZG; X-ray; 3.21 A; A/C/G/I=1-451.
DR PDB; 6VPO; EM; 4.40 A; A=1-451.
DR PDB; 6VPP; EM; 4.40 A; A=1-451.
DR PDBsum; 1FFX; -.
DR PDBsum; 1IA0; -.
DR PDBsum; 1TUB; -.
DR PDBsum; 2HXF; -.
DR PDBsum; 2HXH; -.
DR PDBsum; 2P4N; -.
DR PDBsum; 3EDL; -.
DR PDBsum; 3J6E; -.
DR PDBsum; 3J6F; -.
DR PDBsum; 3J6G; -.
DR PDBsum; 3J6H; -.
DR PDBsum; 3J6P; -.
DR PDBsum; 3J7I; -.
DR PDBsum; 4ABO; -.
DR PDBsum; 5MM4; -.
DR PDBsum; 5MM7; -.
DR PDBsum; 5XXT; -.
DR PDBsum; 5XXV; -.
DR PDBsum; 5XXW; -.
DR PDBsum; 5XXX; -.
DR PDBsum; 6KIO; -.
DR PDBsum; 6KIQ; -.
DR PDBsum; 6MLQ; -.
DR PDBsum; 6MLR; -.
DR PDBsum; 6MZE; -.
DR PDBsum; 6MZF; -.
DR PDBsum; 6MZG; -.
DR PDBsum; 6VPO; -.
DR PDBsum; 6VPP; -.
DR AlphaFoldDB; P02550; -.
DR SMR; P02550; -.
DR CORUM; P02550; -.
DR IntAct; P02550; 3.
DR MINT; P02550; -.
DR BindingDB; P02550; -.
DR ChEMBL; CHEMBL3658; -.
DR DrugCentral; P02550; -.
DR PeptideAtlas; P02550; -.
DR PRIDE; P02550; -.
DR ABCD; P02550; 1 sequenced antibody.
DR InParanoid; P02550; -.
DR EvolutionaryTrace; P02550; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation;
KW Microtubule; Nitration; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..451
FT /note="Tubulin alpha-1A chain"
FT /id="PRO_0000048131"
FT CHAIN 1..450
FT /note="Detyrosinated tubulin alpha-1A chain"
FT /evidence="ECO:0000250|UniProtKB:Q71U36"
FT /id="PRO_0000437381"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 451
FT /note="Involved in polymerization"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q71U36"
FT MOD_RES 282
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P68373"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68373"
FT MOD_RES 443
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q71U36"
FT MOD_RES 445
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P68369"
FT MOD_RES 451
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q71U36"
FT VARIANT 265
FT /note="A -> G"
FT VARIANT 265
FT /note="A -> I"
FT VARIANT 266
FT /note="H -> I"
FT VARIANT 271..273
FT /note="TYA -> RFB"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 10..28
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:6MZG"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 130..143
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:6MZG"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:6MZG"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 312..322
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:6MZG"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 385..399
FT /evidence="ECO:0007829|PDB:6MZG"
FT TURN 400..404
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:6MZG"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:6MZG"
FT HELIX 416..436
FT /evidence="ECO:0007829|PDB:6MZG"
SQ SEQUENCE 451 AA; 50068 MW; 48D7112D182B33CA CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
RIRKLADQCT GLQGFSVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRAHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYEPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
