Reviewed, UniProtKB/Swiss-Prot P02550 (TBA1A_PIG)

Names and origin

Protein names

Recommended name:
    Tubulin alpha-1A chain
Alternative name(s):
    Tubulin alpha-1 chain
    Alpha-tubulin 1

Gene names

Name:

TUBA1A

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.
Subunit structure	Dimer of alpha and beta chains.
Post-translational modification	Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules By similarity.
Miscellaneous	The highly acidic C-terminal region may bind cations such as calcium.
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Microtubule
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 451

451

Tubulin alpha-1A chain

PRO_0000048131

Regions

Nucleotide binding

142 – 148

7

GTP Potential

Sites

Site

451

1

Involved in polymerization

Amino acid modifications

Modified residue

6

1

Phosphoserine By similarity

Modified residue

48

1

Phosphoserine By similarity

Modified residue

272

1

Phosphotyrosine By similarity

Modified residue

439

1

Phosphoserine By similarity

Natural variations

Natural variant

265

1

A → G

Natural variant

265

1

A → I

Natural variant

266

1

H → I

Natural variant

271 – 273

3

TYA → RFB

Secondary structure

1

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451

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

11 – 18

8

Turn

19 – 25

7

Beta strand

26 – 30

5

Beta strand

39 – 41

3

Beta strand

66 – 68

3

Helix

74 – 76

3

Beta strand

77 – 81

5

Helix

104 – 107

4

Turn

109 – 117

9

Helix

118 – 123

6

Turn

124 – 127

4

Beta strand

128 – 130

3

Beta strand

135 – 138

4

Turn

144 – 148

5

Helix

150 – 160

11

Beta strand

180 – 182

3

Helix

183 – 190

8

Turn

206 – 208

3

Helix

209 – 212

4

Turn

213 – 217

5

Helix

224 – 236

13

Turn

237 – 239

3

Helix

240 – 242

3

Beta strand

246 – 248

3

Helix

253 – 255

3

Turn

257 – 259

3

Beta strand

262 – 264

3

Beta strand

269 – 272

4

Beta strand

278 – 280

3

Turn

288 – 290

3

Helix

294 – 296

3

Helix

298 – 300

3

Beta strand

301 – 303

3

Helix

307 – 309

3

Beta strand

318 – 322

5

Helix

325 – 336

12

Beta strand

345 – 347

3

Turn

364 – 367

4

Beta strand

372 – 379

8

Helix

384 – 387

4

Helix

390 – 392

3

Helix

393 – 396

4

Helix

403 – 406

4

Turn

407 – 411

5

Beta strand

415 – 419

5

Turn

420 – 422

3

Turn

424 – 426

3

Helix

427 – 431

5

Turn

432 – 436

5

Sequences

	Sequence		Length	Mass (Da)
	P02550-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 48D7112D182B33CA	FASTA	451	50,068
	10 20 30 40 50 60 MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 70 80 90 100 110 120 HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD 130 140 150 160 170 180 RIRKLADQCT GLQGFSVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA 190 200 210 220 230 240 VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA 250 260 270 280 290 300 SLRFDGALNV DLTEFQTNLV PYPRAHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 310 320 330 340 350 360 QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYEPP 370 380 390 400 410 420 TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 430 440 450 AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y

References

[1]	"Complete amino acid sequence of alpha-tubulin from porcine brain." Ponstingl H., Krauhs E., Little M., Kempf T. Proc. Natl. Acad. Sci. U.S.A. 78:2757-2761(1981) [PubMed: 7019911] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Brain.
[2]	"Localization of the ATP binding site on alpha-tubulin." Zabrecky J.R., Cole R.D. Arch. Biochem. Biophys. 225:475-481(1983) [PubMed: 6688710] [Abstract] Cited for: BINDING SITE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

UBPGA. A93874.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFX	X-ray	3.95	A/C	1-451	[»]
1IA0	electron microscopy	15.00	A	1-451	[»]
1TUB	X-ray	3.70	A	1-440	[»]
2HXF	electron microscopy	10.00	A	1-451	[»]
2HXH	electron microscopy	11.00	A	1-451	[»]
2P4N	electron microscopy	9.00	A	1-451	[»]
2WBE	electron microscopy	9.40	A	1-451	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000000201; ENSSSCP00000000199; ENSSSCG00000000190; Sus scrofa. [Genome view]
ENSSSCT00000000202; ENSSSCP00000000200; ENSSSCG00000000190; Sus scrofa. [Genome view]
ENSSSCT00000000206; ENSSSCP00000000204; ENSSSCG00000000193; Sus scrofa. [Genome view]

Phylogenomic databases

HOVERGEN

P02550.

Family and domain databases

InterPro

IPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
IPR019746. Tubulin_FtsZ_N.
[Graphical view]

Gene3D

G3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit.
G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit.

PANTHER

PTHR11588:SF10. Alpha_tubulin. 1 hit.
PTHR11588. Tubulin. 1 hit.

Pfam

PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]

PRINTS

PR01162. ALPHATUBULIN.
PR01161. TUBULIN.

SMART

SM00865. Tubulin_C. 1 hit.
[Graphical view]

PROSITE

PS00227. TUBULIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TBA1A_PIG

Accession

Primary (citable) accession number: P02550

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 24, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)