P63270 (ACTH_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin, gamma-enteric smooth muscle

Alternative name(s):
Alpha-actin-3
Gamma-2-actin
Smooth muscle gamma-actin

Gene names

Name:	ACTG2
Synonyms:	ACTA3, ACTSG

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subunit structure	Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Oxidation of Met-45 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced By similarity.
Miscellaneous	In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
Molecular function	Muscle protein
PTM	Acetylation Oxidation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 2

2

Removed in mature form By similarity

PRO_0000000754

Chain

3 – 376

374

Actin, gamma-enteric smooth muscle

PRO_0000000755

Amino acid modifications

Modified residue

3

1

N-acetylglutamate By similarity

Modified residue

45

1

Methionine sulfoxide By similarity

Experimental info

Sequence conflict

221

1

A → P in AAC05823. Ref.2

Secondary structure

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376

Helix Strand Turn

Details...

Beta strand

9 – 13

5

Beta strand

15 – 22

8

Beta strand

29 – 33

5

Beta strand

36 – 41

6

Beta strand

43 – 45

3

Beta strand

54 – 56

3

Helix

57 – 61

5

Helix

63 – 65

3

Beta strand

66 – 69

4

Helix

80 – 92

13

Turn

93 – 95

3

Helix

99 – 101

3

Beta strand

104 – 108

5

Helix

114 – 126

13

Beta strand

131 – 137

7

Helix

138 – 145

8

Beta strand

151 – 156

6

Beta strand

161 – 167

7

Helix

173 – 175

3

Beta strand

177 – 179

3

Helix

183 – 196

14

Helix

204 – 217

14

Helix

224 – 233

10

Beta strand

239 – 242

4

Beta strand

248 – 253

6

Helix

254 – 260

7

Turn

261 – 263

3

Helix

265 – 268

4

Helix

275 – 285

11

Helix

290 – 295

6

Beta strand

298 – 303

6

Helix

304 – 306

3

Helix

310 – 319

10

Turn

334 – 337

4

Helix

339 – 349

11

Helix

352 – 355

4

Helix

360 – 364

5

Sequences

	Sequence		Length	Mass (Da)
	P63270 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 6EC08CD5EEAD445E	FASTA	376	41,877
	10 20 30 40 50 60 MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ 70 80 90 100 110 120 SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE EHPTLLTEAP LNPKANREKM 130 140 150 160 170 180 TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THNVPIYEGY ALPHAIMRLD 190 200 210 220 230 240 LAGRDLTDYL MKILTERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS 250 260 270 280 290 300 YELPDGQVIT IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL 310 320 330 340 350 360 SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK 370 PEYDEAGPSI VHRKCF

References

[1]	"Molecular cloning and expression of the chicken smooth muscle gamma-actin mRNA." Kovacs A.M., Zimmer W.E. Cell Motil. Cytoskeleton 24:67-81(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Smooth muscle.
[2]	Kovacs A.M., Zimmer W.E. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Smooth muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S63494 mRNA. Translation: AAB27386.1.
AF012348 Genomic DNA. Translation: AAC05823.1.

IPI

IPI00580021.

PIR

ATCHSM. I51208.

RefSeq

NP_990503.1. NM_205172.1.

UniGene

Gga.644.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3W3D	X-ray	1.80	A	3-376	[»]

ProteinModelPortal

P63270.

ModBase

Search...

Proteomic databases

PRIDE

P63270.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

396084.

KEGG

gga:396084.

Organism-specific databases

CTD

72.

Phylogenomic databases

HOVERGEN

HBG003771.

KO

K12315.

Family and domain databases

InterPro

IPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]

PANTHER

PTHR11937. PTHR11937. 1 hit.

Pfam

PF00022. Actin. 1 hit.
[Graphical view]

PRINTS

PR00190. ACTIN.

SMART

SM00268. ACTIN. 1 hit.
[Graphical view]

PROSITE

PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

20816142.

PMAP-CutDB

P63270.

Entry information

Entry name

ACTH_CHICK

Accession

Primary (citable) accession number: P63270
Secondary accession number(s): O73680, P12718

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program