P18601 (ACT2_ARTSX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Actin, clone 211
Organism	Artemia sp. (Brine shrimp)
Taxonomic identifier	6662 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Crustacea › Branchiopoda › Sarsostraca › Anostraca › Artemiidae › Artemia

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 transcript 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. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Oxidation of Met-45 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	There are at least 4 actin isoforms expressed during artemia development.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Oxidation
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_0000000612
	Chain	3 – 376	374	Actin, clone 211		PRO_0000000613
Amino acid modifications
	Modified residue	3	1	N-acetylaspartate By similarity
	Modified residue	45	1	Methionine sulfoxide By similarity
	Modified residue	48	1	Methionine sulfoxide By similarity

Sequences

	Sequence		Length	Mass (Da)
	P18601 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 7EF88D8ADF3BD19B	FASTA	376	41,784
	10 20 30 40 50 60 MCDDDVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ 70 80 90 100 110 120 SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPILLTEAP LNPKANREKM 130 140 150 160 170 180 TQIMFETFNS PAMYVAIQAV LSIYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD 190 200 210 220 230 240 LAGRDLIDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS 250 260 270 280 290 300 YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANTVL 310 320 330 340 350 360 SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK 370 QEYDESGPGI VHRKCF

References

[1]	"Molecular cloning and expression of four actin isoforms during Artemia development." Macias M.-T., Sastre L. Nucleic Acids Res. 18:5219-5225(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52603 mRNA. Translation: CAA36836.1.
PIR	S11451.
3D structure databases
ProteinModelPortal	P18601.
SMR	P18601. Positions 3-376.
ModBase	Search...
Proteomic databases
PRIDE	P18601.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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...

Entry information

Entry name

ACT2_ARTSX

Accession

Primary (citable) accession number: P18601

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)