P63267 (ACTH_HUMAN) 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, ACTL3, ACTSG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Muscle protein
PTM	Oxidation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	muscle contraction Traceable author statement. Source: Reactome
Cellular_component	cell periphery Inferred from electronic annotation. Source: Compara cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P63267-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P63267-2)

The sequence of this isoform differs from the canonical sequence as follows:
     43-85: Missing.

Note: No experimental confirmation available.

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_0000000748
	Chain	3 – 376	374	Actin, gamma-enteric smooth muscle		PRO_0000000749
Amino acid modifications
	Modified residue	45	1	Methionine sulfoxide By similarity
Natural variations
	Alternative sequence	43 – 85	43	Missing in isoform 2.		VSP_045861
Experimental info
	Sequence conflict	130	1	V → F in CAG38753. Ref.4
	Sequence conflict	157	1	G → C in BAG65327. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: 1D423B1372E4BFCD	FASTA	333	37,083
	10 20 30 40 50 60 MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQIWHHSFYN ELRVAPEEHP 70 80 90 100 110 120 TLLTEAPLNP KANREKMTQI MFETFNVPAM YVAIQAVLSL YASGRTTGIV LDSGDGVTHN 130 140 150 160 170 180 VPIYEGYALP HAIMRLDLAG RDLTDYLMKI LTERGYSFVT TAEREIVRDI KEKLCYVALD 190 200 210 220 230 240 FENEMATAAS SSSLEKSYEL PDGQVITIGN ERFRCPETLF QPSFIGMESA GIHETTYNSI 250 260 270 280 290 300 MKCDIDIRKD LYANNVLSGG TTMYPGIADR MQKEITALAP STMKIKIIAP PERKYSVWIG 310 320 330 GSILASLSTF QQMWISKPEY DEAGPSIVHR KCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of a human smooth muscle (enteric type) gamma-actin cDNA." Miwa T., Kamada S., Kakunaga T. Nucleic Acids Res. 18:4263-4263(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Stomach.
[2]	"Structure, chromosome location, and expression of the human smooth muscle (enteric type) gamma-actin gene: evolution of six human actin genes." Miwa T., Manabe Y., Kurokawa K., Kamada S., Kanda N., Bruns G., Ueyama H., Kakunaga T. Mol. Cell. Biol. 11:3296-3306(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Uterus.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Mammary gland and Prostate.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X16940 mRNA. Translation: CAA34814.1. D00654 Genomic DNA. Translation: BAA00546.1. AK304523 mRNA. Translation: BAG65327.1. AK312955 mRNA. Translation: BAG35794.1. CR536515 mRNA. Translation: CAG38753.1. CR541794 mRNA. Translation: CAG46593.1. AC073046 Genomic DNA. Translation: AAX88909.1. CH471053 Genomic DNA. Translation: EAW99713.1. BC012617 mRNA. Translation: AAH12617.1. BC094877 mRNA. Translation: AAH94877.1.
IPI	IPI00025416. IPI00916212.
PIR	A40261.
RefSeq	NP_001186822.1. NM_001199893.1. NP_001606.1. NM_001615.3.
UniGene	Hs.516105.
3D structure databases
ProteinModelPortal	P63267.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63267. 9 interactions.
MINT	MINT-256943.
STRING	9606.ENSP00000295137.
PTM databases
PhosphoSite	P63267.
Polymorphism databases
DMDM	54036679.
2D gel databases
OGP	P12718.
Proteomic databases
PRIDE	P63267.
Protocols and materials databases
DNASU	72.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000345517; ENSP00000295137; ENSG00000163017. ENST00000409624; ENSP00000386857; ENSG00000163017. ENST00000409731; ENSP00000386929; ENSG00000163017.
GeneID	72.
KEGG	hsa:72.
UCSC	uc002sjw.3. human.
Organism-specific databases
CTD	72.
GeneCards	GC02P074119.
HGNC	HGNC:145. ACTG2.
HPA	CAB003761. HPA041271.
MIM	102545. gene.
neXtProt	NX_P63267.
PharmGKB	PA24469.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HOG000233340.
HOVERGEN	HBG003771.
InParanoid	P63267.
KO	K12315.
OMA	MEITALA.
PhylomeDB	P63267.
Enzyme and pathway databases
Reactome	REACT_17044. Muscle contraction.
Gene expression databases
ArrayExpress	P63267.
Bgee	P63267.
CleanEx	HS_ACTG2.
Genevestigator	P63267.
GermOnline	ENSG00000163017. Homo sapiens.
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
ChiTaRS	ACTG2. human.
GenomeRNAi	72.
NextBio	283.
PMAP-CutDB	P63267.
SOURCE	Search...

Entry information

Entry name

ACTH_HUMAN

Accession

Primary (citable) accession number: P63267
Secondary accession number(s): B2R7E7 , B4E315, D6W5H8, E9PG30, P12718, Q504R1, Q6FI22

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.