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UniProtKB/Swiss-Prot entry P63267


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACTH_HUMAN
Primary accession number P63267
Secondary accession numbers B2R7E7 P12718 Q504R1 Q6FI22
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 51)
Name and origin of the protein
Protein name Actin, gamma-enteric smooth muscle
Synonyms Smooth muscle gamma-actin
Gamma-2-actin
Alpha-actin-3
Gene name
Name: ACTG2
Synonyms: ACTA3, ACTL3, ACTSG
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Stomach;
DOI=10.1093/nar/18.14.4263; PubMed=2377475 [NCBI, ExPASy, EBI, Israel, Japan]
Miwa T., Kamada S., Kakunaga T.;
"The nucleotide sequence of a human smooth muscle (enteric type) gamma-actin cDNA.";
Nucleic Acids Res. 18:4263-4263(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1710027 [NCBI, ExPASy, EBI, Israel, Japan]
Miwa T., Manabe Y., Kurokawa K., Kamada S., Kanda N., Bruns G., Ueyama H., Kakunaga T.;
"Structure, chromosome location, and expression of the human smooth muscle (enteric type) gamma-actin gene: evolution of six human actin genes.";
Mol. Cell. Biol. 11:3296-3306(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland, and Prostate;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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: 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.
  • 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.
  • SIMILARITY: Belongs to the actin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X16940; CAA34814.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D00654; BAA00546.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312955; BAG35794.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536515; CAG38753.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541794; CAG46593.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC073046; AAX88909.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012617; AAH12617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC094877; AAH94877.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00025416; -.
PIR A40261; A40261.
RefSeq NP_001606.1; -.
UniGene Hs.516105
3D structure databases
HSSP P02568; 1IJJ. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR P63267; 5-372.
ModBase P63267.
PTM databases
PhosphoSite P63267; -.
2D gel databases
HSC-2DPAGE P63267; -.
OGP P12718; -.
Organism-specific databases
GeneCards GC02P074031; -.
H-InvDB HIX0002173; -.
HGNC HGNC:145; ACTG2.
GenAtlas ACTG2.
HPA CAB003761; -.
MIM 102545; gene. [NCBI / EBI]
PharmGKB PA24469; -.
Gene expression databases
ArrayExpress P63267; -.
Bgee P63267; -.
CleanEx HS_ACTG2; -.
GermOnline ENSG00000163017; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005856; Cellular component: cytoskeleton (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004000; Actin-like.
IPR004001; Actin_CS.
Graphical view of domain structure.
PANTHER PTHR11937; Actin_like; 1.
Pfam PF00022; Actin; 1.
Pfam graphical view of domain structure.
PRINTS PR00190; ACTIN.
SMART SM00268; ACTIN; 1.
SMART graphical view of domain structure.
PROSITE PS00406; ACTINS_1; 1.
PS00432; ACTINS_2; 1.
PS01132; ACTINS_ACT_LIKE; 1.
Proteomic databases
PRIDE P63267; -.
Genome annotation databases
Ensembl ENSG00000163017; Homo sapiens. [Contig view]
GeneID 72; -.
KEGG hsa:72; -.
Phylogenomic databases
HOGENOM P63267; -.
HOVERGEN P63267; -.
OMA P63267; MEITALA.
Other
NextBio 283; -.
PMAP-CutDB P63267; -.
SOURCE ACTG2; Homo sapiens.
ProtoNet P63267.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Muscle protein; Nucleotide-binding.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
PROPEP   1     2  2     Removed in mature form (By similarity). PRO_0000000748
CHAIN   3   376  374     Actin, gamma-enteric smooth muscle. PRO_0000000749
MOD_RES   3     3        N-acetylglutamate (By similarity). 
CONFLICT   130   130        V -> F (in Ref. 4; CAG38753). 
Sequence information
Length: 376 AA [This is the length of the unprocessed precursor] Molecular weight: 41877 Da [This is the MW of the unprocessed precursor] CRC64: 6EC08CD5EEAD445E [This is a checksum on the sequence]
        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 

P63267 in FASTA format

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