ID ACTH_HUMAN Reviewed; 376 AA. AC P63267; B2R7E7; P12718; Q504R1; Q6FI22; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 03-NOV-2009, entry version 57. DE RecName: Full=Actin, gamma-enteric smooth muscle; DE AltName: Full=Smooth muscle gamma-actin; DE AltName: Full=Gamma-2-actin; DE AltName: Full=Alpha-actin-3; GN Name=ACTG2; Synonyms=ACTA3, ACTL3, ACTSG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Stomach; RX MEDLINE=90332437; PubMed=2377475; DOI=10.1093/nar/18.14.4263; RA Miwa T., Kamada S., Kakunaga T.; RT "The nucleotide sequence of a human smooth muscle (enteric type) RT gamma-actin cDNA."; RL Nucleic Acids Res. 18:4263-4263(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91246198; PubMed=1710027; RA Miwa T., Manabe Y., Kurokawa K., Kamada S., Kanda N., Bruns G., RA Ueyama H., Kakunaga T.; RT "Structure, chromosome location, and expression of the human smooth RT muscle (enteric type) gamma-actin gene: evolution of six human actin RT genes."; RL Mol. Cell. Biol. 11:3296-3306(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland, and Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell motility. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X16940; CAA34814.1; -; mRNA. DR EMBL; D00654; BAA00546.1; -; Genomic_DNA. DR EMBL; AK312955; BAG35794.1; -; mRNA. DR EMBL; CR536515; CAG38753.1; -; mRNA. DR EMBL; CR541794; CAG46593.1; -; mRNA. DR EMBL; AC073046; AAX88909.1; -; Genomic_DNA. DR EMBL; BC012617; AAH12617.1; -; mRNA. DR EMBL; BC094877; AAH94877.1; -; mRNA. DR IPI; IPI00025416; -. DR PIR; A40261; A40261. DR RefSeq; NP_001606.1; -. DR UniGene; Hs.516105; -. DR HSSP; P02568; 1IJJ. DR SMR; P63267; 5-372. DR STRING; P63267; -. DR PhosphoSite; P63267; -. DR HSC-2DPAGE; P63267; -. DR OGP; P12718; -. DR PRIDE; P63267; -. DR Ensembl; ENST00000345517; ENSP00000295137; ENSG00000163017; Homo sapiens. DR Ensembl; ENST00000409624; ENSP00000386857; ENSG00000163017; Homo sapiens. DR Ensembl; ENST00000409731; ENSP00000386929; ENSG00000163017; Homo sapiens. DR Ensembl; ENST00000409918; ENSP00000387182; ENSG00000163017; Homo sapiens. DR Ensembl; ENST00000429756; ENSP00000392894; ENSG00000163017; Homo sapiens. DR Ensembl; ENST00000438902; ENSP00000410706; ENSG00000163017; Homo sapiens. DR Ensembl; ENST00000442912; ENSP00000410020; ENSG00000163017; Homo sapiens. DR GeneID; 72; -. DR KEGG; hsa:72; -. DR UCSC; uc002sjw.1; human. DR CTD; 72; -. DR GeneCards; GC02P074031; -. DR H-InvDB; HIX0002173; -. DR HGNC; HGNC:145; ACTG2. DR HPA; CAB003761; -. DR MIM; 102545; gene. DR PharmGKB; PA24469; -. DR HOGENOM; P63267; -. DR HOVERGEN; P63267; -. DR OMA; MEITALA; -. DR NextBio; 283; -. DR PMAP-CutDB; P63267; -. DR ArrayExpress; P63267; -. DR Bgee; P63267; -. DR CleanEx; HS_ACTG2; -. DR Genevestigator; P63267; -. DR GermOnline; ENSG00000163017; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR InterPro; IPR004000; Actin-like. DR InterPro; IPR004001; Actin_CS. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. PE 1: Evidence at protein level; KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; KW Muscle protein; Nucleotide-binding. FT PROPEP 1 2 Removed in mature form (By similarity). FT /FTId=PRO_0000000748. FT CHAIN 3 376 Actin, gamma-enteric smooth muscle. FT /FTId=PRO_0000000749. FT MOD_RES 3 3 N-acetylglutamate (By similarity). FT CONFLICT 130 130 V -> F (in Ref. 4; CAG38753). SQ SEQUENCE 376 AA; 41877 MW; 6EC08CD5EEAD445E CRC64; MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THNVPIYEGY ALPHAIMRLD LAGRDLTDYL MKILTERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS YELPDGQVIT IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK PEYDEAGPSI VHRKCF //