ID A0A087WSZ2_HUMAN Unreviewed; 944 AA. AC A0A087WSZ2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 27-SEP-2017, entry version 24. DE SubName: Full=Alpha-actinin-3 {ECO:0000313|Ensembl:ENSP00000422007}; GN Name=ACTN3 {ECO:0000313|Ensembl:ENSP00000422007}; 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 {ECO:0000313|Ensembl:ENSP00000422007, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000422007} 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 [2] {ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [3] {ECO:0000313|Ensembl:ENSP00000422007} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00448}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSP00000422007}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AMYH02024979; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP002748; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001245300.2; NM_001258371.2. DR UniGene; Hs.654432; -. DR UniGene; Hs.737862; -. DR ProteinModelPortal; A0A087WSZ2; -. DR PeptideAtlas; A0A087WSZ2; -. DR PRIDE; A0A087WSZ2; -. DR Ensembl; ENST00000502692; ENSP00000422007; ENSG00000248746. DR GeneID; 89; -. DR UCSC; uc031xsh.2; human. DR CTD; 89; -. DR EuPathDB; HostDB:ENSG00000248746.5; -. DR HGNC; HGNC:165; ACTN3. DR OpenTargets; ENSG00000248746; -. DR GeneTree; ENSGT00760000118813; -. DR OMA; QTMRAMQ; -. DR OrthoDB; EOG091G020R; -. DR GenomeRNAi; 89; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000248746; -. DR ExpressionAtlas; A0A087WSZ2; baseline and differential. DR GO; GO:0005903; C:brush border; IEA:Ensembl. DR GO; GO:0030018; C:Z disc; IEA:Ensembl. DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl. DR GO; GO:0006936; P:muscle contraction; IEA:Ensembl. DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl. DR GO; GO:0045820; P:negative regulation of glycolytic process; IEA:Ensembl. DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IEA:Ensembl. DR GO; GO:1901078; P:negative regulation of relaxation of muscle; IEA:Ensembl. DR GO; GO:1900159; P:positive regulation of bone mineralization involved in bone maturation; IEA:Ensembl. DR GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; IEA:Ensembl. DR GO; GO:1904025; P:positive regulation of glucose catabolic process to lactate via pyruvate; IEA:Ensembl. DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IEA:Ensembl. DR GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IEA:Ensembl. DR GO; GO:1903715; P:regulation of aerobic respiration; IEA:Ensembl. DR GO; GO:0014728; P:regulation of the force of skeletal muscle contraction; IEA:Ensembl. DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEA:Ensembl. DR GO; GO:0014732; P:skeletal muscle atrophy; IEA:Ensembl. DR GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl. DR CDD; cd00014; CH; 2. DR CDD; cd00051; EFh; 1. DR Gene3D; 1.10.418.10; -; 2. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH-domain. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR014837; EF-hand_Ca_insen. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR Pfam; PF00307; CH; 2. DR Pfam; PF08726; EFhand_Ca_insen; 1. DR Pfam; PF00435; Spectrin; 4. DR SMART; SM00033; CH; 2. DR SMART; SM00054; EFh; 2. DR SMART; SM00150; SPEC; 2. DR SUPFAM; SSF47473; SSF47473; 1. DR SUPFAM; SSF47576; SSF47576; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS50222; EF_HAND_2; 2. PE 1: Evidence at protein level; KW Actin-binding {ECO:0000256|SAAS:SAAS00782879}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A087WSZ2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Repeat {ECO:0000256|SAAS:SAAS00782917}. FT DOMAIN 88 192 Calponin-homology (CH). FT {ECO:0000259|PROSITE:PS50021}. FT DOMAIN 201 304 Calponin-homology (CH). FT {ECO:0000259|PROSITE:PS50021}. FT DOMAIN 803 838 EF-hand. {ECO:0000259|PROSITE:PS50222}. FT DOMAIN 839 874 EF-hand. {ECO:0000259|PROSITE:PS50222}. FT COILED 322 349 {ECO:0000256|SAM:Coils}. FT COILED 543 570 {ECO:0000256|SAM:Coils}. FT COILED 728 755 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 944 AA; 107629 MW; D8A7BE9FA569BD3D CRC64; MGIGLCVPPA RCWKRLTRSS RGQPLERPAA TIIIGLSIVE RSKQTQRGPV DFSRSHSAPA AEQECKPRIS AARSTPAPPS PAVPGFRTTP CQTFTAWCNS HLRKAGTQIE NIEEDFRNGL KLMLLLEVIS GERLPRPDKG KMRFHKIANV NKALDFIASK GVKLVSIGAE EIVDGNLKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYRN VNVQNFHTSW KDGLALCALI HRHRPDLIDY AKLRKDDPIG NLNTAFEVAE KYLDIPKMLD AEDIVNTPKP DEKAIMTYVS CFYHAFAGAE QAETAANRIC KVLAVNQENE KLMEEYEKLA SELLEWIRRT VPWLENRVGE PSMSAMQRKL EDFRDYRRLH KPPRIQEKCQ LEINFNTLQT KLRLSHRPAF MPSEGKLVSD IANAWRGLEQ VEKGYEDWLL SEIRRLQRLQ HLAEKFRQKA SLHEAWTRGK EEMLSQRDYD SALLQEVRAL LRRHEAFESD LAAHQDRVEH IAALAQELNE LDYHEAASVN SRCQAICDQW DNLGTLTQKR RDALERMEKL LETIDRLQLE FARRAAPFNN WLDGAVEDLQ DVWLVHSVEE TQSLLTAHDQ FKATLPEADR ERGAIMGIQG EIQKICQTYG LRPCSTNPYI TLSPQDINTK WDMVRKLVPS CDQTLQEELA RQQVNERLRR QFAAQANAIG PWIQAKVEEV GRLAAGLAGS LEEQMAGLRQ QEQNIINYKT NIDRLEGDHQ LLQESLVFDN KHTVYSMEHI RVGWEQLLTS IARTINEVEN QVLTRDAKGL SQEQLNEFRA SFNHFDRKQN GMMEPDDFRA CLISMGYDLG EVEFARIMTM VDPNAAGVVT FQAFIDFMTR ETAETDTTEQ VVASFKILAG DKNYITPEEL RRELPAKQAE YCIRRMVPYK GSGAPAGALD YVAFSSALYG ESDL //