ACTN1_HUMAN
ID ACTN1_HUMAN Reviewed; 892 AA.
AC P12814; B3V8S3; B4DHH3; B7TY16; Q1HE25; Q9BTN1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 248.
DE RecName: Full=Alpha-actinin-1;
DE AltName: Full=Alpha-actinin cytoskeletal isoform;
DE AltName: Full=F-actin cross-linking protein;
DE AltName: Full=Non-muscle alpha-actinin-1;
GN Name=ACTN1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=2780298; DOI=10.1093/nar/17.16.6725;
RA Millake D.B., Blanchard A.D., Patel B., Critchley D.R.;
RT "The cDNA sequence of a human placental alpha-actinin.";
RL Nucleic Acids Res. 17:6725-6725(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2349951;
RA Youssoufian H., McAfee M., Kwiatkowski D.J.;
RT "Cloning and chromosomal localization of the human cytoskeletal alpha-
RT actinin gene reveals linkage to the beta-spectrin gene.";
RL Am. J. Hum. Genet. 47:62-71(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=18353764; DOI=10.1074/mcp.m700590-mcp200;
RA Thorsen K., Sorensen K.D., Brems-Eskildsen A.S., Modin C., Gaustadnes M.,
RA Hein A.M., Kruhoffer M., Laurberg S., Borre M., Wang K., Brunak S.,
RA Krainer A.R., Torring N., Dyrskjot L., Andersen C.L., Orntoft T.F.;
RT "Alternative splicing in colon, bladder, and prostate cancer identified by
RT exon array analysis.";
RL Mol. Cell. Proteomics 7:1214-1224(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Tongue;
RA Mancini U.M., Tajara E.H.;
RT "A new mRNA isoform from ACTN1 gene.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Mansilla F., Orntoft T.F., Birkenkamp-Demtroeder K.;
RT "Actinin alpha 1 alternative splicing variant.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Skin;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 297-892 (ISOFORM 1).
RX PubMed=2169343;
RA Nishiyama M., Ozturk M., Frohlich M., Mafune K., Steele G. Jr., Wands J.R.;
RT "Expression of human alpha-actinin in human hepatocellular carcinoma.";
RL Cancer Res. 50:6291-6294(1990).
RN [12]
RP PROTEIN SEQUENCE OF 1-21.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [13]
RP PROTEIN SEQUENCE OF 134-146.
RX PubMed=8713105; DOI=10.1006/bbrc.1996.1082;
RA Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.;
RT "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-
RT actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes.";
RL Biochem. Biophys. Res. Commun. 224:666-674(1996).
RN [14]
RP PROTEIN SEQUENCE OF 566-577; 727-738 AND 835-863, AND SUBCELLULAR LOCATION.
RX PubMed=7750553; DOI=10.1016/0014-5793(95)00362-d;
RA Dubernard V., Faucher D., Launay J.-M., Legrand C.;
RT "Identification of the cytoskeletal protein alpha-actinin as a platelet
RT thrombospondin-binding protein.";
RL FEBS Lett. 364:109-114(1995).
RN [15]
RP INTERACTION WITH TTID.
RX PubMed=10369880; DOI=10.1093/hmg/8.7.1329;
RA Salmikangas P., Mykkaenen O.M., Groenholm M., Heiska L., Kere J.,
RA Carpen O.;
RT "Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded
RT by a candidate gene for limb-girdle muscular dystrophy.";
RL Hum. Mol. Genet. 8:1329-1336(1999).
RN [16]
RP INTERACTION WITH MYOZ2.
RX PubMed=11114196; DOI=10.1073/pnas.260501097;
RA Frey N., Richardson J.A., Olson E.N.;
RT "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000).
RN [17]
RP PHOSPHORYLATION AT TYR-12.
RX PubMed=11369769; DOI=10.1074/jbc.m101678200;
RA Izaguirre G., Aguirre L., Hu Y.P., Lee H.Y., Schlaepfer D.D.,
RA Aneskievich B.J., Haimovich B.;
RT "The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylated on
RT its actin-binding domain by the focal adhesion kinase.";
RL J. Biol. Chem. 276:28676-28685(2001).
RN [18]
RP INTERACTION WITH LPP.
RX PubMed=12615977; DOI=10.1242/jcs.00309;
RA Li B., Zhuang L., Reinhard M., Trueb B.;
RT "The lipoma preferred partner LPP interacts with alpha-actinin.";
RL J. Cell Sci. 116:1359-1366(2003).
RN [19]
RP INTERACTION WITH DDN.
RX PubMed=16464232; DOI=10.1111/j.1471-4159.2006.03679.x;
RA Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A.;
RT "Postsynaptic recruitment of Dendrin depends on both dendritic mRNA
RT transport and synaptic anchoring.";
RL J. Neurochem. 96:1659-1666(2006).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-195 AND LYS-676, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471 AND SER-677, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 30-253.
RX PubMed=16698282; DOI=10.1016/j.jsb.2006.01.013;
RA Borrego-Diaz E., Kerff F., Lee S.H., Ferron F., Li Y., Dominguez R.;
RT "Crystal structure of the actin-binding domain of alpha-actinin 1:
RT evaluating two competing actin-binding models.";
RL J. Struct. Biol. 155:230-238(2006).
RN [26]
RP VARIANTS BDPLT15 LYS-32; GLN-46; ILE-105; LYS-225; TRP-738 AND GLN-752,
RP VARIANT TRP-197, AND CHARACTERIZATION OF VARIANTS BDPLT15 LYS-32 AND
RP ILE-105.
RX PubMed=23434115; DOI=10.1016/j.ajhg.2013.01.015;
RA Kunishima S., Okuno Y., Yoshida K., Shiraishi Y., Sanada M., Muramatsu H.,
RA Chiba K., Tanaka H., Miyazaki K., Sakai M., Ohtake M., Kobayashi R.,
RA Iguchi A., Niimi G., Otsu M., Takahashi Y., Miyano S., Saito H., Kojima S.,
RA Ogawa S.;
RT "ACTN1 mutations cause congenital macrothrombocytopenia.";
RL Am. J. Hum. Genet. 92:431-438(2013).
RN [27]
RP VARIANT BDPLT15 GLN-46, CHARACTERIZATION OF VARIANT BDPLT15 GLN-46, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24069336; DOI=10.1371/journal.pone.0074728;
RA Gueguen P., Rouault K., Chen J.M., Raguenes O., Fichou Y., Hardy E.,
RA Gobin E., Pan-Petesch B., Kerbiriou M., Trouve P., Marcorelles P.,
RA Abgrall J.F., Le Marechal C., Ferec C.;
RT "A missense mutation in the alpha-actinin 1 gene (ACTN1) is the cause of
RT autosomal dominant macrothrombocytopenia in a large French family.";
RL PLoS ONE 8:E74728-E74728(2013).
CC -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC actin to a variety of intracellular structures. This is a bundling
CC protein.
CC -!- SUBUNIT: Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP
CC (PubMed:10369880, PubMed:11114196, PubMed:12615977). Interacts with DDN
CC (PubMed:16464232). Interacts with PSD. Interacts with MICALL2 (By
CC similarity). Interacts with DNM2 and CTTN. Interacts with PDLIM1.
CC Interacts with PDLIM2. Interacts with PDLIM4 (via PDZ domain) (By
CC similarity). {ECO:0000250|UniProtKB:Q7TPR4,
CC ECO:0000250|UniProtKB:Q9Z1P2, ECO:0000269|PubMed:10369880,
CC ECO:0000269|PubMed:11114196, ECO:0000269|PubMed:12615977,
CC ECO:0000269|PubMed:16464232}.
CC -!- INTERACTION:
CC P12814; P35609: ACTN2; NbExp=3; IntAct=EBI-351710, EBI-77797;
CC P12814; Q08043: ACTN3; NbExp=3; IntAct=EBI-351710, EBI-2880652;
CC P12814; Q92624: APPBP2; NbExp=3; IntAct=EBI-351710, EBI-743771;
CC P12814; Q96QS3: ARX; NbExp=2; IntAct=EBI-351710, EBI-11107474;
CC P12814; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-351710, EBI-725606;
CC P12814; Q13936: CACNA1C; NbExp=2; IntAct=EBI-351710, EBI-1038838;
CC P12814; Q8NA61: CBY2; NbExp=3; IntAct=EBI-351710, EBI-741724;
CC P12814; P63172: DYNLT1; NbExp=3; IntAct=EBI-351710, EBI-1176455;
CC P12814; P05198: EIF2S1; NbExp=3; IntAct=EBI-351710, EBI-1056162;
CC P12814; Q7L775: EPM2AIP1; NbExp=6; IntAct=EBI-351710, EBI-6255981;
CC P12814; O95257: GADD45G; NbExp=3; IntAct=EBI-351710, EBI-448202;
CC P12814; Q9Y223: GNE; NbExp=3; IntAct=EBI-351710, EBI-4291090;
CC P12814; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-351710, EBI-2511344;
CC P12814; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-351710, EBI-739832;
CC P12814; Q8IY33: MICALL2; NbExp=6; IntAct=EBI-351710, EBI-2555563;
CC P12814; A0A0S2Z4Y0: MYOT; NbExp=3; IntAct=EBI-351710, EBI-16430371;
CC P12814; Q9NP98: MYOZ1; NbExp=4; IntAct=EBI-351710, EBI-744402;
CC P12814; Q9NPC6: MYOZ2; NbExp=11; IntAct=EBI-351710, EBI-746712;
CC P12814; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-351710, EBI-3920396;
CC P12814; P00973: OAS1; NbExp=4; IntAct=EBI-351710, EBI-3932815;
CC P12814; P00973-2: OAS1; NbExp=3; IntAct=EBI-351710, EBI-12081862;
CC P12814; P50479: PDLIM4; NbExp=3; IntAct=EBI-351710, EBI-372861;
CC P12814; Q9BYB0: SHANK3; NbExp=2; IntAct=EBI-351710, EBI-1752330;
CC P12814; P12931: SRC; NbExp=2; IntAct=EBI-351710, EBI-621482;
CC P12814; Q8N3V7: SYNPO; NbExp=2; IntAct=EBI-351710, EBI-352936;
CC P12814; Q9H987-2: SYNPO2L; NbExp=3; IntAct=EBI-351710, EBI-12082116;
CC P12814; Q8WZ42: TTN; NbExp=2; IntAct=EBI-351710, EBI-681210;
CC P12814; P10599: TXN; NbExp=3; IntAct=EBI-351710, EBI-594644;
CC P12814; O75604: USP2; NbExp=3; IntAct=EBI-351710, EBI-743272;
CC P12814; B2R8Y4; NbExp=3; IntAct=EBI-351710, EBI-10175581;
CC P12814; Q8VC66: Ssx2ip; Xeno; NbExp=3; IntAct=EBI-351710, EBI-6654049;
CC P12814; PRO_0000037577 [P27958]; Xeno; NbExp=7; IntAct=EBI-351710, EBI-6904388;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24069336, ECO:0000269|PubMed:7750553}. Cytoplasm,
CC myofibril, sarcomere, Z line {ECO:0000269|PubMed:7750553}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9Z1P2}. Cell junction
CC {ECO:0000250|UniProtKB:Q9Z1P2}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q7TPR4}. Note=Colocalizes with MYOZ2 and PPP3CA
CC at the Z-line of heart and skeletal muscle. Colocalizes with PSD in
CC membrane ruffles and central reticular structures.
CC {ECO:0000250|UniProtKB:Q7TPR4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P12814-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12814-2; Sequence=VSP_041264;
CC Name=3;
CC IsoId=P12814-3; Sequence=VSP_043525;
CC Name=4;
CC IsoId=P12814-4; Sequence=VSP_041264, VSP_047763;
CC -!- DISEASE: Bleeding disorder, platelet-type, 15 (BDPLT15) [MIM:615193]:
CC An autosomal dominant form of macrothrombocytopenia. Affected
CC individuals usually have no or only mild bleeding tendency, such as
CC epistaxis. Laboratory studies show decreased numbers of large platelets
CC and anisocytosis, but the platelets show no in vitro functional
CC abnormalities. {ECO:0000269|PubMed:23434115,
CC ECO:0000269|PubMed:24069336}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; X15804; CAA33803.1; -; mRNA.
DR EMBL; M95178; AAA51582.1; -; mRNA.
DR EMBL; EU716325; ACE62922.1; -; mRNA.
DR EMBL; DQ496098; ABF50047.1; -; mRNA.
DR EMBL; FJ410030; ACJ24535.1; -; mRNA.
DR EMBL; BT007207; AAP35871.1; -; mRNA.
DR EMBL; AK295099; BAG58135.1; -; mRNA.
DR EMBL; AL117694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW80975.1; -; Genomic_DNA.
DR EMBL; BC003576; AAH03576.1; -; mRNA.
DR EMBL; BC015766; AAH15766.1; -; mRNA.
DR EMBL; X55187; CAA38970.1; -; mRNA.
DR CCDS; CCDS45129.1; -. [P12814-2]
DR CCDS; CCDS45130.1; -. [P12814-3]
DR CCDS; CCDS9792.1; -. [P12814-1]
DR PIR; S05503; FAHUAA.
DR RefSeq; NP_001093.1; NM_001102.3. [P12814-1]
DR RefSeq; NP_001123476.1; NM_001130004.1. [P12814-3]
DR RefSeq; NP_001123477.1; NM_001130005.1. [P12814-2]
DR PDB; 2EYI; X-ray; 1.70 A; A=30-253.
DR PDB; 2EYN; X-ray; 1.80 A; A=30-253.
DR PDB; 2N8Y; NMR; -; A=743-892.
DR PDB; 2N8Z; NMR; -; A=743-892.
DR PDBsum; 2EYI; -.
DR PDBsum; 2EYN; -.
DR PDBsum; 2N8Y; -.
DR PDBsum; 2N8Z; -.
DR AlphaFoldDB; P12814; -.
DR SMR; P12814; -.
DR BioGRID; 106602; 243.
DR CORUM; P12814; -.
DR DIP; DIP-33184N; -.
DR IntAct; P12814; 122.
DR MINT; P12814; -.
DR STRING; 9606.ENSP00000377941; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB06773; Human calcitonin.
DR CarbonylDB; P12814; -.
DR GlyGen; P12814; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P12814; -.
DR MetOSite; P12814; -.
DR PhosphoSitePlus; P12814; -.
DR SwissPalm; P12814; -.
DR BioMuta; ACTN1; -.
DR DMDM; 46397817; -.
DR OGP; P12814; -.
DR EPD; P12814; -.
DR jPOST; P12814; -.
DR MassIVE; P12814; -.
DR MaxQB; P12814; -.
DR PaxDb; P12814; -.
DR PeptideAtlas; P12814; -.
DR PRIDE; P12814; -.
DR ProteomicsDB; 52871; -. [P12814-1]
DR ProteomicsDB; 52872; -. [P12814-2]
DR ProteomicsDB; 52873; -. [P12814-3]
DR ProteomicsDB; 6259; -.
DR Antibodypedia; 51; 497 antibodies from 39 providers.
DR DNASU; 87; -.
DR Ensembl; ENST00000193403.10; ENSP00000193403.6; ENSG00000072110.16. [P12814-1]
DR Ensembl; ENST00000394419.9; ENSP00000377941.4; ENSG00000072110.16. [P12814-3]
DR Ensembl; ENST00000438964.6; ENSP00000414272.2; ENSG00000072110.16. [P12814-2]
DR Ensembl; ENST00000538545.6; ENSP00000439828.2; ENSG00000072110.16. [P12814-4]
DR GeneID; 87; -.
DR KEGG; hsa:87; -.
DR MANE-Select; ENST00000394419.9; ENSP00000377941.4; NM_001130004.2; NP_001123476.1. [P12814-3]
DR UCSC; uc001xkl.4; human. [P12814-1]
DR CTD; 87; -.
DR DisGeNET; 87; -.
DR GeneCards; ACTN1; -.
DR HGNC; HGNC:163; ACTN1.
DR HPA; ENSG00000072110; Tissue enhanced (smooth).
DR MalaCards; ACTN1; -.
DR MIM; 102575; gene.
DR MIM; 615193; phenotype.
DR neXtProt; NX_P12814; -.
DR OpenTargets; ENSG00000072110; -.
DR Orphanet; 140957; Autosomal dominant macrothrombocytopenia.
DR PharmGKB; PA24; -.
DR VEuPathDB; HostDB:ENSG00000072110; -.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000155548; -.
DR HOGENOM; CLU_005217_1_1_1; -.
DR InParanoid; P12814; -.
DR OMA; QRFENVN; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; P12814; -.
DR TreeFam; TF352676; -.
DR PathwayCommons; P12814; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-373753; Nephrin family interactions.
DR Reactome; R-HSA-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; P12814; -.
DR SIGNOR; P12814; -.
DR BioGRID-ORCS; 87; 16 hits in 1083 CRISPR screens.
DR ChiTaRS; ACTN1; human.
DR EvolutionaryTrace; P12814; -.
DR GeneWiki; Actinin,_alpha_1; -.
DR GenomeRNAi; 87; -.
DR Pharos; P12814; Tbio.
DR PRO; PR:P12814; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P12814; protein.
DR Bgee; ENSG00000072110; Expressed in blood vessel layer and 205 other tissues.
DR ExpressionAtlas; P12814; baseline and differential.
DR Genevisible; P12814; HS.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0031143; C:pseudopodium; TAS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005519; F:cytoskeletal regulatory protein binding; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0099186; F:structural constituent of postsynapse; IDA:SynGO.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0017166; F:vinculin binding; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IEA:Ensembl.
DR GO; GO:0051639; P:actin filament network formation; IMP:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR GO; GO:0030220; P:platelet formation; IMP:UniProtKB.
DR GO; GO:0036344; P:platelet morphogenesis; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Calcium;
KW Cell junction; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..892
FT /note="Alpha-actinin-1"
FT /id="PRO_0000073431"
FT DOMAIN 31..135
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 144..250
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 274..384
FT /note="Spectrin 1"
FT REPEAT 394..499
FT /note="Spectrin 2"
FT REPEAT 509..620
FT /note="Spectrin 3"
FT REPEAT 630..733
FT /note="Spectrin 4"
FT DOMAIN 746..781
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 787..822
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..247
FT /note="Actin-binding"
FT REGION 274..733
FT /note="Interaction with DDN"
FT /evidence="ECO:0000269|PubMed:16464232"
FT BINDING 759
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 761
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 763
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 765
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 770
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 12
FT /note="Phosphotyrosine; by FAK1"
FT /evidence="ECO:0000269|PubMed:11369769"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 195
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 676
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1P2"
FT VAR_SEQ 761..787
FT /note="DHSGTLGPEEFKACLISLGYDIGNDPQ -> KKTGMMDTDDFRACLISMGYN
FT M (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18353764, ECO:0000303|Ref.5"
FT /id="VSP_041264"
FT VAR_SEQ 787
FT /note="Q -> QKKTGMMDTDDFRACLISMGYNM (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_043525"
FT VAR_SEQ 840
FT /note="K -> KLQEGGKMQTAHAAFTPPGFAAVSGRAALRLLDFAAFLTTLSSQ
FT (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_047763"
FT VARIANT 32
FT /note="Q -> K (in BDPLT15; the mutation dominantly affects
FT the actin filament assembly likely resulting in abnormal
FT cytoskeletal organization; dbSNP:rs387907346)"
FT /evidence="ECO:0000269|PubMed:23434115"
FT /id="VAR_069910"
FT VARIANT 46
FT /note="R -> Q (in BDPLT15; disorganization of the actin and
FT alpha-actinin 1 filaments; dbSNP:rs387907348)"
FT /evidence="ECO:0000269|PubMed:23434115,
FT ECO:0000269|PubMed:24069336"
FT /id="VAR_069911"
FT VARIANT 105
FT /note="V -> I (in BDPLT15; the mutation dominantly affects
FT the actin filament assembly likely resulting in abnormal
FT cytoskeletal organization; dbSNP:rs387907345)"
FT /evidence="ECO:0000269|PubMed:23434115"
FT /id="VAR_069912"
FT VARIANT 197
FT /note="R -> W (in dbSNP:rs904887313)"
FT /evidence="ECO:0000269|PubMed:23434115"
FT /id="VAR_069913"
FT VARIANT 225
FT /note="E -> K (in BDPLT15; dbSNP:rs387907350)"
FT /evidence="ECO:0000269|PubMed:23434115"
FT /id="VAR_069914"
FT VARIANT 707
FT /note="N -> T (in dbSNP:rs7157661)"
FT /id="VAR_053883"
FT VARIANT 738
FT /note="R -> W (in BDPLT15; dbSNP:rs387907349)"
FT /evidence="ECO:0000269|PubMed:23434115"
FT /id="VAR_069915"
FT VARIANT 752
FT /note="R -> Q (in BDPLT15; dbSNP:rs387907347)"
FT /evidence="ECO:0000269|PubMed:23434115"
FT /id="VAR_069916"
FT VARIANT 868
FT /note="T -> S (in dbSNP:rs11557769)"
FT /id="VAR_053884"
FT CONFLICT 317
FT /note="R -> L (in Ref. 11; CAA38970)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="R -> H (in Ref. 7; BAG58135)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="T -> A (in Ref. 7; BAG58135)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="Q -> L (in Ref. 11; CAA38970)"
FT /evidence="ECO:0000305"
FT CONFLICT 630..631
FT /note="RL -> SV (in Ref. 1; CAA33803)"
FT /evidence="ECO:0000305"
FT CONFLICT 654..656
FT /note="GRI -> ARF (in Ref. 11; CAA38970)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="Y -> D (in Ref. 11; CAA38970)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="L -> S (in Ref. 11; CAA38970)"
FT /evidence="ECO:0000305"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2EYI"
FT TURN 55..61
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:2EYI"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:2EYI"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:2EYI"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 235..249
FT /evidence="ECO:0007829|PDB:2EYI"
FT HELIX 745..751
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 754..757
FT /evidence="ECO:0007829|PDB:2N8Y"
FT STRAND 763..766
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 768..774
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 775..778
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 788..798
FT /evidence="ECO:0007829|PDB:2N8Y"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 809..816
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 818..820
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 826..830
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 832..837
FT /evidence="ECO:0007829|PDB:2N8Y"
FT STRAND 841..844
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 845..851
FT /evidence="ECO:0007829|PDB:2N8Y"
FT HELIX 855..863
FT /evidence="ECO:0007829|PDB:2N8Y"
FT STRAND 864..867
FT /evidence="ECO:0007829|PDB:2N8Y"
FT STRAND 869..872
FT /evidence="ECO:0007829|PDB:2N8Y"
FT STRAND 876..881
FT /evidence="ECO:0007829|PDB:2N8Y"
FT TURN 884..888
FT /evidence="ECO:0007829|PDB:2N8Y"
SQ SEQUENCE 892 AA; 103058 MW; 6DA3E4D1A0289519 CRC64;
MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT QIENIEEDFR
DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI ASKGVKLVSI GAEEIVDGNV
KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC
ALIHRHRPEL IDYGKLRKDD PLTNLNTAFD VAEKYLDIPK MLDAEDIVGT ARPDEKAIMT
YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR
VPENTMHAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR PAFMPSEGRM
VSDINNAWGC LEQVEKGYEE WLLNEIRRLE RLDHLAEKFR QKASIHEAWT DGKEAMLRQK
DYETATLSEI KALLKKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYYDSP SVNARCQKIC
DQWDNLGALT QKRREALERT EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT
IEEIQGLTTA HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI
NGKWDHVRQL VPRRDQALTE EHARQQHNER LRKQFGAQAN VIGPWIQTKM EEIGRISIEM
HGTLEDQLSH LRQYEKSIVN YKPKIDQLEG DHQLIQEALI FDNKHTNYTM EHIRVGWEQL
LTTIARTINE VENQILTRDA KGISQEQMNE FRASFNHFDR DHSGTLGPEE FKACLISLGY
DIGNDPQGEA EFARIMSIVD PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK
NYITMDELRR ELPPDQAEYC IARMAPYTGP DSVPGALDYM SFSTALYGES DL
