MTPN_HUMAN
ID MTPN_HUMAN Reviewed; 118 AA.
AC P58546;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Myotrophin;
DE AltName: Full=Protein V-1;
GN Name=MTPN;
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], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=10329199; DOI=10.1006/jmcc.1998.0903;
RA Anderson K.M., Berrebi-Bertrand I., Kirkpatrick R.B., McQueney M.S.,
RA Underwood D.C., Rouanet S., Chabot-Fletcher M.;
RT "cDNA sequence and characterization of the gene that encodes human
RT myotrophin/V-1 protein, a mediator of cardiac hypertrophy.";
RL J. Mol. Cell. Cardiol. 31:705-719(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP FUNCTION, IDENTIFICATION IN AN ACTIN CAPPING COMPLEX, AND INTERACTION WITH
RP CAPZA1 AND CAPZB.
RX PubMed=16895918; DOI=10.1074/jbc.m606278200;
RA Bhattacharya N., Ghosh S., Sept D., Cooper J.A.;
RT "Binding of myotrophin/V-1 to actin-capping protein: implications for how
RT capping protein binds to the filament barbed end.";
RL J. Biol. Chem. 281:31021-31030(2006).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-11 AND LYS-24, 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CAPZA1 AND CAPZB, AND
RP FUNCTION.
RX PubMed=20625546; DOI=10.1371/journal.pbio.1000416;
RA Takeda S., Minakata S., Koike R., Kawahata I., Narita A., Kitazawa M.,
RA Ota M., Yamakuni T., Maeda Y., Nitanai Y.;
RT "Two distinct mechanisms for actin capping protein regulation--steric and
RT allosteric inhibition.";
RL PLoS Biol. 8:E1000416-E1000416(2010).
CC -!- FUNCTION: Promotes dimerization of NF-kappa-B subunits and regulates
CC NF-kappa-B transcription factor activity (By similarity). Plays a role
CC in the regulation of the growth of actin filaments. Inhibits the
CC activity of the F-actin-capping protein complex formed by the CAPZA1
CC and CAPZB heterodimer. Promotes growth of cardiomyocytes, but not
CC cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy.
CC {ECO:0000250, ECO:0000269|PubMed:10329199, ECO:0000269|PubMed:16895918,
CC ECO:0000269|PubMed:20625546}.
CC -!- SUBUNIT: Interacts with RELA (By similarity). Interacts with the
CC heterodimer formed by CAPZA1 and CAPZB. {ECO:0000250,
CC ECO:0000269|PubMed:16895918, ECO:0000269|PubMed:20625546}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}.
CC Cytoplasm, perinuclear region {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10329199}.
CC -!- INDUCTION: Up-regulated in heart left ventricle of patients with severe
CC coronary artery disease and history of myocardial ischemia. Up-
CC regulated in heart left ventricle of patients with dilated
CC cardiomyopathy. {ECO:0000269|PubMed:10329199}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the MPD6 protein from a non-overlapping reading frame.
CC MPD6 belongs to a group of cryptic antigens without conventional
CC genomic structure. It is encoded by a cryptic open reading frame
CC located in the 3'-untranslated region of MTPN.
CC -!- SIMILARITY: Belongs to the myotrophin family. {ECO:0000305}.
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DR EMBL; AC015987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028093; AAH28093.1; -; mRNA.
DR CCDS; CCDS5842.1; -.
DR RefSeq; NP_665807.1; NM_145808.3.
DR PDB; 3AAA; X-ray; 2.20 A; C=1-118.
DR PDB; 7DF7; X-ray; 2.30 A; A/B=1-118.
DR PDB; 7DSA; X-ray; 2.80 A; C=1-118.
DR PDB; 7DSB; X-ray; 2.44 A; C=1-118.
DR PDBsum; 3AAA; -.
DR PDBsum; 7DF7; -.
DR PDBsum; 7DSA; -.
DR PDBsum; 7DSB; -.
DR AlphaFoldDB; P58546; -.
DR BMRB; P58546; -.
DR SMR; P58546; -.
DR BioGRID; 126455; 140.
DR DIP; DIP-50234N; -.
DR IntAct; P58546; 26.
DR MINT; P58546; -.
DR STRING; 9606.ENSP00000376800; -.
DR GlyGen; P58546; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P58546; -.
DR PhosphoSitePlus; P58546; -.
DR SwissPalm; P58546; -.
DR BioMuta; MTPN; -.
DR DMDM; 20138912; -.
DR OGP; P58546; -.
DR EPD; P58546; -.
DR jPOST; P58546; -.
DR MassIVE; P58546; -.
DR PaxDb; P58546; -.
DR PeptideAtlas; P58546; -.
DR PRIDE; P58546; -.
DR ProteomicsDB; 57087; -.
DR TopDownProteomics; P58546; -.
DR Antibodypedia; 18167; 109 antibodies from 25 providers.
DR DNASU; 136319; -.
DR Ensembl; ENST00000393085.4; ENSP00000376800.3; ENSG00000105887.11.
DR GeneID; 136319; -.
DR KEGG; hsa:136319; -.
DR MANE-Select; ENST00000393085.4; ENSP00000376800.3; NM_145808.4; NP_665807.1.
DR CTD; 136319; -.
DR DisGeNET; 136319; -.
DR GeneCards; MTPN; -.
DR HGNC; HGNC:15667; MTPN.
DR HPA; ENSG00000105887; Low tissue specificity.
DR MIM; 606484; gene.
DR neXtProt; NX_P58546; -.
DR OpenTargets; ENSG00000105887; -.
DR PharmGKB; PA31271; -.
DR VEuPathDB; HostDB:ENSG00000105887; -.
DR eggNOG; KOG4214; Eukaryota.
DR GeneTree; ENSGT00430000031071; -.
DR HOGENOM; CLU_000134_45_7_1; -.
DR InParanoid; P58546; -.
DR OMA; TALIDCT; -.
DR OrthoDB; 1435166at2759; -.
DR PhylomeDB; P58546; -.
DR TreeFam; TF327387; -.
DR PathwayCommons; P58546; -.
DR SignaLink; P58546; -.
DR BioGRID-ORCS; 136319; 18 hits in 1075 CRISPR screens.
DR ChiTaRS; MTPN; human.
DR EvolutionaryTrace; P58546; -.
DR GeneWiki; MTPN; -.
DR GenomeRNAi; 136319; -.
DR Pharos; P58546; Tbio.
DR PRO; PR:P58546; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P58546; protein.
DR Bgee; ENSG00000105887; Expressed in cardiac muscle of right atrium and 191 other tissues.
DR ExpressionAtlas; P58546; baseline and differential.
DR Genevisible; P58546; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0008290; C:F-actin capping protein complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; NAS:UniProtKB.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010557; P:positive regulation of macromolecule biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISS:UniProtKB.
DR GO; GO:2000812; P:regulation of barbed-end actin filament capping; IDA:UniProtKB.
DR GO; GO:0008361; P:regulation of cell size; IDA:UniProtKB.
DR GO; GO:0016202; P:regulation of striated muscle tissue development; NAS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; NAS:UniProtKB.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ANK repeat; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62774"
FT CHAIN 2..118
FT /note="Myotrophin"
FT /id="PRO_0000067031"
FT REPEAT 2..30
FT /note="ANK 1"
FT REPEAT 34..66
FT /note="ANK 2"
FT REPEAT 67..99
FT /note="ANK 3"
FT MOD_RES 2
FT /note="N-acetylcysteine"
FT /evidence="ECO:0000250|UniProtKB:P62774"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:3AAA"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:3AAA"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:3AAA"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:3AAA"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3AAA"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:3AAA"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:3AAA"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:3AAA"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:3AAA"
SQ SEQUENCE 118 AA; 12895 MW; 9097FFDF61D329A2 CRC64;
MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD
INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ
