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   27-MAR-2024, entry version 181.
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; 153.
DR   DIP; DIP-50234N; -.
DR   IntAct; P58546; 28.
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; 9606-ENSP00000376800; -.
DR   PeptideAtlas; P58546; -.
DR   ProteomicsDB; 57087; -.
DR   Pumba; P58546; -.
DR   TopDownProteomics; P58546; -.
DR   Antibodypedia; 18167; 124 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   AGR; HGNC:15667; -.
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; WAIKNGD; -.
DR   OrthoDB; 5475373at2759; -.
DR   PhylomeDB; P58546; -.
DR   TreeFam; TF327387; -.
DR   PathwayCommons; P58546; -.
DR   SignaLink; P58546; -.
DR   BioGRID-ORCS; 136319; 21 hits in 1147 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 193 other cell types or tissues.
DR   ExpressionAtlas; P58546; baseline and differential.
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; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR   PANTHER; PTHR24171:SF8; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   Genevisible; P58546; HS.
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
//