Full text data of MTPN
MTPN
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Myotrophin (Protein V-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Myotrophin (Protein V-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00179589
IPI00179589 Myotrophin Ubiquitous, protein binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00179589 Myotrophin Ubiquitous, protein binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P58546
ID MTPN_HUMAN Reviewed; 118 AA.
AC P58546;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Myotrophin;
DE AltName: Full=Protein V-1;
GN Name=MTPN;
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], FUNCTION, INDUCTION, AND TISSUE
RP 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, IDENTIFICATION IN AN ACTIN CAPPING COMPLEX, AND INTERACTION
RP WITH WITH 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
RT how capping protein binds to the filament barbed end.";
RL J. Biol. Chem. 281:31021-31030(2006).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2; LYS-4; LYS-11 AND LYS-24,
RP MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CAPZA1 AND
RP CAPZB, AND 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
RT and allosteric inhibition.";
RL PLoS Biol. 8:E1000416-E1000416(2010).
CC -!- FUNCTION: Promotes dimerization of NF-kappa-B subunits and
CC regulates NF-kappa-B transcription factor activity (By
CC similarity). Plays a role in the regulation of the growth of actin
CC filaments. Inhibits the activity of the F-actin-capping protein
CC complex formed by the CAPZA1 and CAPZB heterodimer. Promotes
CC growth of cardiomyocytes, but not cardiomyocyte proliferation.
CC Promotes cardiac muscle hypertrophy.
CC -!- SUBUNIT: Interacts with RELA (By similarity). Interacts with the
CC heterodimer formed by CAPZA1 and CAPZB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Nucleus (By
CC similarity). Cytoplasm, perinuclear region (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: Up-regulated in heart left ventricle of patients with
CC severe coronary artery disease and history of myocardial ischemia.
CC Up-regulated in heart left ventricle of patients with dilated
CC cardiomyopathy.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene
CC which also produces the MPD6 protein from a non-overlapping
CC reading frame. MPD6 belongs to a group of cryptic antigens without
CC conventional genomic structure. It is encoded by a cryptic open
CC reading frame located in the 3'-untranslated region of MTPN.
CC -!- SIMILARITY: Belongs to the myotrophin family.
CC -!- SIMILARITY: Contains 3 ANK repeats.
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; AC015987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028093; AAH28093.1; -; mRNA.
DR RefSeq; NP_665807.1; NM_145808.3.
DR UniGene; Hs.602015; -.
DR PDB; 3AAA; X-ray; 2.20 A; C=1-118.
DR PDBsum; 3AAA; -.
DR ProteinModelPortal; P58546; -.
DR SMR; P58546; 2-118.
DR DIP; DIP-50234N; -.
DR IntAct; P58546; 3.
DR PhosphoSite; P58546; -.
DR DMDM; 20138912; -.
DR OGP; P58546; -.
DR PaxDb; P58546; -.
DR PeptideAtlas; P58546; -.
DR PRIDE; P58546; -.
DR DNASU; 136319; -.
DR Ensembl; ENST00000393085; ENSP00000376800; ENSG00000105887.
DR GeneID; 136319; -.
DR KEGG; hsa:136319; -.
DR UCSC; uc003vte.4; human.
DR CTD; 136319; -.
DR GeneCards; GC07M135613; -.
DR HGNC; HGNC:15667; MTPN.
DR HPA; HPA019735; -.
DR MIM; 606484; gene.
DR neXtProt; NX_P58546; -.
DR PharmGKB; PA31271; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000276399; -.
DR HOVERGEN; HBG019067; -.
DR InParanoid; P58546; -.
DR OMA; MSDKEFM; -.
DR OrthoDB; EOG7SBNQP; -.
DR PhylomeDB; P58546; -.
DR ChiTaRS; MTPN; human.
DR EvolutionaryTrace; P58546; -.
DR GeneWiki; MTPN; -.
DR GenomeRNAi; 136319; -.
DR NextBio; 83582; -.
DR PRO; PR:P58546; -.
DR ArrayExpress; P58546; -.
DR Bgee; P58546; -.
DR CleanEx; HS_MTPN; -.
DR Genevestigator; P58546; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
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:0006584; P:catecholamine metabolic process; IEA:Ensembl.
DR GO; GO:0016049; P:cell growth; IDA:UniProtKB.
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: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; IPR020683; Ankyrin_rpt-contain_dom.
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; Complete proteome; Cytoplasm;
KW Nucleus; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 118 Myotrophin.
FT /FTId=PRO_0000067031.
FT REPEAT 2 30 ANK 1.
FT REPEAT 34 66 ANK 2.
FT REPEAT 67 99 ANK 3.
FT MOD_RES 2 2 N-acetylcysteine.
FT MOD_RES 4 4 N6-acetyllysine.
FT MOD_RES 11 11 N6-acetyllysine.
FT MOD_RES 24 24 N6-acetyllysine.
FT HELIX 3 11
FT HELIX 15 23
FT HELIX 38 44
FT HELIX 48 55
FT TURN 56 58
FT HELIX 71 78
FT HELIX 81 89
FT HELIX 104 107
FT HELIX 111 117
SQ SEQUENCE 118 AA; 12895 MW; 9097FFDF61D329A2 CRC64;
MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD
INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ
//
ID MTPN_HUMAN Reviewed; 118 AA.
AC P58546;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 111.
DE RecName: Full=Myotrophin;
DE AltName: Full=Protein V-1;
GN Name=MTPN;
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], FUNCTION, INDUCTION, AND TISSUE
RP 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, IDENTIFICATION IN AN ACTIN CAPPING COMPLEX, AND INTERACTION
RP WITH WITH 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
RT how capping protein binds to the filament barbed end.";
RL J. Biol. Chem. 281:31021-31030(2006).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2; LYS-4; LYS-11 AND LYS-24,
RP MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CAPZA1 AND
RP CAPZB, AND 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
RT and allosteric inhibition.";
RL PLoS Biol. 8:E1000416-E1000416(2010).
CC -!- FUNCTION: Promotes dimerization of NF-kappa-B subunits and
CC regulates NF-kappa-B transcription factor activity (By
CC similarity). Plays a role in the regulation of the growth of actin
CC filaments. Inhibits the activity of the F-actin-capping protein
CC complex formed by the CAPZA1 and CAPZB heterodimer. Promotes
CC growth of cardiomyocytes, but not cardiomyocyte proliferation.
CC Promotes cardiac muscle hypertrophy.
CC -!- SUBUNIT: Interacts with RELA (By similarity). Interacts with the
CC heterodimer formed by CAPZA1 and CAPZB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Nucleus (By
CC similarity). Cytoplasm, perinuclear region (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: Up-regulated in heart left ventricle of patients with
CC severe coronary artery disease and history of myocardial ischemia.
CC Up-regulated in heart left ventricle of patients with dilated
CC cardiomyopathy.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene
CC which also produces the MPD6 protein from a non-overlapping
CC reading frame. MPD6 belongs to a group of cryptic antigens without
CC conventional genomic structure. It is encoded by a cryptic open
CC reading frame located in the 3'-untranslated region of MTPN.
CC -!- SIMILARITY: Belongs to the myotrophin family.
CC -!- SIMILARITY: Contains 3 ANK repeats.
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; AC015987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028093; AAH28093.1; -; mRNA.
DR RefSeq; NP_665807.1; NM_145808.3.
DR UniGene; Hs.602015; -.
DR PDB; 3AAA; X-ray; 2.20 A; C=1-118.
DR PDBsum; 3AAA; -.
DR ProteinModelPortal; P58546; -.
DR SMR; P58546; 2-118.
DR DIP; DIP-50234N; -.
DR IntAct; P58546; 3.
DR PhosphoSite; P58546; -.
DR DMDM; 20138912; -.
DR OGP; P58546; -.
DR PaxDb; P58546; -.
DR PeptideAtlas; P58546; -.
DR PRIDE; P58546; -.
DR DNASU; 136319; -.
DR Ensembl; ENST00000393085; ENSP00000376800; ENSG00000105887.
DR GeneID; 136319; -.
DR KEGG; hsa:136319; -.
DR UCSC; uc003vte.4; human.
DR CTD; 136319; -.
DR GeneCards; GC07M135613; -.
DR HGNC; HGNC:15667; MTPN.
DR HPA; HPA019735; -.
DR MIM; 606484; gene.
DR neXtProt; NX_P58546; -.
DR PharmGKB; PA31271; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000276399; -.
DR HOVERGEN; HBG019067; -.
DR InParanoid; P58546; -.
DR OMA; MSDKEFM; -.
DR OrthoDB; EOG7SBNQP; -.
DR PhylomeDB; P58546; -.
DR ChiTaRS; MTPN; human.
DR EvolutionaryTrace; P58546; -.
DR GeneWiki; MTPN; -.
DR GenomeRNAi; 136319; -.
DR NextBio; 83582; -.
DR PRO; PR:P58546; -.
DR ArrayExpress; P58546; -.
DR Bgee; P58546; -.
DR CleanEx; HS_MTPN; -.
DR Genevestigator; P58546; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
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:0006584; P:catecholamine metabolic process; IEA:Ensembl.
DR GO; GO:0016049; P:cell growth; IDA:UniProtKB.
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: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; IPR020683; Ankyrin_rpt-contain_dom.
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; Complete proteome; Cytoplasm;
KW Nucleus; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 118 Myotrophin.
FT /FTId=PRO_0000067031.
FT REPEAT 2 30 ANK 1.
FT REPEAT 34 66 ANK 2.
FT REPEAT 67 99 ANK 3.
FT MOD_RES 2 2 N-acetylcysteine.
FT MOD_RES 4 4 N6-acetyllysine.
FT MOD_RES 11 11 N6-acetyllysine.
FT MOD_RES 24 24 N6-acetyllysine.
FT HELIX 3 11
FT HELIX 15 23
FT HELIX 38 44
FT HELIX 48 55
FT TURN 56 58
FT HELIX 71 78
FT HELIX 81 89
FT HELIX 104 107
FT HELIX 111 117
SQ SEQUENCE 118 AA; 12895 MW; 9097FFDF61D329A2 CRC64;
MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD
INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ
//
MIM
606484
*RECORD*
*FIELD* NO
606484
*FIELD* TI
*606484 MYOTROPHIN; MTPN
;;V-1
*FIELD* TX
CLONING
Myotrophin, a 12-kD protein, was originally isolated by Sen et al.
read more(1990) from the hypertrophied ventricles of spontaneously hypertensive
rats and later by Sil et al. (1993) from dilated cardiomyopathic human
hearts. Mukherjee et al. (1993) found that myotrophin increases the
transcript levels of protooncogenes as well as the transcript levels of
beta-myosin heavy chain (160760) and ANF (108780), markers for cardiac
hypertrophy.
Taoka et al. (1992) characterized Mtpn purified from rat cerebellum. The
117-amino acid protein contained an acetylated N terminus and 2.5
internal 33-amino acid ankyrin repeats. Sivasubramanian et al. (1996)
identified a second half-ankyrin repeat in rat Mtpn. Northern blot
analysis detected up to 7 transcripts between 0.4 and 4.3 kb expressed
in all rat tissues examined. Highest levels were detected in brain, and
lowest levels in skeletal muscle. By 3-dimensional alignment,
Knuefermann et al. (2002) determined that mammalian myotrophin resembles
a truncated I-kappa-B-alpha (NFKBIA; 164008) without the signal response
domain and PEST sequence.
See 611050 for information on MPD6, a tumor antigen encoded by a cryptic
ORF in the 3-prime UTR of MTPN mRNA.
GENE FUNCTION
By gel shift assays, Sivasubramanian et al. (1996) determined that
recombinant rat myotrophin interacted with p50 NFKB1 (164011)-p65 RELA
(164014) complexes and formed a ternary protein-DNA complex. Myotrophin
antibodies inhibited formation of the complexes, and p50 and p65
antibodies supershifted the complexes. Knuefermann et al. (2002)
determined that endogenous HeLa cell MTPN is predominantly cytoplasmic
and translocates to the nucleus during sustained NFKB activation. They
presented evidence that recombinant mammalian myotrophin can promote the
formation of transcriptionally repressive p50-p50 homodimers from
monomeric p50 proteins and can convert the preformed active p50-p65
heterodimers to the p50-p50 and p65-p65 homodimers. Overexpression of
myotrophin significantly repressed NFKB-driven transcription of a
reporter plasmid. Hiwatashi et al. (2002) found that, in rat adrenal
glands, Mtpn was more highly expressed in noradrenergic chromaffin cells
than in adrenergic chromaffin cells that preferentially express the
glucocorticoid receptor 138040. In cultured bovine adrenal medullary
cells, a synthetic glucocorticoid inhibited expression of Mtpn, and the
inhibition was reversed by a glucocorticoid receptor antagonist.
Yamakuni et al. (2002) found that transfected rat pheochromocytoma cells
overexpressing rat Mtpn showed enhanced K+-induced dopamine secretion
that was associated with elevated intracellular Ca(2+) levels and
increased dense-cored vesicle number.
Poy et al. (2004) showed that Mtpn is a target of the microRNA miR375
(611173). Inhibition of Mtpn by small interfering (si) RNA mimicked the
effects of miR375 on glucose-stimulated insulin secretion and
exocytosis, in which overexpression of miR375 suppressed glucose-induced
insulin secretion and inhibition of endogenous miR375 function enhanced
insulin secretion. Repression of Mtpn was mediated by a single miRNA375
target site in the 3-prime untranslated region of the Mtpn gene.
MAPPING
By fluorescence in situ hybridization, Mitra et al. (2001) mapped the
MTPN gene to chromosome 7q33-q35.
*FIELD* RF
1. Hiwatashi, Y.; Kurahashi, Y.; Hatada, R.; Ueno, S.; Honma, T.;
Yanagihara, N.; Yanase, H.; Iwanaga, T.; Ohizumi, Y.; Yamakuni, T.
: Glucocorticoid inhibits expression of V-1, a catecholamine biosynthesis
regulatory protein, in cultured adrenal medullary cells. FEBS Lett. 528:
166-170, 2002.
2. Knuefermann, P.; Chen, P.; Misra, A.; Shi, S. P.; Abdellatif, M.;
Sivasubramanian, N.: Myotrophin/V-1, a protein up-regulated in the
failing human heart and in postnatal cerebellum, converts NFkappa
B p50-p65 heterodimers to p50-p50 and p65-p65 homodimers. J. Biol.
Chem. 277: 23888-28897, 2002.
3. Mitra, S.; Timur, A. A.; Gupta, S.; Wang, Q.; Sen, S.: Assignment
of myotrophin to human chromosome band 7q33-q35 by in situ hybridization. Cytogenet.
Cell Genet. 93: 151-152, 2001.
4. Mukherjee, D. P.; McTiernan, C. F.; Sen, S.: Myotrophin induces
early response genes and enhances cardiac gene expression. Hypertension 21:
142-148, 1993.
5. Poy, M. N.; Eliasson, L.; Krutzfeldt, J.; Kuwajima, S.; Ma, X.;
MacDonald, P. E.; Pfeffer, S.; Tuschi, T.; Rajewsky, N.; Rorsman,
P.; Stoffel, M.: A pancreatic islet-specific microRNA regulates insulin
secretion. Nature 432: 226-230, 2004.
6. Sen, S.; Kundu, G.; Mekhail, N.; Castel, J.; Misono, K.; Healy,
B.: Myotrophin: purification of a novel peptide from spontaneously
hypertensive rat heart that influences myocardial growth. J. Biol.
Chem. 265: 16635-16643, 1990.
7. Sil, P.; Misono, K.; Sen, S.: Myotrophin in human cardiomyopathic
heart. Circ. Res. 73: 98-108, 1993.
8. Sivasubramanian, N.; Adhikary, G.; Sil, P. C.; Sen, S.: Cardiac
myotrophin exhibits rel/NF-kappa B interacting activity in vitro. J.
Biol. Chem. 271: 2812-2816, 1996.
9. Taoka, M.; Yamakuni, T.; Song, S. Y.; Yamakawa, Y.; Seta, K.; Okuyama,
T.; Isobe, T.: A rat cerebellar protein containing the cdc10/SWI6
motif. Europ. J. Biochem. 207: 615-620, 1992.
10. Yamakuni, T.; Yamamoto, T.; Ishida, Y.; Yamamoto, H.; Song, S.
Y.; Adachi, E.; Hiwatashi, Y.; Ohizumi, Y.: V-1, a catecholamine
biosynthesis regulatory protein, positively controls catecholamine
secretion in PC12D cells. FEBS Lett. 530: 94-98, 2002.
*FIELD* CN
Ada Hamosh - updated: 6/27/2007
Patricia A. Hartz - updated: 8/8/2003
*FIELD* CD
Carol A. Bocchini: 11/24/2001
*FIELD* ED
alopez: 07/06/2007
terry: 6/27/2007
mgross: 5/22/2007
cwells: 8/8/2003
carol: 5/1/2002
terry: 3/5/2002
cwells: 11/26/2001
carol: 11/24/2001
*RECORD*
*FIELD* NO
606484
*FIELD* TI
*606484 MYOTROPHIN; MTPN
;;V-1
*FIELD* TX
CLONING
Myotrophin, a 12-kD protein, was originally isolated by Sen et al.
read more(1990) from the hypertrophied ventricles of spontaneously hypertensive
rats and later by Sil et al. (1993) from dilated cardiomyopathic human
hearts. Mukherjee et al. (1993) found that myotrophin increases the
transcript levels of protooncogenes as well as the transcript levels of
beta-myosin heavy chain (160760) and ANF (108780), markers for cardiac
hypertrophy.
Taoka et al. (1992) characterized Mtpn purified from rat cerebellum. The
117-amino acid protein contained an acetylated N terminus and 2.5
internal 33-amino acid ankyrin repeats. Sivasubramanian et al. (1996)
identified a second half-ankyrin repeat in rat Mtpn. Northern blot
analysis detected up to 7 transcripts between 0.4 and 4.3 kb expressed
in all rat tissues examined. Highest levels were detected in brain, and
lowest levels in skeletal muscle. By 3-dimensional alignment,
Knuefermann et al. (2002) determined that mammalian myotrophin resembles
a truncated I-kappa-B-alpha (NFKBIA; 164008) without the signal response
domain and PEST sequence.
See 611050 for information on MPD6, a tumor antigen encoded by a cryptic
ORF in the 3-prime UTR of MTPN mRNA.
GENE FUNCTION
By gel shift assays, Sivasubramanian et al. (1996) determined that
recombinant rat myotrophin interacted with p50 NFKB1 (164011)-p65 RELA
(164014) complexes and formed a ternary protein-DNA complex. Myotrophin
antibodies inhibited formation of the complexes, and p50 and p65
antibodies supershifted the complexes. Knuefermann et al. (2002)
determined that endogenous HeLa cell MTPN is predominantly cytoplasmic
and translocates to the nucleus during sustained NFKB activation. They
presented evidence that recombinant mammalian myotrophin can promote the
formation of transcriptionally repressive p50-p50 homodimers from
monomeric p50 proteins and can convert the preformed active p50-p65
heterodimers to the p50-p50 and p65-p65 homodimers. Overexpression of
myotrophin significantly repressed NFKB-driven transcription of a
reporter plasmid. Hiwatashi et al. (2002) found that, in rat adrenal
glands, Mtpn was more highly expressed in noradrenergic chromaffin cells
than in adrenergic chromaffin cells that preferentially express the
glucocorticoid receptor 138040. In cultured bovine adrenal medullary
cells, a synthetic glucocorticoid inhibited expression of Mtpn, and the
inhibition was reversed by a glucocorticoid receptor antagonist.
Yamakuni et al. (2002) found that transfected rat pheochromocytoma cells
overexpressing rat Mtpn showed enhanced K+-induced dopamine secretion
that was associated with elevated intracellular Ca(2+) levels and
increased dense-cored vesicle number.
Poy et al. (2004) showed that Mtpn is a target of the microRNA miR375
(611173). Inhibition of Mtpn by small interfering (si) RNA mimicked the
effects of miR375 on glucose-stimulated insulin secretion and
exocytosis, in which overexpression of miR375 suppressed glucose-induced
insulin secretion and inhibition of endogenous miR375 function enhanced
insulin secretion. Repression of Mtpn was mediated by a single miRNA375
target site in the 3-prime untranslated region of the Mtpn gene.
MAPPING
By fluorescence in situ hybridization, Mitra et al. (2001) mapped the
MTPN gene to chromosome 7q33-q35.
*FIELD* RF
1. Hiwatashi, Y.; Kurahashi, Y.; Hatada, R.; Ueno, S.; Honma, T.;
Yanagihara, N.; Yanase, H.; Iwanaga, T.; Ohizumi, Y.; Yamakuni, T.
: Glucocorticoid inhibits expression of V-1, a catecholamine biosynthesis
regulatory protein, in cultured adrenal medullary cells. FEBS Lett. 528:
166-170, 2002.
2. Knuefermann, P.; Chen, P.; Misra, A.; Shi, S. P.; Abdellatif, M.;
Sivasubramanian, N.: Myotrophin/V-1, a protein up-regulated in the
failing human heart and in postnatal cerebellum, converts NFkappa
B p50-p65 heterodimers to p50-p50 and p65-p65 homodimers. J. Biol.
Chem. 277: 23888-28897, 2002.
3. Mitra, S.; Timur, A. A.; Gupta, S.; Wang, Q.; Sen, S.: Assignment
of myotrophin to human chromosome band 7q33-q35 by in situ hybridization. Cytogenet.
Cell Genet. 93: 151-152, 2001.
4. Mukherjee, D. P.; McTiernan, C. F.; Sen, S.: Myotrophin induces
early response genes and enhances cardiac gene expression. Hypertension 21:
142-148, 1993.
5. Poy, M. N.; Eliasson, L.; Krutzfeldt, J.; Kuwajima, S.; Ma, X.;
MacDonald, P. E.; Pfeffer, S.; Tuschi, T.; Rajewsky, N.; Rorsman,
P.; Stoffel, M.: A pancreatic islet-specific microRNA regulates insulin
secretion. Nature 432: 226-230, 2004.
6. Sen, S.; Kundu, G.; Mekhail, N.; Castel, J.; Misono, K.; Healy,
B.: Myotrophin: purification of a novel peptide from spontaneously
hypertensive rat heart that influences myocardial growth. J. Biol.
Chem. 265: 16635-16643, 1990.
7. Sil, P.; Misono, K.; Sen, S.: Myotrophin in human cardiomyopathic
heart. Circ. Res. 73: 98-108, 1993.
8. Sivasubramanian, N.; Adhikary, G.; Sil, P. C.; Sen, S.: Cardiac
myotrophin exhibits rel/NF-kappa B interacting activity in vitro. J.
Biol. Chem. 271: 2812-2816, 1996.
9. Taoka, M.; Yamakuni, T.; Song, S. Y.; Yamakawa, Y.; Seta, K.; Okuyama,
T.; Isobe, T.: A rat cerebellar protein containing the cdc10/SWI6
motif. Europ. J. Biochem. 207: 615-620, 1992.
10. Yamakuni, T.; Yamamoto, T.; Ishida, Y.; Yamamoto, H.; Song, S.
Y.; Adachi, E.; Hiwatashi, Y.; Ohizumi, Y.: V-1, a catecholamine
biosynthesis regulatory protein, positively controls catecholamine
secretion in PC12D cells. FEBS Lett. 530: 94-98, 2002.
*FIELD* CN
Ada Hamosh - updated: 6/27/2007
Patricia A. Hartz - updated: 8/8/2003
*FIELD* CD
Carol A. Bocchini: 11/24/2001
*FIELD* ED
alopez: 07/06/2007
terry: 6/27/2007
mgross: 5/22/2007
cwells: 8/8/2003
carol: 5/1/2002
terry: 3/5/2002
cwells: 11/26/2001
carol: 11/24/2001