MTPN_RAT
ID MTPN_RAT Reviewed; 118 AA.
AC P62775; P80144; Q58HB3; Q9DCN8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Myotrophin;
DE AltName: Full=Granule cell differentiation protein;
DE AltName: Full=Protein V-1;
GN Name=Mtpn; Synonyms=Gcdp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8144589; DOI=10.1016/s0021-9258(17)36974-0;
RA Taoka M., Isobe T., Okuyama T., Watanabe M., Kondo H., Yamakawa Y.,
RA Ozawa F., Hishinuma F., Kubota M., Minegishi A., Song S.-Y., Yamakuni T.;
RT "Murine cerebellar neurons express a novel gene encoding a protein related
RT to cell cycle control and cell fate determination proteins.";
RL J. Biol. Chem. 269:9946-9951(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8576259; DOI=10.1074/jbc.271.5.2812;
RA Sivasubramanian N.C., Adhikary G., Sil P.C., Sen S.;
RT "Cardiac myotrophin exhibits rel/NF-kappa B interacting activity in
RT vitro.";
RL J. Biol. Chem. 271:2812-2816(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=15946807; DOI=10.1016/j.gene.2005.03.045;
RA Adhikary G., Gupta S., Sil P., Saad Y., Sen S.;
RT "Characterization and functional significance of myotrophin: a gene with
RT multiple transcripts.";
RL Gene 353:31-40(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [5]
RP PROTEIN SEQUENCE OF 2-118, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT CYS-2.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=1633812; DOI=10.1111/j.1432-1033.1992.tb17088.x;
RA Taoka M., Yamakuni T., Song S.-Y., Yamakawa Y., Seta K., Okuyama T.,
RA Isobe T.;
RT "A rat cerebellar protein containing the cdc10/SW16 motif.";
RL Eur. J. Biochem. 207:615-620(1992).
RN [6]
RP PROTEIN SEQUENCE OF 37-57 AND 67-85, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17041682;
RA Knuefermann P., Shi S.P., Chen P., Sakata Y., Baumgarten G.,
RA Sivasubramanian N.;
RT "Myotrophin/V-1 does not act as an extracellular signal to induce myocyte
RT hypertrophy.";
RL Tex. Heart Inst. J. 33:281-289(2006).
RN [8]
RP SUBCELLULAR LOCATION, INTERACTION WITH RELA, MUTAGENESIS OF GLU-33, AND
RP FUNCTION.
RX PubMed=18693253; DOI=10.1074/jbc.m801210200;
RA Das B., Gupta S., Vasanji A., Xu Z., Misra S., Sen S.;
RT "Nuclear co-translocation of myotrophin and p65 stimulates myocyte growth.
RT Regulation by myotrophin hairpin loops.";
RL J. Biol. Chem. 283:27947-27956(2008).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=9194197; DOI=10.1002/pro.5560060625;
RA Yang Y., Rao N.S., Walker E., Sen S., Qin J.;
RT "Nuclear magnetic resonance assignment and secondary structure of an
RT ankyrin-like repeat-bearing protein: myotrophin.";
RL Protein Sci. 6:1347-1351(1997).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=9634699; DOI=10.1016/s0969-2126(98)00063-x;
RA Yang Y., Nanduri S., Sen S., Qin J.;
RT "The structural basis of ankyrin-like repeat function as revealed by the
RT solution structure of myotrophin.";
RL Structure 6:619-626(1998).
CC -!- FUNCTION: Plays a role in the regulation of the growth of actin
CC filaments. Inhibits the activity of the F-actin-capping protein complex
CC formed by the CAPZA1 and CAPZB heterodimer (By similarity). Promotes
CC dimerization of NF-kappa-B subunits and regulates NF-kappa-B
CC transcription factor activity. Promotes growth of cardiomyocytes, but
CC not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy.
CC {ECO:0000250, ECO:0000269|PubMed:17041682,
CC ECO:0000269|PubMed:18693253}.
CC -!- SUBUNIT: Interacts with the heterodimer formed by CAPZA1 and CAPZB (By
CC similarity). Interacts with RELA. {ECO:0000250,
CC ECO:0000269|PubMed:18693253}.
CC -!- INTERACTION:
CC P62775; Q5XI32: Capzb; NbExp=3; IntAct=EBI-2128047, EBI-2128068;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, perinuclear
CC region.
CC -!- DEVELOPMENTAL STAGE: At the completion of differentiation and migration
CC of granular cells and at the initiation of the formation of synapses in
CC cerebellar neurons.
CC -!- SIMILARITY: Belongs to the myotrophin family. {ECO:0000305}.
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DR EMBL; D26179; BAA05167.1; -; mRNA.
DR EMBL; U21661; AAC52498.1; -; mRNA.
DR EMBL; AY951952; AAX54865.1; -; mRNA.
DR EMBL; BC088136; AAH88136.1; -; mRNA.
DR PIR; A54412; A54412.
DR RefSeq; NP_077350.1; NM_024374.4.
DR PDB; 1MYO; NMR; -; A=1-118.
DR PDB; 2MYO; NMR; -; A=1-118.
DR PDBsum; 1MYO; -.
DR PDBsum; 2MYO; -.
DR AlphaFoldDB; P62775; -.
DR BMRB; P62775; -.
DR SMR; P62775; -.
DR IntAct; P62775; 1.
DR STRING; 10116.ENSRNOP00000015808; -.
DR iPTMnet; P62775; -.
DR PhosphoSitePlus; P62775; -.
DR jPOST; P62775; -.
DR PaxDb; P62775; -.
DR PRIDE; P62775; -.
DR Ensembl; ENSRNOT00000103488; ENSRNOP00000082083; ENSRNOG00000011857.
DR GeneID; 79215; -.
DR KEGG; rno:79215; -.
DR UCSC; RGD:619806; rat.
DR CTD; 136319; -.
DR RGD; 619806; Mtpn.
DR eggNOG; KOG4214; Eukaryota.
DR GeneTree; ENSGT00430000031071; -.
DR HOGENOM; CLU_000134_45_7_1; -.
DR InParanoid; P62775; -.
DR OMA; TALIDCT; -.
DR OrthoDB; 1435166at2759; -.
DR PhylomeDB; P62775; -.
DR TreeFam; TF327387; -.
DR EvolutionaryTrace; P62775; -.
DR PRO; PR:P62775; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000011857; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; P62775; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0008290; C:F-actin capping protein complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0006584; P:catecholamine metabolic process; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IEP:RGD.
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; IDA:UniProtKB.
DR GO; GO:0010557; P:positive regulation of macromolecule biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IDA:UniProtKB.
DR GO; GO:2000812; P:regulation of barbed-end actin filament capping; ISS:UniProtKB.
DR GO; GO:0008361; P:regulation of cell size; ISO:RGD.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEP:RGD.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEP:RGD.
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;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1633812"
FT CHAIN 2..118
FT /note="Myotrophin"
FT /id="PRO_0000067033"
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:0000269|PubMed:1633812"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58546"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58546"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58546"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P58546"
FT MUTAGEN 33
FT /note="E->A: Reduced interaction with RELA. Reduced
FT translocation to the nucleus. Reduced activation of NF-
FT kappa-B transcription factor activity."
FT /evidence="ECO:0000269|PubMed:18693253"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:1MYO"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:1MYO"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1MYO"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1MYO"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:1MYO"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1MYO"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:1MYO"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1MYO"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1MYO"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:1MYO"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:1MYO"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1MYO"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:1MYO"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1MYO"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:1MYO"
SQ SEQUENCE 118 AA; 12861 MW; 9097FFDF61DB8BA2 CRC64;
MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD
INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTALEATDN QAIKALLQ
