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MTPN_CANLF
ID   MTPN_CANLF              Reviewed;         118 AA.
AC   Q863Z4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Myotrophin;
GN   Name=MTPN;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Mishra S., Rastogi S., Sabbah H.N., Gupta R.C.;
RT   "Cloning and sequencing of cardiac myotrophin gene.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes dimerization of NF-kappa-B subunits and regulates
CC       NF-kappa-B transcription factor activity. Promotes growth of
CC       cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac
CC       muscle hypertrophy. Plays a role in the regulation of the growth of
CC       actin filaments. Inhibits the activity of the F-actin-capping protein
CC       complex formed by the CAPZA1 and CAPZB heterodimer (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RELA. Interacts with the heterodimer formed by
CC       CAPZA1 and CAPZB (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Cytoplasm, perinuclear region {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the myotrophin family. {ECO:0000305}.
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DR   EMBL; AY266681; AAP23872.1; -; mRNA.
DR   RefSeq; NP_001002989.1; NM_001002989.1.
DR   AlphaFoldDB; Q863Z4; -.
DR   BMRB; Q863Z4; -.
DR   SMR; Q863Z4; -.
DR   STRING; 9612.ENSCAFP00000039244; -.
DR   PaxDb; Q863Z4; -.
DR   PRIDE; Q863Z4; -.
DR   Ensembl; ENSCAFT00030018938; ENSCAFP00030016529; ENSCAFG00030010231.
DR   Ensembl; ENSCAFT00040029969; ENSCAFP00040026036; ENSCAFG00040016241.
DR   GeneID; 403487; -.
DR   KEGG; cfa:403487; -.
DR   CTD; 136319; -.
DR   eggNOG; KOG4214; Eukaryota.
DR   HOGENOM; CLU_000134_45_7_1; -.
DR   InParanoid; Q863Z4; -.
DR   OMA; TALIDCT; -.
DR   OrthoDB; 1435166at2759; -.
DR   TreeFam; TF327387; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Bgee; ENSCAFG00000028992; Expressed in prefrontal cortex and 45 other tissues.
DR   GO; GO:0030424; C:axon; ISS:AgBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS: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; ISS:UniProtKB.
DR   GO; GO:0008361; P:regulation of cell size; 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   3: Inferred from homology;
KW   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_0000067030"
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: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"
SQ   SEQUENCE   118 AA;  12895 MW;  9097FFDF61D329A2 CRC64;
     MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD
     INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ
 
 
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