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