ID   MTPN_MOUSE              Reviewed;         118 AA.
AC   P62774; P80144; Q543M6; Q9DCN8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Myotrophin;
DE   AltName: Full=Granule cell differentiation protein;
DE   AltName: Full=Protein V-1;
GN   Name=Mtpn; Synonyms=Gcdp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7607560; DOI=10.1016/0378-1119(95)00131-o;
RA   Pennica D., Shaw K.J., Luoh S., Wood W.I.;
RT   "Isolation of cDNA clones encoding the mouse protein V-1.";
RL   Gene 158:305-306(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J;
RC   TISSUE=Bone marrow, Kidney, Spinal ganglion, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2 AND LYS-4, CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [6]
RP   STRUCTURE BY NMR IN COMPLEX WITH CAPZA1 AND CAPZB, AND FUNCTION.
RX   PubMed=20538588; DOI=10.1074/jbc.m110.135848;
RA   Zwolak A., Fujiwara I., Hammer J.A. III, Tjandra N.;
RT   "Structural basis for capping protein sequestration by myotrophin (V-1).";
RL   J. Biol. Chem. 285:25767-25781(2010).
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 (By similarity). Plays a role in the regulation of
CC       the growth of actin filaments. Inhibits the activity of the F-actin-
CC       capping protein complex formed by the CAPZA1 and CAPZB heterodimer.
CC       {ECO:0000250, ECO:0000269|PubMed:20538588}.
CC   -!- SUBUNIT: Interacts with RELA (By similarity). Interacts with the
CC       heterodimer formed by CAPZA1 and CAPZB. {ECO:0000250,
CC       ECO:0000269|PubMed:20538588}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250}.
CC       Cytoplasm, perinuclear region {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the myotrophin family. {ECO:0000305}.
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DR   EMBL; U20290; AAA86719.1; -; mRNA.
DR   EMBL; AK002620; BAB22235.1; -; mRNA.
DR   EMBL; AK028027; BAC25707.1; -; mRNA.
DR   EMBL; AK049398; BAC33734.1; -; mRNA.
DR   EMBL; AK083888; BAC39050.1; -; mRNA.
DR   EMBL; AK132029; BAE20953.1; -; mRNA.
DR   EMBL; AK145755; BAE26630.1; -; mRNA.
DR   EMBL; AK146305; BAE27061.1; -; mRNA.
DR   EMBL; AK146473; BAE27198.1; -; mRNA.
DR   EMBL; AK150750; BAE29820.1; -; mRNA.
DR   EMBL; AK151106; BAE30116.1; -; mRNA.
DR   EMBL; AK151147; BAE30153.1; -; mRNA.
DR   EMBL; AK151485; BAE30438.1; -; mRNA.
DR   EMBL; AK151564; BAE30506.1; -; mRNA.
DR   EMBL; AK151640; BAE30570.1; -; mRNA.
DR   EMBL; AK151687; BAE30611.1; -; mRNA.
DR   EMBL; AK152272; BAE31088.1; -; mRNA.
DR   EMBL; BC043084; AAH43084.1; -; mRNA.
DR   EMBL; BC054811; AAH54811.1; -; mRNA.
DR   CCDS; CCDS20002.1; -.
DR   RefSeq; NP_032124.1; NM_008098.4.
DR   PDB; 2KXP; NMR; -; C=1-118.
DR   PDBsum; 2KXP; -.
DR   AlphaFoldDB; P62774; -.
DR   BMRB; P62774; -.
DR   SMR; P62774; -.
DR   BioGRID; 199860; 8.
DR   IntAct; P62774; 1.
DR   STRING; 10090.ENSMUSP00000031866; -.
DR   GlyGen; P62774; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62774; -.
DR   PhosphoSitePlus; P62774; -.
DR   SwissPalm; P62774; -.
DR   CPTAC; non-CPTAC-3730; -.
DR   EPD; P62774; -.
DR   jPOST; P62774; -.
DR   MaxQB; P62774; -.
DR   PaxDb; 10090-ENSMUSP00000031866; -.
DR   PeptideAtlas; P62774; -.
DR   ProteomicsDB; 290216; -.
DR   Pumba; P62774; -.
DR   Antibodypedia; 18167; 124 antibodies from 25 providers.
DR   DNASU; 14489; -.
DR   Ensembl; ENSMUST00000031866.9; ENSMUSP00000031866.6; ENSMUSG00000029840.9.
DR   GeneID; 14489; -.
DR   KEGG; mmu:14489; -.
DR   UCSC; uc009bit.2; mouse.
DR   AGR; MGI:99445; -.
DR   CTD; 136319; -.
DR   MGI; MGI:99445; Mtpn.
DR   VEuPathDB; HostDB:ENSMUSG00000029840; -.
DR   eggNOG; KOG4214; Eukaryota.
DR   GeneTree; ENSGT00430000031071; -.
DR   InParanoid; P62774; -.
DR   OMA; WAIKNGD; -.
DR   OrthoDB; 5475373at2759; -.
DR   PhylomeDB; P62774; -.
DR   TreeFam; TF327387; -.
DR   BioGRID-ORCS; 14489; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Mtpn; mouse.
DR   PRO; PR:P62774; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P62774; Protein.
DR   Bgee; ENSMUSG00000029840; Expressed in pigmented layer of retina and 272 other cell types or tissues.
DR   ExpressionAtlas; P62774; baseline and differential.
DR   GO; GO:0030424; C:axon; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
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: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; ISO:MGI.
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; PTHR24189; MYOTROPHIN; 1.
DR   PANTHER; PTHR24189:SF52; MYOTROPHIN; 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; P62774; MM.
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:0007744|PubMed:23806337"
FT   CHAIN           2..118
FT                   /note="Myotrophin"
FT                   /id="PRO_0000067032"
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:0007744|PubMed:23806337"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
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   CONFLICT        26
FT                   /note="E -> K (in Ref. 2; BAB22235)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..7
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   HELIX           9..12
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   HELIX           15..22
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   HELIX           40..45
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   HELIX           71..76
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   HELIX           82..88
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   STRAND          96..101
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   HELIX           102..106
FT                   /evidence="ECO:0007829|PDB:2KXP"
FT   HELIX           111..114
FT                   /evidence="ECO:0007829|PDB:2KXP"
SQ   SEQUENCE   118 AA;  12861 MW;  9097FFDF61DB8BA2 CRC64;
     MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD
     INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTALEATDN QAIKALLQ
//