MTPN_MOUSE
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 03-AUG-2022, entry version 134.
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, Pancreas,
RC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 iPTMnet; P62774; -.
DR PhosphoSitePlus; P62774; -.
DR SwissPalm; P62774; -.
DR CPTAC; non-CPTAC-3730; -.
DR EPD; P62774; -.
DR jPOST; P62774; -.
DR MaxQB; P62774; -.
DR PaxDb; P62774; -.
DR PeptideAtlas; P62774; -.
DR PRIDE; P62774; -.
DR ProteomicsDB; 290216; -.
DR Antibodypedia; 18167; 109 antibodies from 25 providers.
DR DNASU; 14489; -.
DR Ensembl; ENSMUST00000031866; ENSMUSP00000031866; ENSMUSG00000029840.
DR GeneID; 14489; -.
DR KEGG; mmu:14489; -.
DR UCSC; uc009bit.2; mouse.
DR CTD; 136319; -.
DR MGI; MGI:99445; Mtpn.
DR VEuPathDB; HostDB:ENSMUSG00000029840; -.
DR eggNOG; KOG4214; Eukaryota.
DR GeneTree; ENSGT00430000031071; -.
DR InParanoid; P62774; -.
DR OMA; TALIDCT; -.
DR OrthoDB; 1435166at2759; -.
DR PhylomeDB; P62774; -.
DR TreeFam; TF327387; -.
DR BioGRID-ORCS; 14489; 1 hit in 73 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 268 other tissues.
DR ExpressionAtlas; P62774; baseline and differential.
DR Genevisible; P62774; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; -; 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; 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
