P62774 (MTPN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myotrophin

Alternative name(s):
Granule cell differentiation protein
Protein V-1

Gene names

Name:	Mtpn
Synonyms:	Gcdp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	118 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy By similarity. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Ref.4
Subunit structure	Interacts with RELA By similarity. Interacts with the heterodimer formed by CAPZA1 and CAPZB.
Subcellular location	Cytoplasm Probable. Nucleus By similarity. Cytoplasm › perinuclear region By similarity.
Sequence similarities	Belongs to the myotrophin family. Contains 3 ANK repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	ANK repeat Repeat
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	catecholamine metabolic process Inferred from electronic annotation. Source: Compara cell growth Inferred from electronic annotation. Source: Compara cerebellar granule cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cardiac muscle hypertrophy Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of macromolecule biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein metabolic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of barbed-end actin filament capping Inferred from sequence or structural similarity. Source: UniProtKB skeletal muscle tissue regeneration Inferred from electronic annotation. Source: Compara striated muscle cell differentiation Inferred from electronic annotation. Source: Compara
Cellular_component	F-actin capping protein complex Inferred from electronic annotation. Source: Compara axon Inferred from electronic annotation. Source: Compara cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 118

117

Myotrophin

PRO_0000067032

Regions

Repeat

2 – 30

29

ANK 1

Repeat

34 – 66

33

ANK 2

Repeat

67 – 99

33

ANK 3

Amino acid modifications

Modified residue

2

1

N-acetylcysteine By similarity

Modified residue

4

1

N6-acetyllysine By similarity

Modified residue

11

1

N6-acetyllysine By similarity

Modified residue

24

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

26

1

E → K in BAB22235. Ref.2

Secondary structure

1

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118

Helix Strand Turn

Details...

Helix

3 – 7

5

Helix

9 – 12

4

Helix

15 – 22

8

Turn

23 – 25

3

Beta strand

32 – 35

4

Helix

40 – 45

6

Turn

47 – 49

3

Helix

53 – 56

4

Turn

60 – 62

3

Helix

71 – 76

6

Helix

82 – 88

7

Beta strand

96 – 101

6

Helix

102 – 106

5

Helix

111 – 114

4

Sequences

	Sequence		Length	Mass (Da)
	P62774 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9097FFDF61DB8BA2	FASTA	118	12,861
	10 20 30 40 50 60 MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD 70 80 90 100 110 INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTALEATDN QAIKALLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of cDNA clones encoding the mouse protein V-1." Pennica D., Shaw K.J., Luoh S., Wood W.I. Gene 158:305-306(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and DBA/2. Tissue: Bone marrow, Kidney, Spinal ganglion and Stomach.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	"Structural basis for capping protein sequestration by myotrophin (V-1)." Zwolak A., Fujiwara I., Hammer J.A. III, Tjandra N. J. Biol. Chem. 285:25767-25781(2010) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR IN COMPLEX WITH CAPZA1 AND CAPZB, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U20290 mRNA. Translation: AAA86719.1.
AK002620 mRNA. Translation: BAB22235.1.
AK028027 mRNA. Translation: BAC25707.1.
AK049398 mRNA. Translation: BAC33734.1.
AK083888 mRNA. Translation: BAC39050.1.
AK132029 mRNA. Translation: BAE20953.1.
AK145755 mRNA. Translation: BAE26630.1.
AK146305 mRNA. Translation: BAE27061.1.
AK146473 mRNA. Translation: BAE27198.1.
AK150750 mRNA. Translation: BAE29820.1.
AK151106 mRNA. Translation: BAE30116.1.
AK151147 mRNA. Translation: BAE30153.1.
AK151485 mRNA. Translation: BAE30438.1.
AK151564 mRNA. Translation: BAE30506.1.
AK151640 mRNA. Translation: BAE30570.1.
AK151687 mRNA. Translation: BAE30611.1.
AK152272 mRNA. Translation: BAE31088.1.
BC043084 mRNA. Translation: AAH43084.1.
BC054811 mRNA. Translation: AAH54811.1.

IPI

IPI00228583.

RefSeq

NP_032124.1. NM_008098.4.

UniGene

Mm.182746.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KXP	NMR	-	C	1-118	[»]

ProteinModelPortal

P62774.

SMR

P62774. Positions 1-118.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62774. 1 interaction.

PTM databases

PhosphoSite

P62774.

Proteomic databases

PaxDb

P62774.

PRIDE

P62774.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000031866; ENSMUSP00000031866; ENSMUSG00000029840.

GeneID

14489.

KEGG

mmu:14489.

UCSC

uc009bit.2. mouse.

Organism-specific databases

CTD

136319.

MGI

MGI:99445. Mtpn.

Phylogenomic databases

eggNOG

COG0666.

GeneTree

ENSGT00430000031071.

HOGENOM

HOG000276399.

HOVERGEN

HBG019067.

InParanoid

P62774.

OMA

MSDKEFM.

OrthoDB

EOG470TJP.

Gene expression databases

Bgee

P62774.

CleanEx

MM_MTPN.

Genevestigator

P62774.

GermOnline

ENSMUSG00000029840. Mus musculus.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]

Pfam

PF12796. Ank_2. 1 hit.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 2 hits.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MTPN. mouse.

NextBio

286160.

SOURCE

Search...

Entry information

Entry name

MTPN_MOUSE

Accession

Primary (citable) accession number: P62774
Secondary accession number(s): P80144, Q543M6, Q9DCN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program