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Protein

Metalloendopeptidase OMA1, mitochondrial

Gene

Oma1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. May also cleave UQCC3 under these conditions. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions.By similarity2 Publications

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi323 – 3231Zinc; catalyticPROSITE-ProRule annotation
Active sitei324 – 3241PROSITE-ProRule annotation
Metal bindingi327 – 3271Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi388 – 3881Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM48.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloendopeptidase OMA1, mitochondrial (EC:3.4.24.-)
Alternative name(s):
Overlapping with the m-AAA protease 1 homolog
Gene namesi
Name:Oma1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914263. Oma1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei192 – 21221HelicalSequence analysisAdd
BLAST
Transmembranei337 – 35721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

Mice develop normally with males and females being fertile. They however display transcriptional changes in genes of lipid and glucose metabolic pathways and substantial alterations in circulating blood parameters. Moreover, mice exhibit an increase in body weight due to increased adipose mass, hepatic steatosis, decreased energy expenditure and impaired thermogenenesis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7979MitochondrionSequence analysisAdd
BLAST
Chaini80 – 521442Metalloendopeptidase OMA1, mitochondrialPRO_0000302810Add
BLAST

Post-translational modificationi

In normal conditions, cleaved into an inactive 40 kDa form. Following CCCP treatment that induces loss of mitochondrial membrane potential, the 40 kDa form is reduced in favor of an active 60 kDa form (By similarity).By similarity

Proteomic databases

EPDiQ9D8H7.
MaxQBiQ9D8H7.
PaxDbiQ9D8H7.
PRIDEiQ9D8H7.

PTM databases

iPTMnetiQ9D8H7.
PhosphoSiteiQ9D8H7.

Expressioni

Gene expression databases

BgeeiQ9D8H7.
GenevisibleiQ9D8H7. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045269.

Structurei

3D structure databases

ProteinModelPortaliQ9D8H7.
SMRiQ9D8H7. Positions 278-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M48 family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2661. Eukaryota.
COG0501. LUCA.
GeneTreeiENSGT00390000007027.
HOGENOMiHOG000115266.
HOVERGENiHBG096685.
InParanoidiQ9D8H7.
OMAiFAIIVGR.
OrthoDBiEOG7Q8CNJ.
PhylomeDBiQ9D8H7.
TreeFamiTF329133.

Family and domain databases

InterProiIPR001915. Peptidase_M48.
[Graphical view]
PfamiPF01435. Peptidase_M48. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9D8H7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSLLYGLQST RINRFLSGVN NLANRRQWTP PASCPLAPKL RAVNAYWGLN
60 70 80 90 100
TVSHCHSVTL LPRNFLFCRT LNHKKSRCLS SAQSKELGVL TYRCTVRGDS
110 120 130 140 150
VLRQGARKVA GVPALAASCS PSCPAVIEAR SFRTSARVQA APVPLLLLIL
160 170 180 190 200
KPVQKLLAII VGRGIRKWWQ ALPPNKKELF KDSVRKNKWR LLLGLSAFGL
210 220 230 240 250
LFVVFYFTHL EVSPVTGRSK LLLVGKEHFR LLSDLEYEVW MEEFKNDLLP
260 270 280 290 300
ERDPRYLTVK EMVYHLTQCN RDVPGISETN WVVHVVDSPA VNAFVLPNGQ
310 320 330 340 350
VFIFTGLLNS VTDVHQLSFL LGHEIAHAVL GHAAEKASLV HLLDFLGMIF
360 370 380 390 400
LTMIWAICPR DSLAVLGQWI QSKLQEYMFD RPYSRTLEAE ADKVGLQLAA
410 420 430 440 450
KACADVRASS VFWQQMEFSE SLHGYPKLPE WLSTHPSHGN RAEYLDRLIP
460 470 480 490 500
QALKLREVCN CPPLSGPDPR LLFRLTVKRF LEDSEKEDLN ITVKKQKTDA
510 520
LPMQKQEQIP LTYVLEKRTA G
Length:521
Mass (Da):58,878
Last modified:June 1, 2001 - v1
Checksum:i80BCBFA70C9E2D5F
GO
Isoform 2 (identifier: Q9D8H7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     226-231: KEHFRL → ESWAP
     232-521: Missing.

Note: No experimental confirmation available.
Show »
Length:230
Mass (Da):25,541
Checksum:i080F483234D0A492
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371R → M in BAE22875 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei226 – 2316KEHFRL → ESWAP in isoform 2. 1 PublicationVSP_027959
Alternative sequencei232 – 521290Missing in isoform 2. 1 PublicationVSP_027960Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008020 mRNA. Translation: BAB25414.1.
AK076209 mRNA. Translation: BAC36255.1.
AK136208 mRNA. Translation: BAE22875.1.
AL772338 Genomic DNA. Translation: CAM25530.1.
BC016238 mRNA. Translation: AAH16238.1.
CCDSiCCDS18412.1. [Q9D8H7-1]
RefSeqiNP_080185.1. NM_025909.3. [Q9D8H7-1]
XP_006503362.1. XM_006503299.2. [Q9D8H7-1]
XP_006503363.1. XM_006503300.2. [Q9D8H7-1]
UniGeneiMm.30021.

Genome annotation databases

EnsembliENSMUST00000035780; ENSMUSP00000045269; ENSMUSG00000035069. [Q9D8H7-1]
GeneIDi67013.
KEGGimmu:67013.
UCSCiuc008txq.1. mouse. [Q9D8H7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008020 mRNA. Translation: BAB25414.1.
AK076209 mRNA. Translation: BAC36255.1.
AK136208 mRNA. Translation: BAE22875.1.
AL772338 Genomic DNA. Translation: CAM25530.1.
BC016238 mRNA. Translation: AAH16238.1.
CCDSiCCDS18412.1. [Q9D8H7-1]
RefSeqiNP_080185.1. NM_025909.3. [Q9D8H7-1]
XP_006503362.1. XM_006503299.2. [Q9D8H7-1]
XP_006503363.1. XM_006503300.2. [Q9D8H7-1]
UniGeneiMm.30021.

3D structure databases

ProteinModelPortaliQ9D8H7.
SMRiQ9D8H7. Positions 278-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045269.

Protein family/group databases

MEROPSiM48.017.

PTM databases

iPTMnetiQ9D8H7.
PhosphoSiteiQ9D8H7.

Proteomic databases

EPDiQ9D8H7.
MaxQBiQ9D8H7.
PaxDbiQ9D8H7.
PRIDEiQ9D8H7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035780; ENSMUSP00000045269; ENSMUSG00000035069. [Q9D8H7-1]
GeneIDi67013.
KEGGimmu:67013.
UCSCiuc008txq.1. mouse. [Q9D8H7-1]

Organism-specific databases

CTDi115209.
MGIiMGI:1914263. Oma1.

Phylogenomic databases

eggNOGiKOG2661. Eukaryota.
COG0501. LUCA.
GeneTreeiENSGT00390000007027.
HOGENOMiHOG000115266.
HOVERGENiHBG096685.
InParanoidiQ9D8H7.
OMAiFAIIVGR.
OrthoDBiEOG7Q8CNJ.
PhylomeDBiQ9D8H7.
TreeFamiTF329133.

Miscellaneous databases

PROiQ9D8H7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8H7.
GenevisibleiQ9D8H7. MM.

Family and domain databases

InterProiIPR001915. Peptidase_M48.
[Graphical view]
PfamiPF01435. Peptidase_M48. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Egg and Small intestine.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] (ISOFORM 1).
    Tissue: Eye.
  4. "Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1."
    Ehses S., Raschke I., Mancuso G., Bernacchia A., Geimer S., Tondera D., Martinou J.C., Westermann B., Rugarli E.I., Langer T.
    J. Cell Biol. 187:1023-1036(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart.
  6. "Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice."
    Quiros P.M., Ramsay A.J., Sala D., Fernandez-Vizarra E., Rodriguez F., Peinado J.R., Fernandez-Garcia M.S., Vega J.A., Enriquez J.A., Zorzano A., Lopez-Otin C.
    EMBO J. 31:2117-2133(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiOMA1_MOUSE
AccessioniPrimary (citable) accession number: Q9D8H7
Secondary accession number(s): Q3UWN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.