Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Metalloendopeptidase OMA1, mitochondrial

Gene

Oma1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi306 – 3061Zinc; catalyticBy similarity
Active sitei307 – 3071By similarity
Metal bindingi310 – 3101Zinc; catalyticBy similarity
Metal bindingi371 – 3711Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1304821. Oma1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei175 – 19521HelicalSequence analysisAdd
BLAST
Transmembranei320 – 34021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionSequence analysisAdd
BLAST
Chaini42 – 504463Metalloendopeptidase OMA1, mitochondrialBy similarityPRO_0000417519Add
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

PaxDbiD3ZS74.
PeptideAtlasiD3ZS74.

Expressioni

Gene expression databases

GenevisibleiD3ZS74. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009515.

Structurei

3D structure databases

ProteinModelPortaliD3ZS74.
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.
InParanoidiD3ZS74.
OMAiFAIIVGR.
OrthoDBiEOG7Q8CNJ.
PhylomeDBiD3ZS74.
TreeFamiTF329133.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

D3ZS74-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFLYGLQSA TRNQFLSGVN TLARRRTWTP PAGCPLASRL PAVNANWGLS
60 70 80 90 100
TVSHCYSVIL LPRNLHFCRT LKNKRSRCLS SAQSKEMGVL TYNWTVWGDA
110 120 130 140 150
SCSPNYAAIR EVRSFHTSAP RQAAPVPLLM LILKPVQKLL AIIVGRGIRK
160 170 180 190 200
WWQALPPDKK ALFKDSVKRN KWRLLLGLSA FGLLFVVFYF THLEVSPVTG
210 220 230 240 250
RSKLLLVGKE HFRLLSDLEY EVWMEEFKND LLPEEDPRYL TVKKVVYHLT
260 270 280 290 300
QCNQDVPGVS EINWVVHVVH SPKVNAFVLP NGQVFVFTGL LNSVTDMHQL
310 320 330 340 350
SFLLGHEIAH AVLGHAAEKA SLVHLLDFLG MIFLTMIWAI CPRDSLAVLG
360 370 380 390 400
QWIQSKLQEY MFDRPYSRTL EAEADKIGLQ LAAKACVDVR ASSVFWQQME
410 420 430 440 450
FSESLHGYPK LPEWLSTHPS HGNRAEYLDR LIPQALKLRE VCNCPPLSGP
460 470 480 490 500
DPRLLFRLTV KHLLEDSEKE DLNITVKKQK PDALPIQKQE QIPLTYALGK

RTAG
Length:504
Mass (Da):57,145
Last modified:April 20, 2010 - v1
Checksum:iD7456DE65BC9ECDE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473998 Genomic DNA. Translation: EDL97870.1.
RefSeqiNP_001100139.1. NM_001106669.1.
XP_006238537.1. XM_006238475.2.
UniGeneiRn.14712.

Genome annotation databases

EnsembliENSRNOT00000009516; ENSRNOP00000009515; ENSRNOG00000007214.
GeneIDi298282.
KEGGirno:298282.
UCSCiRGD:1304821. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473998 Genomic DNA. Translation: EDL97870.1.
RefSeqiNP_001100139.1. NM_001106669.1.
XP_006238537.1. XM_006238475.2.
UniGeneiRn.14712.

3D structure databases

ProteinModelPortaliD3ZS74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009515.

Proteomic databases

PaxDbiD3ZS74.
PeptideAtlasiD3ZS74.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009516; ENSRNOP00000009515; ENSRNOG00000007214.
GeneIDi298282.
KEGGirno:298282.
UCSCiRGD:1304821. rat.

Organism-specific databases

CTDi115209.
RGDi1304821. Oma1.

Phylogenomic databases

eggNOGiKOG2661. Eukaryota.
COG0501. LUCA.
GeneTreeiENSGT00390000007027.
InParanoidiD3ZS74.
OMAiFAIIVGR.
OrthoDBiEOG7Q8CNJ.
PhylomeDBiD3ZS74.
TreeFamiTF329133.

Miscellaneous databases

PROiD3ZS74.

Gene expression databases

GenevisibleiD3ZS74. RN.

Family and domain databases

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

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.

Entry informationi

Entry nameiOMA1_RAT
AccessioniPrimary (citable) accession number: D3ZS74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: April 20, 2010
Last modified: July 6, 2016
This is version 41 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. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.