Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Lon protease homolog, mitochondrial (EC 3.4.21.-) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15)

 LONM_RAT                Reviewed;         950 AA.
Q924S5;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
30-AUG-2017, entry version 112.
RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
EC=3.4.21.- {ECO:0000255|HAMAP-Rule:MF_03120};
AltName: Full=Lon protease-like protein {ECO:0000255|HAMAP-Rule:MF_03120};
Short=LONP {ECO:0000255|HAMAP-Rule:MF_03120};
AltName: Full=Mitochondrial ATP-dependent protease Lon {ECO:0000255|HAMAP-Rule:MF_03120};
AltName: Full=Serine protease 15 {ECO:0000255|HAMAP-Rule:MF_03120};
Flags: Precursor;
Name=Lonp1; Synonyms=Lon, Prss15;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=12082077; DOI=10.1083/jcb.200108103;
Hori O., Ichinoda F., Tamatani T., Yamaguchi A., Sato N., Ozawa K.,
Kitao Y., Miyazaki M., Harding H.P., Ron D., Tohyama M., Stern D.M.,
Ogawa S.;
"Transmission of cell stress from endoplasmic reticulum to
mitochondria: enhanced expression of Lon protease.";
J. Cell Biol. 157:1151-1160(2002).
[2]
SUBCELLULAR LOCATION.
PubMed=7961901;
Wang N., Maurizi M.R., Emmert-Buck L., Gottesman M.M.;
"Synthesis, processing, and localization of human Lon protease.";
J. Biol. Chem. 269:29308-29313(1994).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12752449; DOI=10.1046/j.1432-1033.2003.03598.x;
Bakala H., Delaval E., Hamelin M., Bismuth J., Borot-Laloi C.,
Corman B., Friguet B.;
"Changes in rat liver mitochondria with aging. Lon protease-like
reactivity and N(epsilon)-carboxymethyllysine accumulation in the
matrix.";
Eur. J. Biochem. 270:2295-2302(2003).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15560797; DOI=10.1111/j.1432-1033.2004.04422.x;
Delaval E., Perichon M., Friguet B.;
"Age-related impairment of mitochondrial matrix aconitase and ATP-
stimulated protease in rat liver and heart.";
Eur. J. Biochem. 271:4559-4564(2004).
-!- FUNCTION: ATP-dependent serine protease that mediates the
selective degradation of misfolded, unassembled or oxidatively
damaged polypeptides as well as certain short-lived regulatory
proteins in the mitochondrial matrix. May also have a chaperone
function in the assembly of inner membrane protein complexes.
Participates in the regulation of mitochondrial gene expression
and in the maintenance of the integrity of the mitochondrial
genome. Binds to mitochondrial promoters and RNA in a single-
stranded, site-specific, and strand-specific manner. May regulate
mitochondrial DNA replication and/or gene expression using site-
specific, single-stranded DNA binding to target the degradation of
regulatory proteins binding to adjacent sites in mitochondrial
promoters. {ECO:0000255|HAMAP-Rule:MF_03120,
ECO:0000269|PubMed:12752449, ECO:0000269|PubMed:15560797}.
-!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
central cavity. DNA and RNA binding is stimulated by substrate and
inhibited by ATP binding. Interacts with TWNK and mitochondrial
DNA polymerase subunit POLG. {ECO:0000255|HAMAP-Rule:MF_03120}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
Rule:MF_03120, ECO:0000269|PubMed:12752449,
ECO:0000269|PubMed:15560797, ECO:0000269|PubMed:7961901}.
-!- INDUCTION: By hypoxia or ER stress. {ECO:0000269|PubMed:12082077}.
-!- SIMILARITY: Belongs to the peptidase S16 family.
{ECO:0000255|HAMAP-Rule:MF_03120}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB064323; BAB62423.1; -; mRNA.
RefSeq; NP_596895.1; NM_133404.1.
UniGene; Rn.146805; -.
ProteinModelPortal; Q924S5; -.
SMR; Q924S5; -.
IntAct; Q924S5; 1.
STRING; 10116.ENSRNOP00000066618; -.
MEROPS; S16.002; -.
iPTMnet; Q924S5; -.
PhosphoSitePlus; Q924S5; -.
PaxDb; Q924S5; -.
PRIDE; Q924S5; -.
Ensembl; ENSRNOT00000074253; ENSRNOP00000066618; ENSRNOG00000046502.
GeneID; 170916; -.
KEGG; rno:170916; -.
CTD; 9361; -.
RGD; 621598; Lonp1.
eggNOG; KOG2004; Eukaryota.
eggNOG; COG0466; LUCA.
GeneTree; ENSGT00530000063553; -.
HOVERGEN; HBG000798; -.
InParanoid; Q924S5; -.
KO; K08675; -.
OMA; MEMIDMS; -.
OrthoDB; EOG091G01TN; -.
PhylomeDB; Q924S5; -.
PRO; PR:Q924S5; -.
Proteomes; UP000002494; Chromosome 9.
Bgee; ENSRNOG00000046502; -.
Genevisible; Q924S5; RN.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0043531; F:ADP binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:RGD.
GO; GO:0070182; F:DNA polymerase binding; IEA:Ensembl.
GO; GO:0051880; F:G-quadruplex DNA binding; IEA:Ensembl.
GO; GO:0070362; F:mitochondrial heavy strand promoter anti-sense binding; IEA:Ensembl.
GO; GO:0070361; F:mitochondrial light strand promoter anti-sense binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0043623; P:cellular protein complex assembly; IMP:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IBA:GO_Central.
GO; GO:0007005; P:mitochondrion organization; IEP:RGD.
GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IDA:RGD.
GO; GO:0010044; P:response to aluminum ion; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
Gene3D; 3.30.230.10; -; 1.
HAMAP; MF_03120; lonm_euk; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR004815; Lon_bac/euk-typ.
InterPro; IPR008269; Lon_proteolytic.
InterPro; IPR027065; Lon_Prtase.
InterPro; IPR003111; Lon_substr-bd.
InterPro; IPR027503; Lonm_euk.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008268; Peptidase_S16_AS.
InterPro; IPR015947; PUA-like_domain.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
PANTHER; PTHR43718; PTHR43718; 1.
Pfam; PF00004; AAA; 1.
Pfam; PF05362; Lon_C; 1.
Pfam; PF02190; LON_substr_bdg; 1.
PIRSF; PIRSF001174; Lon_proteas; 1.
SMART; SM00382; AAA; 1.
SMART; SM00464; LON; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF88697; SSF88697; 1.
TIGRFAMs; TIGR00763; lon; 1.
PROSITE; PS51787; LON_N; 1.
PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PROSITE; PS01046; LON_SER; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; DNA-binding; Hydrolase; Mitochondrion;
Nucleotide-binding; Protease; Reference proteome; Serine protease;
Transit peptide.
TRANSIT 1 65 Mitochondrion. {ECO:0000255|HAMAP-
Rule:MF_03120}.
CHAIN 66 950 Lon protease homolog, mitochondrial.
/FTId=PRO_0000254962.
DOMAIN 112 358 Lon N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU01123}.
DOMAIN 749 939 Lon proteolytic. {ECO:0000255|PROSITE-
ProRule:PRU01122}.
NP_BIND 513 520 ATP. {ECO:0000255|HAMAP-Rule:MF_03120}.
ACT_SITE 845 845 {ECO:0000255|HAMAP-Rule:MF_03120}.
ACT_SITE 888 888 {ECO:0000255|HAMAP-Rule:MF_03120}.
SEQUENCE 950 AA; 105793 MW; D505C3D851B6F0E7 CRC64;
MAASTGYVRL WAAARCWVLR RPLLAVTGGR VPSASGSWLR RGCRVCDTST PWGGRVPMGG
GQWRGLWDAG SRGGSDETSE GGVEDGATAS SGEGPVVTAL APMTVPDVFP HLPLIAISRN
PVFPRFIKIV EVKNKKLVEL LRRKVRLAQP YVGVFLKRDD NNESDVVESL DEIYHTGTFA
QIHEMQDLGD KLRMIVTGHR RIHISRQLEV EPEGLEPEAE NKQKSRRKLK RGKKEVGDEL
GAKPQLEMVT EATSDTSKEV LMVEVENVAH EDFQVTEEVK ALTAEIVKTI RDIIALNPLY
RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL EETNILKRLY KALSLLKKEF
ELSKLQQRLG REVEEKIKQT HRKYLLQEQL KIIKKELGLE KDDKDAIEEK FRERLKELVV
PKHVMDVVDE ELSKLALLDN HSSEFNVTRN YLDWLTSIPW GRQSDENLDL ARAQSVLEED
HYGMEDVKKR VLEFIAVSQL RGSTQGKILC FHGPPGVGKT SIARSIARAL GREYFRFSVG
GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLVLID EVDKIGRGYQ GDPSSALLEL
LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR DRMEMINVSG YVAQEKLAIA
ERYLVPQART LCGLDESKAQ LSATVLTLLI KQYCRESGVR NLQKQVEKVL RKAAYKIVSG
EAQTVHVTPE NLQDFVGKPV FTVERMYDVT PPGVVMGLAW TAMGGSTLFV ETSLRRPQPS
GSKEDKDGSL EVTGQLGDVM KESARIAYTF ARAFLMEQDP ENDFLVTSHI HLHVPEGATP
KDGPSAGCTI VTALLSLALG QPVLQNLAMT GEVSLTGKVL PVGGIKEKTI AAKRAGVTCI
ILPAENRKDF SDLAPFITEG LEVHFVEHYR DIFRIAFPLR EHQEALAVER


Related products :

Catalog number Product name Quantity
EIAAB40101 Homo sapiens,Human,Matriptase,Membrane-type serine protease 1,MT-SP1,Prostamin,PRSS14,Serine protease 14,Serine protease TADG-15,SNC19,ST14,Suppressor of tumorigenicity 14 protein,TADG15,Tumor-associa
EIAAB32605 Disp,Distal intestinal serine protease,Prss30,Rat,Rattus norvegicus,Serine protease 30,Tmprss8,Tmsp1,TMSP-1,Tmsp-1,Transmembrane serine protease 1,Transmembrane serine protease 8
EIAAB32606 Disp,Distal intestinal serine protease,Mouse,Mus musculus,Prss30,Serine protease 30,Tmprss8,Transmembrane serine protease 8
E2234h ELISA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234h CLIA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234h CLIA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234m ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234h Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2
U2234r CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234r ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234m CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234m ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
U2234m CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234r ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234r CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E0691h ELISA kit Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T
E0691h ELISA Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T
U0691h CLIA Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T
EIAAB42592 Adrenal secretory serine protease,Airway trypsin-like protease,AsP,AT,Mat,Mouse,Mus musculus,Tmprss11d,Transmembrane protease serine 11D
EIAAB42593 Adrenal secretory serine protease,Airway trypsin-like protease,AsP,AT,Rat,Rat,Rattus norvegicus,Tmprss11d,Transmembrane protease serine 11D
orb90001 GST_HRV Protease Protease Recombinant is fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes subset of sequences whic 100 IU
E2234r Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus
E2234m Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus
30-350 ST14 is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-pho 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur