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Q3MIB4

- LONP2_RAT

UniProt

Q3MIB4 - LONP2_RAT

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Protein

Lon protease homolog 2, peroxisomal

Gene

Lonp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei743 – 7431UniRule annotation
Active sitei786 – 7861UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi375 – 3828ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. ATP-dependent peptidase activity Source: RefGenome
  3. serine-type endopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. misfolded or incompletely synthesized protein catabolic process Source: RefGenome
  3. protein import into peroxisome matrix Source: UniProtKB-HAMAP
  4. protein processing Source: RefGenome
  5. protein targeting to peroxisome Source: RefGenome
  6. regulation of fatty acid beta-oxidation Source: Ensembl
  7. response to organic cyclic compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_244670. Association of TriC/CCT with target proteins during biosynthesis.

Protein family/group databases

MEROPSiS16.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Lon protease homolog 2, peroxisomalUniRule annotation (EC:3.4.21.-UniRule annotation)
Alternative name(s):
Lon protease-like protein 2UniRule annotation
Short name:
Lon protease 2UniRule annotation
Peroxisomal Lon proteaseUniRule annotation
Gene namesi
Name:Lonp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 19

Organism-specific databases

RGDi1305466. Lonp2.

Subcellular locationi

Peroxisome matrix 1 PublicationUniRule annotation

GO - Cellular componenti

  1. nucleus Source: Ensembl
  2. peroxisomal matrix Source: RGD
  3. peroxisome Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 852851Lon protease homolog 2, peroxisomalPRO_0000287642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ3MIB4.
PRIDEiQ3MIB4.

Expressioni

Gene expression databases

ExpressionAtlasiQ3MIB4. baseline and differential.
GenevestigatoriQ3MIB4.

Interactioni

Subunit structurei

Interacts with PEX5. Interacts with TYSND1.UniRule annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020770.

Structurei

3D structure databases

ProteinModelPortaliQ3MIB4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 219207LonUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi850 – 8523Microbody targeting signalUniRule annotation

Sequence similaritiesi

Belongs to the peptidase S16 family.UniRule annotation
Contains 1 Lon domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0466.
GeneTreeiENSGT00530000063553.
HOGENOMiHOG000261408.
HOVERGENiHBG000798.
InParanoidiQ3MIB4.
KOiK01338.
OMAiDQREYFL.
OrthoDBiEOG77T13V.
PhylomeDBiQ3MIB4.
TreeFamiTF317215.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_03121. lonp2_euk.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR027501. Lonp2_euk.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR003111. Pept_S16_N.
IPR008268. Peptidase_S16_AS.
IPR015947. PUA-like_domain.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10046. PTHR10046. 1 hit.
PfamiPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001174. Lon_proteas. 1 hit.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00763. lon. 1 hit.
PROSITEiPS01046. LON_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q3MIB4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSVNPIQIP SRLPLLLTHE SVLLPGSTMR TSVDTARNLQ LVRSRLLKGT
60 70 80 90 100
SLQSTILGVI PNTPDPASDS QDLPPLHRIG TAALAVQVVG SNWPKPHYTL
110 120 130 140 150
LITGLCRFQI VQVLKEKPYP VAEVEQLDRL EEFPNTCKTR EELGELSEQF
160 170 180 190 200
YRYSVQLVEM LDMSVPAVAK LRRLLDSLPR EALPDILTSI IRTSNKEKLQ
210 220 230 240 250
ILDAVSLEDR FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK RVIAIRPIRR
260 270 280 290 300
ITHIPGALED EEEEEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM
310 320 330 340 350
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARILLD NDHYAMEKLK
360 370 380 390 400
RRVLEYLAVR QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA
410 420 430 440 450
LGGVCDQSDI RGHRRTYVGS MPGRIINGLK TVGVNNPVFL LDEVDKLGKS
460 470 480 490 500
LQGDPAAALL EVLDPEQNHN FTDHYLNVAF DLSQVLFIAT ANTTATIPPA
510 520 530 540 550
LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ IQIPQLTTLA
560 570 580 590 600
IITRYTREAG VRSLDRKFGA ICRAVAVKVA EGQHKEAKLD RSDVADGEGC
610 620 630 640 650
KEHVLEDAKP ESIGDAADLA LPPEMPILID SHALKDILGP PLYELEVSER
660 670 680 690 700
LSQPGVAIGL AWTPLGGKIM FVEASRMDGE GQLTLTGQLG DVMKESAHLA
710 720 730 740 750
ISWLRSNAKK YHLTNAFGSF DLLDNTDIHL HFPAGAVTKD GPSAGVTIVT
760 770 780 790 800
CLASLFSGRL VRSDVAMTGE ITLRGLVLPV GGIKDKVLAA HRAGLKHIII
810 820 830 840 850
PQRNEKDLEE IPSNVKQDLS FVTASCLDEV LNAAFDGGFT VKTRPGLTDS

KL
Length:852
Mass (Da):94,393
Last modified:May 15, 2007 - v2
Checksum:iCB9D9D05F8D5E040
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03113833 Genomic DNA. No translation available.
AABR03113838 Genomic DNA. No translation available.
AABR03114515 Genomic DNA. No translation available.
AABR03113506 Genomic DNA. No translation available.
BC103718 mRNA. Translation: AAI03719.1.
RefSeqiXP_006255300.1. XM_006255238.2.
UniGeneiRn.228635.

Genome annotation databases

EnsembliENSRNOT00000020770; ENSRNOP00000020770; ENSRNOG00000015162.
GeneIDi291922.
KEGGirno:291922.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03113833 Genomic DNA. No translation available.
AABR03113838 Genomic DNA. No translation available.
AABR03114515 Genomic DNA. No translation available.
AABR03113506 Genomic DNA. No translation available.
BC103718 mRNA. Translation: AAI03719.1 .
RefSeqi XP_006255300.1. XM_006255238.2.
UniGenei Rn.228635.

3D structure databases

ProteinModelPortali Q3MIB4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000020770.

Protein family/group databases

MEROPSi S16.006.

Proteomic databases

PaxDbi Q3MIB4.
PRIDEi Q3MIB4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000020770 ; ENSRNOP00000020770 ; ENSRNOG00000015162 .
GeneIDi 291922.
KEGGi rno:291922.

Organism-specific databases

CTDi 83752.
RGDi 1305466. Lonp2.

Phylogenomic databases

eggNOGi COG0466.
GeneTreei ENSGT00530000063553.
HOGENOMi HOG000261408.
HOVERGENi HBG000798.
InParanoidi Q3MIB4.
KOi K01338.
OMAi DQREYFL.
OrthoDBi EOG77T13V.
PhylomeDBi Q3MIB4.
TreeFami TF317215.

Enzyme and pathway databases

Reactomei REACT_244670. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

PROi Q3MIB4.

Gene expression databases

ExpressionAtlasi Q3MIB4. baseline and differential.
Genevestigatori Q3MIB4.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_03121. lonp2_euk.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR027501. Lonp2_euk.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR003111. Pept_S16_N.
IPR008268. Peptidase_S16_AS.
IPR015947. PUA-like_domain.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view ]
PANTHERi PTHR10046. PTHR10046. 1 hit.
Pfami PF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF001174. Lon_proteas. 1 hit.
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR00763. lon. 1 hit.
PROSITEi PS01046. LON_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "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] OF 297-852.
    Tissue: Ovary.
  3. "Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease."
    Kikuchi M., Hatano N., Yokota S., Shimozawa N., Imanaka T., Taniguchi H.
    J. Biol. Chem. 279:421-428(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLONP2_RAT
AccessioniPrimary (citable) accession number: Q3MIB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: November 26, 2014
This is version 75 of the entry and version 2 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

External Data

Dasty 3