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Protein

Protein-lysine 6-oxidase

Gene

Lox

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

Functioni

Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin.

Catalytic activityi

Peptidyl-L-lysyl-peptide + O2 + H2O = peptidyl-allysyl-peptide + NH3 + H2O2.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi286 – 2861CopperSequence analysis
Metal bindingi288 – 2881CopperSequence analysis
Metal bindingi290 – 2901CopperSequence analysis

GO - Molecular functioni

  • copper ion binding Source: RGD
  • protein-lysine 6-oxidase activity Source: RGD

GO - Biological processi

  • aorta development Source: Ensembl
  • collagen fibril organization Source: RGD
  • elastic fiber assembly Source: RGD
  • heart development Source: Ensembl
  • lung development Source: Ensembl
  • response to drug Source: RGD
  • response to hormone Source: RGD
  • response to steroid hormone Source: RGD
  • wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BRENDAi1.4.3.13. 5301.
ReactomeiR-RNO-1566948. Elastic fibre formation.
R-RNO-2243919. Crosslinking of collagen fibrils.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-lysine 6-oxidase (EC:1.4.3.13)
Alternative name(s):
Lysyl oxidase
Gene namesi
Name:Lox
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi3015. Lox.

Subcellular locationi

GO - Cellular componenti

  • collagen trimer Source: Ensembl
  • extracellular space Source: UniProtKB-SubCell
  • nucleus Source: RGD
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 1621411 PublicationPRO_0000018524Add
BLAST
Chaini163 – 411249Protein-lysine 6-oxidasePRO_0000018525Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence analysis
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi232 ↔ 238By similarity
Disulfide bondi285 ↔ 334By similarity
Cross-linki314 ↔ 349Lysine tyrosylquinone (Lys-Tyr)By similarity
Disulfide bondi318 ↔ 324By similarity
Disulfide bondi345 ↔ 355By similarity
Modified residuei349 – 34912',4',5'-topaquinoneBy similarity
Disulfide bondi392 ↔ 406By similarity

Post-translational modificationi

The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein, LTQ, TPQ

Proteomic databases

PaxDbiP16636.

PTM databases

PhosphoSiteiP16636.

Miscellaneous databases

PMAP-CutDBP16636.

Expressioni

Tissue specificityi

Aorta and lung.1 Publication

Gene expression databases

GenevisibleiP16636. RN.

Interactioni

Protein-protein interaction databases

IntActiP16636. 2 interactions.
STRINGi10116.ENSRNOP00000065314.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni207 – 411205Lysyl-oxidase likeAdd
BLAST

Sequence similaritiesi

Belongs to the lysyl oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHTH. Eukaryota.
ENOG41101E4. LUCA.
GeneTreeiENSGT00840000129711.
HOGENOMiHOG000234262.
HOVERGENiHBG000226.
InParanoidiP16636.
KOiK00277.
OMAiYSDDNPY.
OrthoDBiEOG7SN8C6.
PhylomeDBiP16636.
TreeFamiTF326061.

Family and domain databases

InterProiIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
[Graphical view]
PfamiPF01186. Lysyl_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00074. LYSYLOXIDASE.
PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16636-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFAWTVLFL GQLQFCPLLR CAPQAPREPP AAPGAWRQTI QWENNGQVFS
60 70 80 90 100
LLSLGAQYQP QRRRDSSATA PRADGNAAAQ PRTPILLLRD NRTASARART
110 120 130 140 150
PSPSGVAAGR PRPAARHWFQ VGFSPSGAGD GASRRAANRT ASPQPPQLSN
160 170 180 190 200
LRPPSHVDRM VGDDPYNPYK YSDDNPYYNY YDTYERPRSG SRHRPGYGTG
210 220 230 240 250
YFQYGLPDLV PDPYYIQAST YVQKMSMYNL RCAAEENCLA SSAYRADVRD
260 270 280 290 300
YDHRVLLRFP QRVKNQGTSD FLPSRPRYSW EWHSCHQHYH SMDEFSHYDL
310 320 330 340 350
LDASTQRRVA EGHKASFCLE DTSCDYGYHR RFACTAHTQG LSPGCYDTYA
360 370 380 390 400
ADIDCQWIDI TDVQPGNYIL KVSVNPSYLV PESDYSNNVV RCEIRYTGHH
410
AYASGCTISP Y
Length:411
Mass (Da):46,559
Last modified:November 1, 1995 - v2
Checksum:iEE68C9C5AACDFC1A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11038 mRNA. Translation: AAC52176.1.
J02903 mRNA. Translation: AAA41537.1.
BC078861 mRNA. Translation: AAH78861.1.
PIRiB40557. OXRTL.
RefSeqiNP_058757.1. NM_017061.2.
XP_006254775.1. XM_006254713.2.
XP_006254776.1. XM_006254714.2.
UniGeneiRn.11372.

Genome annotation databases

EnsembliENSRNOT00000019844; ENSRNOP00000019844; ENSRNOG00000014426.
ENSRNOT00000074226; ENSRNOP00000065314; ENSRNOG00000014426.
ENSRNOT00000083881; ENSRNOP00000068687; ENSRNOG00000014426.
GeneIDi24914.
KEGGirno:24914.
UCSCiRGD:3015. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11038 mRNA. Translation: AAC52176.1.
J02903 mRNA. Translation: AAA41537.1.
BC078861 mRNA. Translation: AAH78861.1.
PIRiB40557. OXRTL.
RefSeqiNP_058757.1. NM_017061.2.
XP_006254775.1. XM_006254713.2.
XP_006254776.1. XM_006254714.2.
UniGeneiRn.11372.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16636. 2 interactions.
STRINGi10116.ENSRNOP00000065314.

PTM databases

PhosphoSiteiP16636.

Proteomic databases

PaxDbiP16636.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000019844; ENSRNOP00000019844; ENSRNOG00000014426.
ENSRNOT00000074226; ENSRNOP00000065314; ENSRNOG00000014426.
ENSRNOT00000083881; ENSRNOP00000068687; ENSRNOG00000014426.
GeneIDi24914.
KEGGirno:24914.
UCSCiRGD:3015. rat.

Organism-specific databases

CTDi4015.
RGDi3015. Lox.

Phylogenomic databases

eggNOGiENOG410IHTH. Eukaryota.
ENOG41101E4. LUCA.
GeneTreeiENSGT00840000129711.
HOGENOMiHOG000234262.
HOVERGENiHBG000226.
InParanoidiP16636.
KOiK00277.
OMAiYSDDNPY.
OrthoDBiEOG7SN8C6.
PhylomeDBiP16636.
TreeFamiTF326061.

Enzyme and pathway databases

BRENDAi1.4.3.13. 5301.
ReactomeiR-RNO-1566948. Elastic fibre formation.
R-RNO-2243919. Crosslinking of collagen fibrils.

Miscellaneous databases

NextBioi604837.
PMAP-CutDBP16636.
PROiP16636.

Gene expression databases

GenevisibleiP16636. RN.

Family and domain databases

InterProiIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
[Graphical view]
PfamiPF01186. Lysyl_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00074. LYSYLOXIDASE.
PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence."
    Trackman P.C., Pratt A.M., Wolanski A., Tang S.-S., Offner G.D., Troxler R.F., Kagan H.M.
    Biochemistry 29:4863-4870(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Aorta.
  2. "Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence."
    Trackman P.C., Pratt A.M., Wolanski A., Tang S.-S., Offner G.D., Troxler R.F., Kagan H.M.
    Biochemistry 30:8282-8282(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
  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].
    Tissue: Testis.
  4. "Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase."
    Panchenko M.V., Stetler-Stevenson W.G., Trubetskoy O.V., Gacheru S.N., Kagan H.M.
    J. Biol. Chem. 271:7113-7119(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 163-167, PROTEOLYTIC PROCESSING OF N-TERMINUS.
  5. "Post-translational glycosylation and proteolytic processing of a lysyl oxidase precursor."
    Trackman P.C., Bedell-Hogan D., Tang J., Kagan H.M.
    J. Biol. Chem. 267:8666-8671(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF N-TERMINUS.

Entry informationi

Entry nameiLYOX_RAT
AccessioniPrimary (citable) accession number: P16636
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.