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Protein

Lysyl oxidase homolog 3

Gene

Loxl3

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

Functioni

Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins (PubMed:26954549). Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin (PubMed:26307084). Required for somite boundary formation by catalyzing oxidation of fibronectin (FN1), enhancing integrin signaling in myofibers and their adhesion to the myotendinous junction (MTJ) (PubMed:26954549). Acts as a regulator of inflammatory response by inhibiting differentiation of naive CD4+ T-cells into T-helper Th17 or regulatory T-cells (Treg): acts by interacting with STAT3 in the nucleus and catalyzing both deacetylation and oxidation of lysine residues on STAT3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (By similarity). Also able to catalyze deacetylation of lysine residues on STAT3 (By similarity).By similarity3 Publications

Catalytic activityi

[Protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2.By similarity
[protein]-N(6)-acetyl-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + acetamide + H2O2.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarity
  • lysine tyrosylquinone residueBy similarityNote: Contains 1 lysine tyrosylquinone.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi608CopperSequence analysis1
Metal bindingi610CopperSequence analysis1
Metal bindingi612CopperSequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandCopper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lysyl oxidase homolog 3Curated (EC:1.4.3.-By similarity, EC:1.4.3.13By similarity)
Alternative name(s):
Lysyl oxidase-like protein 31 Publication
Lysyl oxidase-related protein 21 Publication
Gene namesi
Name:Loxl3Imported
Synonyms:Lor21 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1337004. Loxl3.

Subcellular locationi

  • Secretedextracellular space 1 Publication
  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: It is unclear how LOXL3 is both intracellular (cytoplasmic and nuclear) and extracellular: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, the intracellular location is clearly reported and at least another protein of the family (LOXL2) also has intracellular and extracellular localization despite the presence of a signal sequence.By similarity

GO - Cellular componenti

  • extracellular region Source: MGI
  • extracellular space Source: BHF-UCL
  • membrane Source: InterPro

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Disruption phenotypei

Perinatal lethality, due to impaired development of the palate shelves and abnormalities in the cartilage primordia of the thoracic vertebrae (PubMed:26307084, PubMed:26954549). Cleft palates and spinal deformities are caused by the decreased collagen cross-links in the palate and spine (PubMed:26307084). In addition, mice display a reduction in the saccular space in the lungs at embryonic day 18.5 (E18.5) (PubMed:26307084, PubMed:27645581). Lungs also show reduced lung volumes and weights and deformed and smaller thoracic cavities (PubMed:27645581). Excess elastic fibers are detected, possibly due to an increased expression of Loxl4 (PubMed:27645581). Embryos show defects in the somitic boundaries, due to defects in myofibers that anchor prematurely or overshoot to adjacent somites, and lack tension (PubMed:26954549). Splenocytes show increased number of T-cells into T-helper Th17 cells and constitutive acetylation of Stat3 (PubMed:28065600).4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001853427 – 754Lysyl oxidase homolog 3Add BLAST728

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi71 ↔ 135PROSITE-ProRule annotation
Disulfide bondi84 ↔ 145PROSITE-ProRule annotation
Glycosylationi112N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi115 ↔ 125PROSITE-ProRule annotation
Disulfide bondi202 ↔ 272PROSITE-ProRule annotation
Disulfide bondi215 ↔ 282PROSITE-ProRule annotation
Disulfide bondi249 ↔ 259PROSITE-ProRule annotation
Glycosylationi267N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi333 ↔ 397PROSITE-ProRule annotation
Disulfide bondi346 ↔ 407PROSITE-ProRule annotation
Disulfide bondi377 ↔ 387PROSITE-ProRule annotation
Glycosylationi391N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi447 ↔ 512PROSITE-ProRule annotation
Disulfide bondi460 ↔ 525PROSITE-ProRule annotation
Glycosylationi482N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi493 ↔ 503PROSITE-ProRule annotation
Disulfide bondi555 ↔ 561PROSITE-ProRule annotation
Disulfide bondi607 ↔ 655PROSITE-ProRule annotation
Glycosylationi626N-linked (GlcNAc...)Sequence analysis1
Cross-linki635 ↔ 671Lysine tyrosylquinone (Lys-Tyr)By similarity
Disulfide bondi639 ↔ 645PROSITE-ProRule annotation
Disulfide bondi667 ↔ 677PROSITE-ProRule annotation
Modified residuei6712',4',5'-topaquinoneBy similarity1
Disulfide bondi714 ↔ 728PROSITE-ProRule annotation

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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, LTQ, TPQ

Proteomic databases

MaxQBiQ9Z175.
PaxDbiQ9Z175.
PeptideAtlasiQ9Z175.
PRIDEiQ9Z175.

PTM databases

PhosphoSitePlusiQ9Z175.

Expressioni

Tissue specificityi

Expressed in palate: predominantly present in the palate mesenchyme and tongue (at protein level) (PubMed:26307084). In spine, expressed in the original intervertebral disk, cartilage primordia, anterior and posterior longitudinal ligaments, meninges of spinal cord, lung and heart (PubMed:26307084). In eyes, strongly expressed in the skin of the eyelid and weakly expressed in the cornea and sclera (PubMed:26307084). In lung, predominantly expressed in the pulmonary mesenchyme (PubMed:27645581). In developing muscle, expressed at myofiber ends (at protein level) (PubMed:26954549).3 Publications

Gene expression databases

BgeeiENSMUSG00000000693.
CleanExiMM_LOXL3.
ExpressionAtlasiQ9Z175. baseline and differential.
GenevisibleiQ9Z175. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9Z175. 3 interactors.
STRINGi10090.ENSMUSP00000000707.

Structurei

3D structure databases

ProteinModelPortaliQ9Z175.
SMRiQ9Z175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 146SRCR 1PROSITE-ProRule annotationAdd BLAST102
Domaini170 – 283SRCR 2PROSITE-ProRule annotationAdd BLAST114
Domaini308 – 408SRCR 3PROSITE-ProRule annotationAdd BLAST101
Domaini418 – 526SRCR 4PROSITE-ProRule annotationAdd BLAST109

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni530 – 733Lysyl-oxidase likeAdd BLAST204

Sequence similaritiesi

Belongs to the lysyl oxidase family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IE2X. Eukaryota.
ENOG410XSN1. LUCA.
GeneTreeiENSGT00870000136394.
HOGENOMiHOG000220841.
HOVERGENiHBG052336.
InParanoidiQ9Z175.
KOiK00280.
OMAiTWYWDSG.
OrthoDBiEOG091G02XD.
TreeFamiTF326061.

Family and domain databases

Gene3Di3.10.250.10. 4 hits.
InterProiView protein in InterPro
IPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
PfamiView protein in Pfam
PF01186. Lysyl_oxidase. 1 hit.
PF00530. SRCR. 4 hits.
PRINTSiPR00074. LYSYLOXIDASE.
PR00258. SPERACTRCPTR.
SMARTiView protein in SMART
SM00202. SR. 4 hits.
SUPFAMiSSF56487. SSF56487. 4 hits.
PROSITEiView protein in PROSITE
PS00926. LYSYL_OXIDASE. 1 hit.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 4 hits.

Sequencei

Sequence statusi: Complete.

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

Q9Z175-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAVSVWYCC PWGLLLLHCL CSFSVGSPSP SISPEKKVGS QGLRFRLAGF
60 70 80 90 100
PRKPYEGRVE IQRAGEWGTI CDDDFTLQAA HVLCRELGFT EATGWTHSAK
110 120 130 140 150
YGPGTGRIWL DNLSCRGTEG SVTECASRGW GNSDCTHDED AGVICKDQRL
160 170 180 190 200
PGFSDSNVIE VEHQLQVEEV RLRPAVEWGR RPLPVTEGLV EVRLPEGWSQ
210 220 230 240 250
VCDKGWSAHN SHVVCGMLGF PGEKRVNMAF YRMLAQKKQH SFGLHSVACV
260 270 280 290 300
GTEAHLSLCS LEFYRANDTT RCSGGNPAVV SCVLGPLYAT FTGQKKQQHS
310 320 330 340 350
KPQGEARVRL KGGAHQGEGR VEVLKAGTWG TVCDRKWDLQ AASVVCRELG
360 370 380 390 400
FGTAREALSG ARMGQGMGAI HLSEVRCSGQ EPSLWRCPSK NITAEDCSHS
410 420 430 440 450
QDAGVRCNLP YTGVETKIRL SGGRSRYEGR VEVQIGIPGH LRWGLICGDD
460 470 480 490 500
WGTLEAMVAC RQLGLGYANH GLQETWYWDS GNVTEVVMSG VRCTGSELSL
510 520 530 540 550
NQCAHHSSHI TCKKTGTRFT AGVICSETAS DLLLHSALVQ ETAYIEDRPL
560 570 580 590 600
HMLYCAAEEN CLASSARSAN WPYGHRRLLR FSSQIHNLGR ADFRPKAGRH
610 620 630 640 650
SWVWHECHGH YHSMDIFTHY DILTPNGTKV AEGHKASFCL EDTECQEDVS
660 670 680 690 700
KRYECANFGE QGITVGCWDL YRHDIDCQWI DITDVKPGNY ILQVVINPNF
710 720 730 740 750
EVAESDFTNN AMKCNCKYDG HRIWVHNCHI GDAFSEEANR RFERYPGQTS

NQIV
Length:754
Mass (Da):83,740
Last modified:July 27, 2011 - v2
Checksum:iC3BF60F77696914D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti347R → P in AAC83205 (PubMed:9927484).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053368 mRNA. Translation: AAC83205.1.
AF084363 Genomic DNA. Translation: AAC95338.1.
AK030548 mRNA. Translation: BAC27016.1.
CH466523 Genomic DNA. Translation: EDK99047.1.
BC011298 mRNA. Translation: AAH11298.1.
CCDSiCCDS20266.1.
RefSeqiNP_038614.2. NM_013586.4.
UniGeneiMm.380433.

Genome annotation databases

EnsembliENSMUST00000000707; ENSMUSP00000000707; ENSMUSG00000000693.
GeneIDi16950.
KEGGimmu:16950.
UCSCiuc009clt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053368 mRNA. Translation: AAC83205.1.
AF084363 Genomic DNA. Translation: AAC95338.1.
AK030548 mRNA. Translation: BAC27016.1.
CH466523 Genomic DNA. Translation: EDK99047.1.
BC011298 mRNA. Translation: AAH11298.1.
CCDSiCCDS20266.1.
RefSeqiNP_038614.2. NM_013586.4.
UniGeneiMm.380433.

3D structure databases

ProteinModelPortaliQ9Z175.
SMRiQ9Z175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z175. 3 interactors.
STRINGi10090.ENSMUSP00000000707.

PTM databases

PhosphoSitePlusiQ9Z175.

Proteomic databases

MaxQBiQ9Z175.
PaxDbiQ9Z175.
PeptideAtlasiQ9Z175.
PRIDEiQ9Z175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000707; ENSMUSP00000000707; ENSMUSG00000000693.
GeneIDi16950.
KEGGimmu:16950.
UCSCiuc009clt.1. mouse.

Organism-specific databases

CTDi84695.
MGIiMGI:1337004. Loxl3.

Phylogenomic databases

eggNOGiENOG410IE2X. Eukaryota.
ENOG410XSN1. LUCA.
GeneTreeiENSGT00870000136394.
HOGENOMiHOG000220841.
HOVERGENiHBG052336.
InParanoidiQ9Z175.
KOiK00280.
OMAiTWYWDSG.
OrthoDBiEOG091G02XD.
TreeFamiTF326061.

Miscellaneous databases

PROiQ9Z175.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000693.
CleanExiMM_LOXL3.
ExpressionAtlasiQ9Z175. baseline and differential.
GenevisibleiQ9Z175. MM.

Family and domain databases

Gene3Di3.10.250.10. 4 hits.
InterProiView protein in InterPro
IPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
PfamiView protein in Pfam
PF01186. Lysyl_oxidase. 1 hit.
PF00530. SRCR. 4 hits.
PRINTSiPR00074. LYSYLOXIDASE.
PR00258. SPERACTRCPTR.
SMARTiView protein in SMART
SM00202. SR. 4 hits.
SUPFAMiSSF56487. SSF56487. 4 hits.
PROSITEiView protein in PROSITE
PS00926. LYSYL_OXIDASE. 1 hit.
PS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 4 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiLOXL3_MOUSE
AccessioniPrimary (citable) accession number: Q9Z175
Secondary accession number(s): Q91VN8, Q9JJ39
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: March 15, 2017
This is version 139 of the entry and version 2 of the sequence. See 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. 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.