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Entry version 157 (17 Jun 2020)
Sequence version 2 (27 Jul 2011)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi608CopperSequence analysis1
Metal bindingi610CopperSequence analysis1
Metal bindingi612CopperSequence analysis1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandCopper, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1566948 Elastic fibre formation
R-MMU-2243919 Crosslinking of collagen fibrils

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Loxl3Imported
Synonyms:Lor21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1337004 Loxl3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 26Sequence analysisAdd BLAST26
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001853427 – 754Lysyl oxidase homolog 3Add BLAST728

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi71 ↔ 135PROSITE-ProRule annotation
Disulfide bondi84 ↔ 145PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi112N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi115 ↔ 125PROSITE-ProRule annotation
Disulfide bondi202 ↔ 272PROSITE-ProRule annotation
Disulfide bondi215 ↔ 282PROSITE-ProRule annotation
Disulfide bondi249 ↔ 259PROSITE-ProRule annotation
Glycosylationi267N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi333 ↔ 397PROSITE-ProRule annotation
Disulfide bondi346 ↔ 407PROSITE-ProRule annotation
Disulfide bondi377 ↔ 387PROSITE-ProRule annotation
Glycosylationi391N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi447 ↔ 512PROSITE-ProRule annotation
Disulfide bondi460 ↔ 525PROSITE-ProRule annotation
Glycosylationi482N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi493 ↔ 503PROSITE-ProRule annotation
Disulfide bondi555 ↔ 561PROSITE-ProRule annotation
Disulfide bondi607 ↔ 655PROSITE-ProRule annotation
Glycosylationi626N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki635 ↔ 671Lysine tyrosylquinone (Lys-Tyr)By similarity
Disulfide bondi639 ↔ 645PROSITE-ProRule annotation
Disulfide bondi667 ↔ 677PROSITE-ProRule annotation
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei6712',4',5'-topaquinoneBy similarity1
Disulfide bondi714 ↔ 728PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9Z175

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9Z175

PeptideAtlas

More...
PeptideAtlasi
Q9Z175

PRoteomics IDEntifications database

More...
PRIDEi
Q9Z175

PTM databases

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9Z175

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000000693 Expressed in fibroblast and 212 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9Z175 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9Z175 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q9Z175, 4 interactors

Molecular INTeraction database

More...
MINTi
Q9Z175

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000000707

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9Z175 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9Z175

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni530 – 733Lysyl-oxidase likeAdd BLAST204

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the lysyl oxidase family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IE2X Eukaryota
ENOG410XSN1 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158157

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_002555_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Z175

KEGG Orthology (KO)

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KOi
K00280

Identification of Orthologs from Complete Genome Data

More...
OMAi
GVRCTGS

Database of Orthologous Groups

More...
OrthoDBi
815466at2759

TreeFam database of animal gene trees

More...
TreeFami
TF326061

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.250.10, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001695 Lysyl_oxidase
IPR019828 Lysyl_oxidase_CS
IPR001190 SRCR
IPR017448 SRCR-like_dom
IPR036772 SRCR-like_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01186 Lysyl_oxidase, 1 hit
PF00530 SRCR, 4 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00074 LYSYLOXIDASE
PR00258 SPERACTRCPTR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00202 SR, 4 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56487 SSF56487, 4 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00926 LYSYL_OXIDASE, 1 hit
PS00420 SRCR_1, 1 hit
PS50287 SRCR_2, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC3BF60F77696914D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9Q0X7E9Q0X7_MOUSE
Lysyl oxidase homolog
Loxl3
472Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti347R → P in AAC83205 (PubMed:9927484).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS20266.1

NCBI Reference Sequences

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RefSeqi
NP_038614.2, NM_013586.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000000707; ENSMUSP00000000707; ENSMUSG00000000693

Database of genes from NCBI RefSeq genomes

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GeneIDi
16950

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:16950

UCSC genome browser

More...
UCSCi
uc009clt.1 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

SMRiQ9Z175
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ9Z175, 4 interactors
MINTiQ9Z175
STRINGi10090.ENSMUSP00000000707

PTM databases

PhosphoSitePlusiQ9Z175

Proteomic databases

MaxQBiQ9Z175
PaxDbiQ9Z175
PeptideAtlasiQ9Z175
PRIDEiQ9Z175

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
31582 174 antibodies

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
84695
MGIiMGI:1337004 Loxl3

Phylogenomic databases

eggNOGiENOG410IE2X Eukaryota
ENOG410XSN1 LUCA
GeneTreeiENSGT00940000158157
HOGENOMiCLU_002555_3_0_1
InParanoidiQ9Z175
KOiK00280
OMAiGVRCTGS
OrthoDBi815466at2759
TreeFamiTF326061

Enzyme and pathway databases

ReactomeiR-MMU-1566948 Elastic fibre formation
R-MMU-2243919 Crosslinking of collagen fibrils

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
16950 1 hit in 12 CRISPR screens

Protein Ontology

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PROi
PR:Q9Z175
RNActiQ9Z175 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000000693 Expressed in fibroblast and 212 other tissues
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
IPR036772 SRCR-like_dom_sf
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLOXL3_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Z175
Secondary accession number(s): Q91VN8, Q9JJ39
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: June 17, 2020
This is version 157 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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