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Entry version 64 (26 Feb 2020)
Sequence version 1 (03 May 2011)
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Protein

Lysyl oxidase homolog 2A

Gene

loxl2a

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
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 transcript 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

Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency (By similarity). Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3 (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity). Required with loxl2b for correct expression of Sox2 and for neural differentiation (PubMed:25959397).By similarity2 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 bindingi517CalciumBy similarity1
Metal bindingi518Calcium; via carbonyl oxygenBy similarity1
Metal bindingi593CopperBy similarity1
Metal bindingi595CopperBy similarity1
Metal bindingi597CopperBy similarity1
Metal bindingi689CalciumBy similarity1
Metal bindingi691Calcium; via carbonyl oxygenBy similarity1
Metal bindingi694CalciumBy similarity1
Metal bindingi695CalciumBy similarity1

<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 functionChromatin regulator, Oxidoreductase, Repressor
Biological processTranscription, Transcription regulation
LigandCalcium, Copper, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.4.3.13 928

<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 2A (EC:1.4.3.13By similarity)
Alternative name(s):
Lysyl oxidase-like protein 2A
<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:loxl2a
<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>OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
<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 identifieri7955 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
<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
  • UP000000437 <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 10

Organism-specific databases

Zebrafish Information Network genome database

More...
ZFINi
ZDB-GENE-070818-1 loxl2a

<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

Basement membrane, Chromosome, Endoplasmic reticulum, Extracellular matrix, 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

Morpholino knockdown in the embryo prevents the formation of intersegmental blood vessels (PubMed:21835952). Morpholino knockdown of loxl2a and loxl2b in the embryo results in increased expression of Sox2 in the central nervous system, particularly in the eye, hindbrain and spinal cord (PubMed:25959397). It also leads to impaired neural differentiation with morphological defects in the brain where the anterior brain is rounder than normal and the eyes present a flatter curvature (PubMed:25959397). Embryo development is also compromised (PubMed:25959397).2 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 – 18Sequence analysisAdd BLAST18
<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_000041800419 – 737Lysyl oxidase homolog 2AAdd BLAST719

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 bondi55 ↔ 119PROSITE-ProRule annotation
Disulfide bondi68 ↔ 129PROSITE-ProRule annotation
Disulfide bondi99 ↔ 109PROSITE-ProRule annotation
Disulfide bondi188 ↔ 259PROSITE-ProRule annotation
Disulfide bondi201 ↔ 269PROSITE-ProRule annotation
Disulfide bondi235 ↔ 245PROSITE-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>Glycosylationi256N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi319 ↔ 382PROSITE-ProRule annotation
Disulfide bondi332 ↔ 392PROSITE-ProRule annotation
Disulfide bondi363 ↔ 373PROSITE-ProRule annotation
Glycosylationi423N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi432 ↔ 498PROSITE-ProRule annotation
Disulfide bondi445 ↔ 511PROSITE-ProRule annotation
Disulfide bondi479 ↔ 489PROSITE-ProRule annotation
Disulfide bondi541 ↔ 592By similarity
Disulfide bondi547 ↔ 662By similarity
Glycosylationi611N-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-linki620 ↔ 656Lysine tyrosylquinone (Lys-Tyr)By similarity
Disulfide bondi624 ↔ 640By similarity
Disulfide bondi630 ↔ 652By similarity
<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 residuei6562',4',5'-topaquinoneBy similarity1
Disulfide bondi699 ↔ 713PROSITE-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

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

More...
PaxDbi
F1QQC3

PRoteomics IDEntifications database

More...
PRIDEi
F1QQC3

<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 the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expression increases between 20 and 48 hours after fertilization and is detected in sprouting intersegmental vessels (PubMed:21835952). At 24 hours after fertilization, expressed throughout the embryo with high levels in eye, mesencephalon and hindbrain boundaries (PubMed:25959397).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSDARG00000044010 Expressed in liver and 18 other tissues

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
7955.ENSDARP00000064612

<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
F1QQC3

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>Domaini29 – 130SRCR 1PROSITE-ProRule annotationAdd BLAST102
Domaini159 – 270SRCR 2PROSITE-ProRule annotationAdd BLAST112
Domaini294 – 393SRCR 3PROSITE-ProRule annotationAdd BLAST100
Domaini403 – 512SRCR 4PROSITE-ProRule annotationAdd BLAST110

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>Regioni516 – 718Lysyl-oxidase likeBy similarityAdd BLAST203

<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

More...
eggNOGi
ENOG410IE2X Eukaryota
ENOG410XSN1 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155874

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
F1QQC3

KEGG Orthology (KO)

More...
KOi
K00280

Identification of Orthologs from Complete Genome Data

More...
OMAi
RRKKNYW

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>Sequencei

<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.

F1QQC3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAVSSALCIF SLLVLAQAQS ELQQPKIELR LAGDKRKHYE GRLEVFYNNE
60 70 80 90 100
WGTVCDDDFS IEAAHVACRQ LGFLGAVAWS PSAKFGQGEG RIWLDNVHCT
110 120 130 140 150
GRENSLAACP SNGFGVSDCR HSEDVGVICN QKRIPGHRFI NIMNNNVETL
160 170 180 190 200
EERVEEIRIR PISSHLKRIP ITEGYVEVKE RGKWRQICDE EWTPLNSRVA
210 220 230 240 250
CGMYGFPGEK NYNNKVYRSL SMRKKKNYWG FSVNCTGNEA HVSSCRLGKA
260 270 280 290 300
LEPKRNGTCG RGLPVVVSCV PGRAFAPSSS IGFRKAYRPE QPLVRLRGGA
310 320 330 340 350
NVGEGRVEVL KNGVWGTVCD DNWNLKAATV VCRELGFGSA KEALTGAKLG
360 370 380 390 400
QGMGPVHMNE VECSGFEKSL TDCYFNNDAL GCSHEEDAAV RCNVPAMGFQ
410 420 430 440 450
KRIRLSGGRN PFEGRVEVLA EKNGSLVWGT VCSENWGIIE AMVVCRQLGL
460 470 480 490 500
GFASHAFQET WYWAGDANAD NVVMSGVRCS GTEMSLPQCL HHGKHINCPK
510 520 530 540 550
GGGRFAAGVS CSDTAPDLVL NAQLVEQTTY LEDRPMYALQ CALEENCLSS
560 570 580 590 600
TARKNDHSSY RRLLRFSSQI HNVGQSDFRP KLGYHAWTWH ECHRHYHSME
610 620 630 640 650
VFTHYDLLSL NGTKVAEGHK ASFCLEDTHC DEGISKRYHC ANFGEQGITV
660 670 680 690 700
GCWDTYRHDI DCQWIDVTDV KPGDYIFQVV INPNYDVAES DYTNNVMKCK
710 720 730
CRYDGYRIWT YSCHIGGSRS SDMDEYSGMS NQLNHLR
Length:737
Mass (Da):82,334
Last modified:May 3, 2011 - v1
<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:iCBB61E1520E97ED3
GO

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 conflicti9 – 11IFS → VFG in ABM86967 (PubMed:17543297).Curated3
Sequence conflicti16A → V in ABM86967 (PubMed:17543297).Curated1
Sequence conflicti147V → I in ABM86967 (PubMed:17543297).Curated1
Sequence conflicti181R → W in ABM86967 (PubMed:17543297).Curated1
Sequence conflicti200A → V in ABM86967 (PubMed:17543297).Curated1
Sequence conflicti232S → L in ABM86967 (PubMed:17543297).Curated1
Sequence conflicti242V → M in ABM86967 (PubMed:17543297).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
EF030481 mRNA Translation: ABM86967.1
BX294119 Genomic DNA No translation available.

NCBI Reference Sequences

More...
RefSeqi
NP_001092714.1, NM_001099244.1
XP_009303525.1, XM_009305250.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSDART00000064613; ENSDARP00000064612; ENSDARG00000044010

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
565508

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dre:565508

<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
EF030481 mRNA Translation: ABM86967.1
BX294119 Genomic DNA No translation available.
RefSeqiNP_001092714.1, NM_001099244.1
XP_009303525.1, XM_009305250.2

3D structure databases

SMRiF1QQC3
ModBaseiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000064612

Proteomic databases

PaxDbiF1QQC3
PRIDEiF1QQC3

Genome annotation databases

EnsembliENSDART00000064613; ENSDARP00000064612; ENSDARG00000044010
GeneIDi565508
KEGGidre:565508

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
565508
ZFINiZDB-GENE-070818-1 loxl2a

Phylogenomic databases

eggNOGiENOG410IE2X Eukaryota
ENOG410XSN1 LUCA
GeneTreeiENSGT00940000155874
InParanoidiF1QQC3
KOiK00280
OMAiRRKKNYW
OrthoDBi815466at2759
TreeFamiTF326061

Enzyme and pathway databases

BRENDAi1.4.3.13 928

Miscellaneous databases

Protein Ontology

More...
PROi
PR:F1QQC3

Gene expression databases

BgeeiENSDARG00000044010 Expressed in liver and 18 other tissues

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
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<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 nameiLOL2A_DANRE
<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: F1QQC3
Secondary accession number(s): A6MH30
<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: June 13, 2012
Last sequence update: May 3, 2011
Last modified: February 26, 2020
This is version 64 of the entry and version 1 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
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