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Entry version 104 (11 Dec 2019)
Sequence version 1 (06 Feb 2007)
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Protein

Lysyl oxidase homolog 2B

Gene

loxl2b

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 loxl2a for correct expression of Sox2 and for neural differentiation (PubMed:25959397).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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 bindingi541CalciumBy similarity1
Metal bindingi542Calcium; via carbonyl oxygenBy similarity1
Metal bindingi617CopperBy similarity1
Metal bindingi619CopperBy similarity1
Metal bindingi621CopperBy similarity1
Metal bindingi713CalciumBy similarity1
Metal bindingi715Calcium; via carbonyl oxygenBy similarity1
Metal bindingi718CalciumBy similarity1
Metal bindingi719CalciumBy 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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DRE-1566948 Elastic fibre formation
R-DRE-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_and_taxonomy_section">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 2B (EC:1.4.3.13By similarity)
Alternative name(s):
Lysyl oxidase-like protein 2B
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:loxl2b
ORF Names:si:dkeyp-32b1.1, zgc:158414
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 5

Organism-specific databases

Zebrafish Information Network genome database

More...
ZFINi
ZDB-GENE-050208-29 loxl2b

<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 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. 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. Embryo development is also compromised.1 Publication

<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 – 20Sequence analysisAdd BLAST20
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000041800521 – 762Lysyl oxidase homolog 2BAdd BLAST742

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 bondi79 ↔ 143PROSITE-ProRule annotation
Disulfide bondi92 ↔ 153PROSITE-ProRule annotation
Disulfide bondi123 ↔ 133PROSITE-ProRule annotation
Disulfide bondi213 ↔ 281PROSITE-ProRule annotation
Disulfide bondi226 ↔ 291PROSITE-ProRule annotation
Disulfide bondi260 ↔ 270PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi278N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi341 ↔ 406PROSITE-ProRule annotation
Disulfide bondi354 ↔ 416PROSITE-ProRule annotation
Disulfide bondi385 ↔ 395PROSITE-ProRule annotation
Glycosylationi447N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi456 ↔ 522PROSITE-ProRule annotation
Disulfide bondi469 ↔ 535PROSITE-ProRule annotation
Disulfide bondi503 ↔ 513PROSITE-ProRule annotation
Disulfide bondi565 ↔ 616By similarity
Disulfide bondi571 ↔ 686By similarity
Glycosylationi635N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-linki644 ↔ 680Lysine tyrosylquinone (Lys-Tyr)By similarity
Disulfide bondi648 ↔ 664By similarity
Disulfide bondi654 ↔ 676By 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 residuei6802',4',5'-topaquinoneBy similarity1
Disulfide bondi723 ↔ 737PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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
A1L1V4

PRoteomics IDEntifications database

More...
PRIDEi
A1L1V4

<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 is initiated during early development throughout the notochord and extinguished between 24 and 48 hours after fertilization (PubMed:17543297). At 24 hours after fertilization, expressed ubiquitously throughout the embryo (PubMed:25959397).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSDARG00000044074 Expressed in 22 organ(s), highest expression level in head

<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.ENSDARP00000118755

<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_and_domains_section">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>Domaini53 – 154SRCR 1PROSITE-ProRule annotationAdd BLAST102
Domaini183 – 292SRCR 2PROSITE-ProRule annotationAdd BLAST110
Domaini316 – 417SRCR 3PROSITE-ProRule annotationAdd BLAST102
Domaini427 – 536SRCR 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>Regioni540 – 742Lysyl-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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000220841

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
A1L1V4

KEGG Orthology (KO)

More...
KOi
K00280

Identification of Orthologs from Complete Genome Data

More...
OMAi
WYWHGNI

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, 2 hits
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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

A1L1V4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLALWSISFV LLCSWRLSYA QYEHLGFAIA YQEPEQDLYT PPELPADTPR
60 70 80 90 100
IQLRLAGEKR KHNEGRVEVF YEGEWGTVCD DDFTIHAAQV ICRELGYFEA
110 120 130 140 150
ISWSPSSKYG KGEGRIWFDN VHCKGKEKSL AQCESNGIGV SDCKHSEDVG
160 170 180 190 200
VVCSDKRIPG FKFVNTLTNN INSLNIQVED VRIRPILASY RKRIPVTEGY
210 220 230 240 250
VEVKDGGKWK QICDDEWTQM NSRVICGMFG FPGQKRYNTR VYKMFARRRK
260 270 280 290 300
PSYWDYTINC TGKEAHLSSC TLGHTLSNST CEEGTPVVVS CIPGRAFAPT
310 320 330 340 350
PMTGYKKAFR QEQPLVRLRG GAVVGEGRVE VLKNGEWGTI CDDNWNLLAA
360 370 380 390 400
TVVCRELGFG SAKEALSGGQ LGQGMGPVHM NEVQCSGFEK SVTECSFNME
410 420 430 440 450
KDSEGCSHEE DAGVKCNVPA MGFQQRLRLS GGRNPFEGRV EVLVERNGSL
460 470 480 490 500
VWGTVCGEGW TTMEAMVVCR QLGLGFASNA FQETWYWPGA VNADAVVMSG
510 520 530 540 550
VRCAGTEMSL SHCLHHGEYL SCPKGGGRFA AGVSCSETAP DLVLNPQVVE
560 570 580 590 600
QTTYLEDRPM FMLQCAYEEN CLASTSSATP ANSPRRLLRF SSQIHNNGQS
610 620 630 640 650
DFRPKISREN WVWHDCHRHY HSMEVFTHYD LLSTNGTKVA EGHKASFCLE
660 670 680 690 700
DSECDEGIEK RYECANFGEQ GITVGCWDTY RHDIDCQWVD ITDVKPGDYI
710 720 730 740 750
FQIVINPNYE VAESDYTNNI VKCRCRYDGH RIWMYNCHIG GSFSAETEDT
760
FPGLINNQVT HR
Length:762
Mass (Da):85,503
Last modified:February 6, 2007 - 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:i9FBAF7387A40DF45
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAN88496 differs from that shown. Reason: Erroneous gene model prediction.Curated

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 conflicti128K → E in AAI55757 (Ref. 3) Curated1
Sequence conflicti230G → S in ABM86968 (PubMed:17543297).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

More...
DDBJi
Links Updated
EF030482 mRNA Translation: ABM86968.1
CT990639 Genomic DNA Translation: CAQ13607.1
CR545472 Genomic DNA Translation: CAN88496.1 Sequence problems.
BX323062 Genomic DNA No translation available.
BC129226 mRNA Translation: AAI29227.1
BC155756 mRNA Translation: AAI55757.1

NCBI Reference Sequences

More...
RefSeqi
NP_001074095.1, NM_001080626.1
XP_009299828.1, XM_009301553.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSDART00000064701; ENSDARP00000064700; ENSDARG00000044074
ENSDART00000144013; ENSDARP00000118755; ENSDARG00000044074
ENSDART00000184129; ENSDARP00000146651; ENSDARG00000044074
ENSDART00000185815; ENSDARP00000157626; ENSDARG00000044074

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
791144

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dre:791144

<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
EF030482 mRNA Translation: ABM86968.1
CT990639 Genomic DNA Translation: CAQ13607.1
CR545472 Genomic DNA Translation: CAN88496.1 Sequence problems.
BX323062 Genomic DNA No translation available.
BC129226 mRNA Translation: AAI29227.1
BC155756 mRNA Translation: AAI55757.1
RefSeqiNP_001074095.1, NM_001080626.1
XP_009299828.1, XM_009301553.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000118755

Proteomic databases

PaxDbiA1L1V4
PRIDEiA1L1V4

Genome annotation databases

EnsembliENSDART00000064701; ENSDARP00000064700; ENSDARG00000044074
ENSDART00000144013; ENSDARP00000118755; ENSDARG00000044074
ENSDART00000184129; ENSDARP00000146651; ENSDARG00000044074
ENSDART00000185815; ENSDARP00000157626; ENSDARG00000044074
GeneIDi791144
KEGGidre:791144

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
791144
ZFINiZDB-GENE-050208-29 loxl2b

Phylogenomic databases

eggNOGiENOG410IE2X Eukaryota
ENOG410XSN1 LUCA
GeneTreeiENSGT00940000155874
HOGENOMiHOG000220841
InParanoidiA1L1V4
KOiK00280
OMAiWYWHGNI
OrthoDBi815466at2759
TreeFamiTF326061

Enzyme and pathway databases

BRENDAi1.4.3.13 928
ReactomeiR-DRE-1566948 Elastic fibre formation
R-DRE-2243919 Crosslinking of collagen fibrils

Miscellaneous databases

Protein Ontology

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PROi
PR:A1L1V4

Gene expression databases

BgeeiENSDARG00000044074 Expressed in 22 organ(s), highest expression level in head

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, 2 hits
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 nameiLOL2B_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: A1L1V4
Secondary accession number(s): A5WUR2, A6MH31, A9JRQ9
<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_and_isoforms">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: February 6, 2007
Last modified: December 11, 2019
This is version 104 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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