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P58022

- LOXL2_MOUSE

UniProt

P58022 - LOXL2_MOUSE

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Protein
Lysyl oxidase homolog 2
Gene
Loxl2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). When secreted in extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. When nuclear, acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin, probably by mediating deamination of histone H3 By similarity. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.1 Publication

Catalytic activityi

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

Cofactori

Copper By similarity.
Contains 1 lysine tyrosylquinone By similarity.

Enzyme regulationi

Specifically inhibited by a mouse monoclonal antibody AB0023, inhibition occurs in a non-competitive manner By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi628 – 6281Copper Reviewed prediction
Metal bindingi630 – 6301Copper Reviewed prediction
Metal bindingi632 – 6321Copper Reviewed prediction

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. copper ion binding Source: InterPro
  3. methylated histone binding Source: UniProtKB
  4. oligosaccharide binding Source: UniProtKB
  5. protein-lysine 6-oxidase activity Source: UniProtKB
  6. scavenger receptor activity Source: InterPro
  7. transcription corepressor activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cellular protein modification process Source: UniProtKB
  2. collagen fibril organization Source: UniProtKB
  3. endothelial cell migration Source: UniProtKB
  4. endothelial cell proliferation Source: UniProtKB
  5. epithelial to mesenchymal transition Source: UniProtKB
  6. histone modification Source: UniProtKB
  7. negative regulation of transcription, DNA-templated Source: UniProtKB
  8. oxidation-reduction process Source: UniProtKB
  9. positive regulation of chondrocyte differentiation Source: UniProtKB
  10. protein deamination Source: UniProtKB
  11. response to copper ion Source: UniProtKB
  12. response to hypoxia Source: UniProtKB
  13. sprouting angiogenesis Source: UniProtKB
  14. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Oxidoreductase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lysyl oxidase homolog 2 (EC:1.4.3.13)
Alternative name(s):
Lysyl oxidase-like protein 2
Gene namesi
Name:Loxl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:2137913. Loxl2.

Subcellular locationi

Secretedextracellular spaceextracellular matrixbasement membrane By similarity. Nucleus By similarity. Chromosome By similarity
Note: Associated with chromatin By similarity. It is unclear how LOXL2 is nuclear: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, different reports confirmed the intracellular location and its key role in transcription regulation.

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. chromosome Source: UniProtKB-SubCell
  3. extracellular space Source: UniProtKB
  4. membrane Source: InterPro
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Chromosome, Extracellular matrix, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed prediction
Add
BLAST
Chaini26 – 776751Lysyl oxidase homolog 2
PRO_0000042854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi87 ↔ 151 By similarity
Disulfide bondi100 ↔ 161 By similarity
Disulfide bondi131 ↔ 141 By similarity
Disulfide bondi221 ↔ 294 By similarity
Disulfide bondi234 ↔ 304 By similarity
Glycosylationi267 – 2671N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi268 ↔ 278 By similarity
Glycosylationi291 – 2911N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi354 ↔ 417 By similarity
Disulfide bondi367 ↔ 427 By similarity
Disulfide bondi398 ↔ 408 By similarity
Glycosylationi458 – 4581N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi467 ↔ 532 By similarity
Disulfide bondi480 ↔ 545 By similarity
Disulfide bondi514 ↔ 524 By similarity
Disulfide bondi575 ↔ 581 By similarity
Disulfide bondi627 ↔ 675 By similarity
Glycosylationi646 – 6461N-linked (GlcNAc...) Reviewed prediction
Cross-linki655 ↔ 691Lysine tyrosylquinone (Lys-Tyr) By similarity
Disulfide bondi659 ↔ 665 By similarity
Disulfide bondi687 ↔ 697 By similarity
Modified residuei691 – 69112',4',5'-topaquinone By similarity
Disulfide bondi734 ↔ 748 By similarity

Post-translational modificationi

The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine By similarity.
N-glycosylated. N-glycosylation on Asn-458 and Asn-646 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, LTQ, TPQ

Proteomic databases

PRIDEiP58022.

PTM databases

PhosphoSiteiP58022.

Expressioni

Tissue specificityi

Ubiquitous. Highest expression in skin, lung and thymus. Present in chondrocytes: mainly expressed by chondrocytes in healing fractures and in epiphyseal growth plates (at protein level).1 Publication

Inductioni

Strongly induced in hypoxia.1 Publication

Gene expression databases

BgeeiP58022.
CleanExiMM_LOXL2.
GenevestigatoriP58022.

Interactioni

Subunit structurei

Component of some chromatin repressor complex. Interacts with SNAI1 By similarity.

Protein-protein interaction databases

IntActiP58022. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP58022.
SMRiP58022. Positions 71-162, 329-428, 438-525.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 162102SRCR 1
Add
BLAST
Domaini191 – 305115SRCR 2
Add
BLAST
Domaini329 – 428100SRCR 3
Add
BLAST
Domaini438 – 546109SRCR 4
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni550 – 753204Lysyl-oxidase like By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the lysyl oxidase family.
Contains 4 SRCR domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG40770.
GeneTreeiENSGT00740000115380.
HOGENOMiHOG000220841.
HOVERGENiHBG052336.
InParanoidiP58022.
KOiK00280.
OMAiGHEWSEV.
OrthoDBiEOG7SN8C6.
PhylomeDBiP58022.
TreeFamiTF326061.

Family and domain databases

Gene3Di3.10.250.10. 4 hits.
InterProiIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
[Graphical view]
PfamiPF01186. Lysyl_oxidase. 1 hit.
PF00530. SRCR. 4 hits.
[Graphical view]
PRINTSiPR00074. LYSYLOXIDASE.
PR00258. SPERACTRCPTR.
SMARTiSM00202. SR. 4 hits.
[Graphical view]
SUPFAMiSSF56487. SSF56487. 4 hits.
PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
PS00420. SRCR_1. 2 hits.
PS50287. SRCR_2. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P58022-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MELHFGSCLS GCLALLVLLP SLSLAQYEGW PYQLQYPEYF QQPAPEHHQR    50
QVPSDVVKIQ VRLAGQKRKH NEGRVEVYYE GQWGTVCDDD FSIHAAHVVC 100
RQVGYVEAKS WAASSSYGPG EGPIWLDNIY CTGKESTLAS CSSNGWGVTD 150
CKHTEDVGVV CSEKRIPGFK FDNSLINQIE SLNIQVEDIR IRPILSAFRH 200
RKPVTEGYVE VKEGKAWKQI CNKHWTAKNS HVVCGMFGFP AEKTYNPKAY 250
KTFASRRKLR YWKFSMNCTG TEAHISSCKL GPSVTRDPVK NATCENGQPA 300
VVSCVPSQIF SPDGPSRFRK AYKPEQPLVR LRGGAQVGEG RVEVLKNGEW 350
GTICDDKWDL VSASVVCREL GFGTAKEAIT GSRLGQGIGP IHLNEVQCTG 400
TEKSIIDCKF NTESQGCNHE EDAGVRCNIP IMGFQKKVRL NGGRNPYEGR 450
VEVLTERNGS LVWGTVCGQN WGIVEAMVVC RQLGLGFASN AFQETWYWHG 500
NIFANNVVMS GVKCSGTELS LAHCRHDEEV ACPEGGVRFG AGVACSETAP 550
DLVLNAEIVQ QTAYLEDRPM SLLQCAMEEN CLSASAVHTD PTRGHRRLLR 600
FSSQIHNNGQ SDFRPKNGRH AWIWHDCHRH YHSMEVFTYY DLLSLNGTKV 650
AEGHKASFCL EDTECEGDIQ KSYECANFGE QGITMGCWDM YRHDIDCQWI 700
DITDVPPGDY LFQVVINPNY EVPESDFSNN IMKCRSRYDG YRIWMYNCHV 750
GGAFSEETEQ KFEHFSGLLN NQLSVQ 776
Length:776
Mass (Da):87,003
Last modified:November 22, 2005 - v2
Checksum:i9DE55C6F37DE5EEF
GO
Isoform 2 (identifier: P58022-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     714-727: VVINPNYEVPESDF → PSNRVLVRAGQTPY
     728-776: Missing.

Note: No experimental confirmation available.

Show »
Length:727
Mass (Da):81,168
Checksum:i9A4A912D0BDA9FCC
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei714 – 72714VVINP…PESDF → PSNRVLVRAGQTPY in isoform 2.
VSP_016231Add
BLAST
Alternative sequencei728 – 77649Missing in isoform 2.
VSP_016232Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti320 – 3201K → E in BAC32186. 1 Publication
Sequence conflicti558 – 5603IVQ → HEE in AAF29046. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK034957 mRNA. Translation: BAC28894.1.
AK045019 mRNA. Translation: BAC32186.1.
AK081898 mRNA. Translation: BAC38364.1.
AK145323 mRNA. Translation: BAE26367.1.
AK159386 mRNA. Translation: BAE35041.1.
AF117951 mRNA. Translation: AAF29046.1.
CCDSiCCDS27241.1. [P58022-1]
RefSeqiNP_201582.2. NM_033325.2. [P58022-1]
XP_003688982.2. XM_003688934.3. [P58022-2]
XP_006519810.1. XM_006519747.1. [P58022-1]
UniGeneiMm.116714.

Genome annotation databases

EnsembliENSMUST00000022660; ENSMUSP00000022660; ENSMUSG00000034205. [P58022-1]
ENSMUST00000100420; ENSMUSP00000097987; ENSMUSG00000034205. [P58022-1]
GeneIDi100862072.
94352.
KEGGimmu:100862072.
mmu:94352.
UCSCiuc007umn.3. mouse. [P58022-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK034957 mRNA. Translation: BAC28894.1 .
AK045019 mRNA. Translation: BAC32186.1 .
AK081898 mRNA. Translation: BAC38364.1 .
AK145323 mRNA. Translation: BAE26367.1 .
AK159386 mRNA. Translation: BAE35041.1 .
AF117951 mRNA. Translation: AAF29046.1 .
CCDSi CCDS27241.1. [P58022-1 ]
RefSeqi NP_201582.2. NM_033325.2. [P58022-1 ]
XP_003688982.2. XM_003688934.3. [P58022-2 ]
XP_006519810.1. XM_006519747.1. [P58022-1 ]
UniGenei Mm.116714.

3D structure databases

ProteinModelPortali P58022.
SMRi P58022. Positions 71-162, 329-428, 438-525.
ModBasei Search...

Protein-protein interaction databases

IntActi P58022. 1 interaction.

PTM databases

PhosphoSitei P58022.

Proteomic databases

PRIDEi P58022.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022660 ; ENSMUSP00000022660 ; ENSMUSG00000034205 . [P58022-1 ]
ENSMUST00000100420 ; ENSMUSP00000097987 ; ENSMUSG00000034205 . [P58022-1 ]
GeneIDi 100862072.
94352.
KEGGi mmu:100862072.
mmu:94352.
UCSCi uc007umn.3. mouse. [P58022-1 ]

Organism-specific databases

CTDi 4017.
MGIi MGI:2137913. Loxl2.

Phylogenomic databases

eggNOGi NOG40770.
GeneTreei ENSGT00740000115380.
HOGENOMi HOG000220841.
HOVERGENi HBG052336.
InParanoidi P58022.
KOi K00280.
OMAi GHEWSEV.
OrthoDBi EOG7SN8C6.
PhylomeDBi P58022.
TreeFami TF326061.

Miscellaneous databases

ChiTaRSi LOXL2. mouse.
NextBioi 352317.
PROi P58022.
SOURCEi Search...

Gene expression databases

Bgeei P58022.
CleanExi MM_LOXL2.
Genevestigatori P58022.

Family and domain databases

Gene3Di 3.10.250.10. 4 hits.
InterProi IPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
[Graphical view ]
Pfami PF01186. Lysyl_oxidase. 1 hit.
PF00530. SRCR. 4 hits.
[Graphical view ]
PRINTSi PR00074. LYSYLOXIDASE.
PR00258. SPERACTRCPTR.
SMARTi SM00202. SR. 4 hits.
[Graphical view ]
SUPFAMi SSF56487. SSF56487. 4 hits.
PROSITEi PS00926. LYSYL_OXIDASE. 1 hit.
PS00420. SRCR_1. 2 hits.
PS50287. SRCR_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Embryo and Head.
  2. "The mouse lysyl oxidase-like 2 gene (mLOXL2) maps to chromosome 14 and is highly expressed in skin, lung and thymus."
    Jourdan-Le Saux C., Le Saux O., Gleyzal C., Sommer P., Csiszar K.
    Matrix Biol. 19:179-183(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 558-776 (ISOFORM 1).
  3. "Lysyl oxidase-like protein-2 regulates sprouting angiogenesis and type IV collagen assembly in the endothelial basement membrane."
    Bignon M., Pichol-Thievend C., Hardouin J., Malbouyres M., Brechot N., Nasciutti L., Barret A., Teillon J., Guillon E., Etienne E., Caron M., Joubert-Caron R., Monnot C., Ruggiero F., Muller L., Germain S.
    Blood 118:3979-3989(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  4. "Lysyl oxidase-like-2 (LOXL2) is a major isoform in chondrocytes and is critically required for differentiation."
    Iftikhar M., Hurtado P., Bais M.V., Wigner N., Stephens D.N., Gerstenfeld L.C., Trackman P.C.
    J. Biol. Chem. 286:909-918(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiLOXL2_MOUSE
AccessioniPrimary (citable) accession number: P58022
Secondary accession number(s): Q8BRE6
, Q8BS86, Q8C4K0, Q9JJ39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 22, 2005
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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