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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.By similarity1 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 – 6281CopperSequence Analysis
Metal bindingi630 – 6301CopperSequence Analysis
Metal bindingi632 – 6321CopperSequence Analysis

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

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.By similarity

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. chromosome Source: UniProtKB-KW
  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 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 776751Lysyl oxidase homolog 2PRO_0000042854Add
BLAST

Amino acid modifications

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

Post-translational modificationi

The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.By similarity
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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, LTQ, TPQ

Proteomic databases

MaxQBiP58022.
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).By similarity

Protein-protein interaction databases

IntActiP58022. 1 interaction.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni550 – 753204Lysyl-oxidase likeBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the lysyl oxidase family.Curated
Contains 4 SRCR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG40770.
GeneTreeiENSGT00760000119251.
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

        10         20         30         40         50
MELHFGSCLS GCLALLVLLP SLSLAQYEGW PYQLQYPEYF QQPAPEHHQR
60 70 80 90 100
QVPSDVVKIQ VRLAGQKRKH NEGRVEVYYE GQWGTVCDDD FSIHAAHVVC
110 120 130 140 150
RQVGYVEAKS WAASSSYGPG EGPIWLDNIY CTGKESTLAS CSSNGWGVTD
160 170 180 190 200
CKHTEDVGVV CSEKRIPGFK FDNSLINQIE SLNIQVEDIR IRPILSAFRH
210 220 230 240 250
RKPVTEGYVE VKEGKAWKQI CNKHWTAKNS HVVCGMFGFP AEKTYNPKAY
260 270 280 290 300
KTFASRRKLR YWKFSMNCTG TEAHISSCKL GPSVTRDPVK NATCENGQPA
310 320 330 340 350
VVSCVPSQIF SPDGPSRFRK AYKPEQPLVR LRGGAQVGEG RVEVLKNGEW
360 370 380 390 400
GTICDDKWDL VSASVVCREL GFGTAKEAIT GSRLGQGIGP IHLNEVQCTG
410 420 430 440 450
TEKSIIDCKF NTESQGCNHE EDAGVRCNIP IMGFQKKVRL NGGRNPYEGR
460 470 480 490 500
VEVLTERNGS LVWGTVCGQN WGIVEAMVVC RQLGLGFASN AFQETWYWHG
510 520 530 540 550
NIFANNVVMS GVKCSGTELS LAHCRHDEEV ACPEGGVRFG AGVACSETAP
560 570 580 590 600
DLVLNAEIVQ QTAYLEDRPM SLLQCAMEEN CLSASAVHTD PTRGHRRLLR
610 620 630 640 650
FSSQIHNNGQ SDFRPKNGRH AWIWHDCHRH YHSMEVFTYY DLLSLNGTKV
660 670 680 690 700
AEGHKASFCL EDTECEGDIQ KSYECANFGE QGITMGCWDM YRHDIDCQWI
710 720 730 740 750
DITDVPPGDY LFQVVINPNY EVPESDFSNN IMKCRSRYDG YRIWMYNCHV
760 770
GGAFSEETEQ KFEHFSGLLN NQLSVQ
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti320 – 3201K → E in BAC32186. (PubMed:16141072)Curated
Sequence conflicti558 – 5603IVQ → HEE in AAF29046. (PubMed:10842102)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei714 – 72714VVINP…PESDF → PSNRVLVRAGQTPY in isoform 2. 1 PublicationVSP_016231Add
BLAST
Alternative sequencei728 – 77649Missing in isoform 2. 1 PublicationVSP_016232Add
BLAST

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...
MobiDBi Search...

Protein-protein interaction databases

IntActi P58022. 1 interaction.

PTM databases

PhosphoSitei P58022.

Proteomic databases

MaxQBi P58022.
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 ENSGT00760000119251.
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: October 29, 2014
This is version 114 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