Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q08397

- LOXL1_HUMAN

UniProt

Q08397 - LOXL1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Lysyl oxidase homolog 1

Gene

LOXL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Active on elastin and collagen substrates.By similarity

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi449 – 4491CopperSequence Analysis
Metal bindingi451 – 4511CopperSequence Analysis
Metal bindingi453 – 4531CopperSequence Analysis

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor Source: Ensembl

GO - Biological processi

  1. extracellular matrix organization Source: Reactome
  2. oxidation-reduction process Source: UniProtKB
  3. protein deamination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_150206. Crosslinking of collagen fibrils.
REACT_150366. Elastic fibre formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysyl oxidase homolog 1 (EC:1.4.3.-)
Alternative name(s):
Lysyl oxidase-like protein 1
Short name:
LOL
Gene namesi
Name:LOXL1
Synonyms:LOXL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:6665. LOXL1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. proteinaceous extracellular matrix Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Exfoliation syndrome (XFS) [MIM:177650]: A disorder characterized by accumulation of abnormal fibrillar deposits in the anterior segment of the eye. In addition to being a cause of glaucoma and glaucomatous optic neuropathy, exfoliation syndrome has also been associated with lens zonule weakness, cataract formation, and systemic vascular complications due to deposition of exfoliation material in extraocular tissues.2 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Susceptibility to exfoliation syndrome is conferred by a risk haplotype that includes two LOXL1 coding non-synonymous SNPs (Arg141Leu and Gly153Asp) and one intronic SNP. Arg141Leu and Gly153Asp are sufficient to confer disease susceptibility in some populations.

Keywords - Diseasei

Glaucoma

Organism-specific databases

MIMi177650. phenotype.
PharmGKBiPA30428.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Propeptidei26 – 9469By similarityPRO_0000018528Add
BLAST
Chaini95 – 574480Lysyl oxidase homolog 1PRO_0000018529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi395 ↔ 401By similarity
Disulfide bondi448 ↔ 497By similarity
Cross-linki477 ↔ 512Lysine tyrosylquinone (Lys-Tyr); alternateBy similarity
Disulfide bondi481 ↔ 487By similarity
Disulfide bondi508 ↔ 518By similarity
Modified residuei512 – 51212',4',5'-topaquinone; alternateBy similarity
Disulfide bondi555 ↔ 569By 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.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, LTQ, TPQ

Proteomic databases

PaxDbiQ08397.
PRIDEiQ08397.

PTM databases

PhosphoSiteiQ08397.

Expressioni

Tissue specificityi

Expressed in ocular tissues including the iris, ciliary body, lens and optic nerve. Not detected in the retina.1 Publication

Gene expression databases

BgeeiQ08397.
CleanExiHS_LOXL1.
ExpressionAtlasiQ08397. baseline and differential.
GenevestigatoriQ08397.

Organism-specific databases

HPAiHPA042111.

Interactioni

Protein-protein interaction databases

BioGridi110200. 3 interactions.
IntActiQ08397. 4 interactions.
STRINGi9606.ENSP00000261921.

Structurei

3D structure databases

ProteinModelPortaliQ08397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 574205Lysyl-oxidase likeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi261 – 2677Poly-Pro

Sequence similaritiesi

Belongs to the lysyl oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77510.
GeneTreeiENSGT00760000119251.
HOGENOMiHOG000234262.
HOVERGENiHBG000226.
InParanoidiQ08397.
KOiK14678.
OMAiQGYVYYR.
OrthoDBiEOG7SN8C6.
PhylomeDBiQ08397.
TreeFamiTF326061.

Family and domain databases

InterProiIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
[Graphical view]
PfamiPF01186. Lysyl_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00074. LYSYLOXIDASE.
PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q08397-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALARGSRQL GALVWGACLC VLVHGQQAQP GQGSDPARWR QLIQWENNGQ
60 70 80 90 100
VYSLLNSGSE YVPAGPQRSE SSSRVLLAGA PQAQQRRSHG SPRRRQAPSL
110 120 130 140 150
PLPGRVGSDT VRGQARHPFG FGQVPDNWRE VAVGDSTGMA RARTSVSQQR
160 170 180 190 200
HGGSASSVSA SAFASTYRQQ PSYPQQFPYP QAPFVSQYEN YDPASRTYDQ
210 220 230 240 250
GFVYYRPAGG GVGAGAAAVA SAGVIYPYQP RARYEEYGGG EELPEYPPQG
260 270 280 290 300
FYPAPERPYV PPPPPPPDGL DRRYSHSLYS EGTPGFEQAY PDPGPEAAQA
310 320 330 340 350
HGGDPRLGWY PPYANPPPEA YGPPRALEPP YLPVRSSDTP PPGGERNGAQ
360 370 380 390 400
QGRLSVGSVY RPNQNGRGLP DLVPDPNYVQ ASTYVQRAHL YSLRCAAEEK
410 420 430 440 450
CLASTAYAPE ATDYDVRVLL RFPQRVKNQG TADFLPNRPR HTWEWHSCHQ
460 470 480 490 500
HYHSMDEFSH YDLLDAATGK KVAEGHKASF CLEDSTCDFG NLKRYACTSH
510 520 530 540 550
TQGLSPGCYD TYNADIDCQW IDITDVQPGN YILKVHVNPK YIVLESDFTN
560 570
NVVRCNIHYT GRYVSATNCK IVQS
Length:574
Mass (Da):63,110
Last modified:February 26, 2008 - v2
Checksum:i7570FEFB3E09066D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411R → L Associated with exfoliation syndrome in the presence of D-153. 4 Publications
Corresponds to variant rs1048661 [ dbSNP | Ensembl ].
VAR_028436
Natural varianti153 – 1531G → D Associated with exfoliation syndrome in the presence of L-141. 3 Publications
Corresponds to variant rs3825942 [ dbSNP | Ensembl ].
VAR_022135

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21186 mRNA. Translation: AAA50162.1.
U24389
, U24395, U24394, U24393, U24391, U24390 Genomic DNA. Translation: AAA68940.1.
AK314222 mRNA. Translation: BAG36895.1.
AC108137 Genomic DNA. No translation available.
BC015090 mRNA. Translation: AAH15090.1.
BC068542 mRNA. Translation: AAH68542.1.
CCDSiCCDS10253.1.
PIRiA48501.
RefSeqiNP_005567.2. NM_005576.2.
UniGeneiHs.65436.

Genome annotation databases

EnsembliENST00000261921; ENSP00000261921; ENSG00000129038.
GeneIDi4016.
KEGGihsa:4016.
UCSCiuc002awc.1. human.

Polymorphism databases

DMDMi189031484.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21186 mRNA. Translation: AAA50162.1 .
U24389
, U24395 , U24394 , U24393 , U24391 , U24390 Genomic DNA. Translation: AAA68940.1 .
AK314222 mRNA. Translation: BAG36895.1 .
AC108137 Genomic DNA. No translation available.
BC015090 mRNA. Translation: AAH15090.1 .
BC068542 mRNA. Translation: AAH68542.1 .
CCDSi CCDS10253.1.
PIRi A48501.
RefSeqi NP_005567.2. NM_005576.2.
UniGenei Hs.65436.

3D structure databases

ProteinModelPortali Q08397.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110200. 3 interactions.
IntActi Q08397. 4 interactions.
STRINGi 9606.ENSP00000261921.

PTM databases

PhosphoSitei Q08397.

Polymorphism databases

DMDMi 189031484.

Proteomic databases

PaxDbi Q08397.
PRIDEi Q08397.

Protocols and materials databases

DNASUi 4016.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261921 ; ENSP00000261921 ; ENSG00000129038 .
GeneIDi 4016.
KEGGi hsa:4016.
UCSCi uc002awc.1. human.

Organism-specific databases

CTDi 4016.
GeneCardsi GC15P074218.
HGNCi HGNC:6665. LOXL1.
HPAi HPA042111.
MIMi 153456. gene.
177650. phenotype.
neXtProti NX_Q08397.
PharmGKBi PA30428.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG77510.
GeneTreei ENSGT00760000119251.
HOGENOMi HOG000234262.
HOVERGENi HBG000226.
InParanoidi Q08397.
KOi K14678.
OMAi QGYVYYR.
OrthoDBi EOG7SN8C6.
PhylomeDBi Q08397.
TreeFami TF326061.

Enzyme and pathway databases

Reactomei REACT_150206. Crosslinking of collagen fibrils.
REACT_150366. Elastic fibre formation.

Miscellaneous databases

ChiTaRSi LOXL1. human.
GeneWikii LOXL1.
GenomeRNAii 4016.
NextBioi 15756.
PROi Q08397.
SOURCEi Search...

Gene expression databases

Bgeei Q08397.
CleanExi HS_LOXL1.
ExpressionAtlasi Q08397. baseline and differential.
Genevestigatori Q08397.

Family and domain databases

InterProi IPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
[Graphical view ]
Pfami PF01186. Lysyl_oxidase. 1 hit.
[Graphical view ]
PRINTSi PR00074. LYSYLOXIDASE.
PROSITEi PS00926. LYSYL_OXIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human cDNA with a predicted protein similar to lysyl oxidase maps to chromosome 15q24-q25."
    Kenyon K., Modi W.S., Contente S., Friedman R.M.
    J. Biol. Chem. 268:18435-18437(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-141.
    Tissue: Skin fibroblast.
  2. "Structure of the human lysyl oxidase-like gene."
    Kenyon K., Sathya G., Contente S., Friedman R.M.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-141.
    Tissue: Placenta.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-153.
    Tissue: Amygdala.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-153.
    Tissue: Lung and Placenta.
  6. Cited for: VARIANTS LEU-141 AND ASP-153, SUSCEPTIBILITY TO XFS.
  7. "Ancestral LOXL1 variants are associated with pseudoexfoliation in Caucasian Australians but with markedly lower penetrance than in Nordic people."
    Hewitt A.W., Sharma S., Burdon K.P., Wang J.J., Baird P.N., Dimasi D.P., Mackey D.A., Mitchell P., Craig J.E.
    Hum. Mol. Genet. 17:710-716(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF VARIANTS LEU-141 AND ASP-153 WITH EXFOLIATION SYNDROME, TISSUE SPECIFICITY.
  8. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: ASSOCIATION OF VARIANTS LEU-141 AND ASP-153 WITH EXFOLIATION SYNDROME.

Entry informationi

Entry nameiLOXL1_HUMAN
AccessioniPrimary (citable) accession number: Q08397
Secondary accession number(s): Q6NUL3, Q96BW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 26, 2008
Last modified: November 26, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3