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Q08397

- LOXL1_HUMAN

UniProt

Q08397 - LOXL1_HUMAN

Protein

Lysyl oxidase homolog 1

Gene

LOXL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    Active on elastin and collagen substrates.By similarity

    Cofactori

    Copper.By similarity
    Contains 1 lysine tyrosylquinone.By similarity

    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

    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. extracellular space Source: UniProtKB-SubCell
    3. proteinaceous extracellular matrix Source: Ensembl

    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

    ArrayExpressiQ08397.
    BgeeiQ08397.
    CleanExiHS_LOXL1.
    GenevestigatoriQ08397.

    Organism-specific databases

    HPAiHPA042111.

    Interactioni

    Protein-protein interaction databases

    BioGridi110200. 3 interactions.
    IntActiQ08397. 2 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.
    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

    MALARGSRQL GALVWGACLC VLVHGQQAQP GQGSDPARWR QLIQWENNGQ    50
    VYSLLNSGSE YVPAGPQRSE SSSRVLLAGA PQAQQRRSHG SPRRRQAPSL 100
    PLPGRVGSDT VRGQARHPFG FGQVPDNWRE VAVGDSTGMA RARTSVSQQR 150
    HGGSASSVSA SAFASTYRQQ PSYPQQFPYP QAPFVSQYEN YDPASRTYDQ 200
    GFVYYRPAGG GVGAGAAAVA SAGVIYPYQP RARYEEYGGG EELPEYPPQG 250
    FYPAPERPYV PPPPPPPDGL DRRYSHSLYS EGTPGFEQAY PDPGPEAAQA 300
    HGGDPRLGWY PPYANPPPEA YGPPRALEPP YLPVRSSDTP PPGGERNGAQ 350
    QGRLSVGSVY RPNQNGRGLP DLVPDPNYVQ ASTYVQRAHL YSLRCAAEEK 400
    CLASTAYAPE ATDYDVRVLL RFPQRVKNQG TADFLPNRPR HTWEWHSCHQ 450
    HYHSMDEFSH YDLLDAATGK KVAEGHKASF CLEDSTCDFG NLKRYACTSH 500
    TQGLSPGCYD TYNADIDCQW IDITDVQPGN YILKVHVNPK YIVLESDFTN 550
    NVVRCNIHYT GRYVSATNCK IVQS 574
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 2 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.
    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

    ArrayExpressi Q08397.
    Bgeei Q08397.
    CleanExi HS_LOXL1.
    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

    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: October 1, 2014
    This is version 127 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