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Protein

Lysyl oxidase homolog 3

Gene

LOXL3

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

Functioni

Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins (PubMed:17018530, PubMed:28065600). Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin (PubMed:17018530). Required for somite boundary formation by catalyzing oxidation of fibronectin (FN1), enhancing integrin signaling in myofibers and their adhesion to the myotendinous junction (MTJ) (By similarity). Acts as a regulator of inflammatory response by inhibiting differentiation of naive CD4+ T-cells into T-helper Th17 or regulatory T-cells (Treg): acts by interacting with STAT3 in the nucleus and catalyzing both deacetylation and oxidation of lysine residues on STAT3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (PubMed:28065600). Also able to catalyze deacetylation of lysine residues on STAT3 (PubMed:28065600).By similarity2 Publications
Isoform 1: Shows protein-lysine 6-oxidase activity toward elastin and different types of collagens, with the highest activity toward collagen type VIII (PubMed:17018530).1 Publication
Isoform 2: Shows protein-lysine 6-oxidase activity toward elastin and different types of collagens, with the highest activity toward collagen type IV (PubMed:17018530).1 Publication

Catalytic activityi

[Protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2.1 Publication
[protein]-N(6)-acetyl-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + acetamide + H2O2.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarity
  • lysine tyrosylquinone residueBy similarityNote: Contains 1 lysine tyrosylquinone.By similarity

Kineticsi

kcat is 0.058 sec(-1) with STAT3 acetylated at 'Lys-685' (for deacetylation activity). kcat is 0.022 sec(-1) with STAT3 acetylated at 'Lys-685' (for lysine 6-oxidase activity).1 Publication
  1. KM=6.72 µM for STAT3 acetylated at 'Lys-685' (for deacetylation activity)1 Publication
  2. KM=1.59 µM for STAT3 acetylated at 'Lys-685' (for lysine 6-oxidase activity)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi607CopperSequence analysis1
    Metal bindingi609CopperSequence analysis1
    Metal bindingi611CopperSequence analysis1

    GO - Molecular functioni

    • copper ion binding Source: UniProtKB
    • fibronectin binding Source: UniProtKB
    • protein-lysine 6-oxidase activity Source: UniProtKB
    • scavenger receptor activity Source: InterPro

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    Biological processInflammatory response
    LigandCopper, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.4.3.13. 2681.
    ReactomeiR-HSA-1566948. Elastic fibre formation.
    R-HSA-2243919. Crosslinking of collagen fibrils.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysyl oxidase homolog 3Curated (EC:1.4.3.-1 Publication, EC:1.4.3.131 Publication)
    Alternative name(s):
    Lysyl oxidase-like protein 31 Publication
    Gene namesi
    Name:LOXL31 PublicationImported
    Synonyms:LOXL1 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:13869. LOXL3.

    Subcellular locationi

    Isoform 2 :
    • Cytoplasm 1 Publication
    • Secretedextracellular space 1 Publication

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • extracellular region Source: UniProtKB
    • extracellular space Source: UniProtKB
    • membrane Source: InterPro
    • nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Defects in LOXL3 are found in a family with an autosomal recessive form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence and sensorineural deafness (PubMed:25663169). Pierre Robin sequence includes an opening in the roof of the mouth (a cleft palate) (PubMed:25663169). The degree of hearing loss varies among affected individuals and may become more severe over time (PubMed:25663169). Syndrome expressivity is variable (PubMed:25663169). Ocular disorders include non-progressive myopia with associated chorioretinal degeneration (PubMed:25663169). Defects in LOXL3 are found in another family with early-onset high myopia (PubMed:26957899). The disease may be caused by mutations affecting the gene represented in this entry (PubMed:25663169, PubMed:26957899).2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi83C → A: Impaired ability to mediate deacetylation of STAT3; when associated with A-214; A-345 and A-459. 1 Publication1
    Mutagenesisi214C → A: Impaired ability to mediate deacetylation of STAT3; when associated with A-83; A-345 and A-459. 1 Publication1
    Mutagenesisi345C → A: Impaired ability to mediate deacetylation of STAT3; when associated with A-83; A-214 and A-459. 1 Publication1
    Mutagenesisi376C → A: Impaired ability to mediate deacetylation of STAT3; when associated with A-446 and A-492. 1 Publication1
    Mutagenesisi446C → A: Impaired ability to mediate deacetylation of STAT3; when associated with A-376 and A-492. 1 Publication1
    Mutagenesisi459C → A: Impaired ability to mediate deacetylation of STAT3; when associated with A-83; A-214 and A-345. 1 Publication1
    Mutagenesisi492C → A: Impaired ability to mediate deacetylation of STAT3; when associated with A-376 and A-446. 1 Publication1
    Mutagenesisi607 – 609HGH → QGQ: Impaired ability to mediate deacetylation of STAT3. 1 Publication3

    Keywords - Diseasei

    Deafness, Stickler syndrome

    Organism-specific databases

    DisGeNETi84695.
    OpenTargetsiENSG00000115318.
    PharmGKBiPA30430.

    Polymorphism and mutation databases

    BioMutaiLOXL3.
    DMDMi14916616.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 25Sequence analysisAdd BLAST25
    ChainiPRO_000001853326 – 753Lysyl oxidase homolog 3Add BLAST728

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi70 ↔ 134PROSITE-ProRule annotation
    Disulfide bondi83 ↔ 144PROSITE-ProRule annotation
    Glycosylationi111N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi114 ↔ 124PROSITE-ProRule annotation
    Disulfide bondi201 ↔ 271PROSITE-ProRule annotation
    Disulfide bondi214 ↔ 281PROSITE-ProRule annotation
    Disulfide bondi248 ↔ 258PROSITE-ProRule annotation
    Glycosylationi266N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi332 ↔ 396PROSITE-ProRule annotation
    Disulfide bondi345 ↔ 406PROSITE-ProRule annotation
    Disulfide bondi376 ↔ 386PROSITE-ProRule annotation
    Glycosylationi390N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi446 ↔ 511PROSITE-ProRule annotation
    Disulfide bondi459 ↔ 524PROSITE-ProRule annotation
    Glycosylationi481N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi492 ↔ 502PROSITE-ProRule annotation
    Disulfide bondi554 ↔ 560PROSITE-ProRule annotation
    Disulfide bondi606 ↔ 654PROSITE-ProRule annotation
    Glycosylationi625N-linked (GlcNAc...)Sequence analysis1
    Cross-linki634 ↔ 670Lysine tyrosylquinone (Lys-Tyr)By similarity
    Disulfide bondi638 ↔ 644PROSITE-ProRule annotation
    Disulfide bondi666 ↔ 676PROSITE-ProRule annotation
    Modified residuei6702',4',5'-topaquinoneBy similarity1
    Disulfide bondi713 ↔ 727PROSITE-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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, LTQ, TPQ

    Proteomic databases

    EPDiP58215.
    PaxDbiP58215.
    PeptideAtlasiP58215.
    PRIDEiP58215.

    PTM databases

    iPTMnetiP58215.
    PhosphoSitePlusiP58215.

    Expressioni

    Tissue specificityi

    Isoform 1: Predominantly detected in the heart, placenta, lung, and small intestine (PubMed:17018530). Isoform 2: Highly detected in the kidney, pancreas, spleen, and thymus, and is absent in lung (PubMed:17018530). In eye, present in all layers of corneas as well as in the limbus and conjunctiva (at protein level) (PubMed:26218558).2 Publications

    Gene expression databases

    BgeeiENSG00000115318.
    CleanExiHS_LOXL3.
    ExpressionAtlasiP58215. baseline and differential.
    GenevisibleiP58215. HS.

    Organism-specific databases

    HPAiHPA035281.

    Interactioni

    Subunit structurei

    Interacts with STAT3 (PubMed:28065600).1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi124210. 11 interactors.
    IntActiP58215. 3 interactors.
    MINTiMINT-1427254.
    STRINGi9606.ENSP00000264094.

    Structurei

    3D structure databases

    ProteinModelPortaliP58215.
    SMRiP58215.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini44 – 145SRCR 1PROSITE-ProRule annotationAdd BLAST102
    Domaini169 – 282SRCR 2PROSITE-ProRule annotationAdd BLAST114
    Domaini307 – 407SRCR 3PROSITE-ProRule annotationAdd BLAST101
    Domaini417 – 525SRCR 4PROSITE-ProRule annotationAdd BLAST109

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni529 – 732Lysyl-oxidase likeAdd BLAST204

    Sequence similaritiesi

    Belongs to the lysyl oxidase family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiENOG410IE2X. Eukaryota.
    ENOG410XSN1. LUCA.
    GeneTreeiENSGT00870000136394.
    HOGENOMiHOG000220841.
    HOVERGENiHBG052336.
    InParanoidiP58215.
    KOiK00280.
    OMAiTWYWDSG.
    OrthoDBiEOG091G02XD.
    PhylomeDBiP58215.
    TreeFamiTF326061.

    Family and domain databases

    Gene3Di3.10.250.10. 1 hit.
    InterProiView protein in InterPro
    IPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    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. 1 hit.
    PS50287. SRCR_2. 4 hits.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P58215-1) [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
    MRPVSVWQWS PWGLLLCLLC SSCLGSPSPS TGPEKKAGSQ GLRFRLAGFP
    60 70 80 90 100
    RKPYEGRVEI QRAGEWGTIC DDDFTLQAAH ILCRELGFTE ATGWTHSAKY
    110 120 130 140 150
    GPGTGRIWLD NLSCSGTEQS VTECASRGWG NSDCTHDEDA GVICKDQRLP
    160 170 180 190 200
    GFSDSNVIEV EHHLQVEEVR IRPAVGWGRR PLPVTEGLVE VRLPDGWSQV
    210 220 230 240 250
    CDKGWSAHNS HVVCGMLGFP SEKRVNAAFY RLLAQRQQHS FGLHGVACVG
    260 270 280 290 300
    TEAHLSLCSL EFYRANDTAR CPGGGPAVVS CVPGPVYAAS SGQKKQQQSK
    310 320 330 340 350
    PQGEARVRLK GGAHPGEGRV EVLKASTWGT VCDRKWDLHA ASVVCRELGF
    360 370 380 390 400
    GSAREALSGA RMGQGMGAIH LSEVRCSGQE LSLWKCPHKN ITAEDCSHSQ
    410 420 430 440 450
    DAGVRCNLPY TGAETRIRLS GGRSQHEGRV EVQIGGPGPL RWGLICGDDW
    460 470 480 490 500
    GTLEAMVACR QLGLGYANHG LQETWYWDSG NITEVVMSGV RCTGTELSLD
    510 520 530 540 550
    QCAHHGTHIT CKRTGTRFTA GVICSETASD LLLHSALVQE TAYIEDRPLH
    560 570 580 590 600
    MLYCAAEENC LASSARSANW PYGHRRLLRF SSQIHNLGRA DFRPKAGRHS
    610 620 630 640 650
    WVWHECHGHY HSMDIFTHYD ILTPNGTKVA EGHKASFCLE DTECQEDVSK
    660 670 680 690 700
    RYECANFGEQ GITVGCWDLY RHDIDCQWID ITDVKPGNYI LQVVINPNFE
    710 720 730 740 750
    VAESDFTNNA MKCNCKYDGH RIWVHNCHIG DAFSEEANRR FERYPGQTSN

    QII
    Length:753
    Mass (Da):83,166
    Last modified:July 11, 2001 - v1
    Checksum:i582C46DA25E05A69
    GO
    Isoform 2 (identifier: P58215-2) [UniParc]FASTAAdd to basket
    Also known as: LOXL3-sv11 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         1-361: Missing.

    Note: Misses three SRCR domains.
    Show »
    Length:392
    Mass (Da):44,049
    Checksum:iEF83ED2AB3CE9EC0
    GO
    Isoform 3 (identifier: P58215-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         159-303: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:608
    Mass (Da):67,445
    Checksum:iB33B22A417B184DD
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti159E → K in AAK91134 (PubMed:11334717).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_050011615I → F. Corresponds to variant dbSNP:rs17010021Ensembl.1
    Natural variantiVAR_077909676C → Y Found in patients with Stickler syndrome; sporadic case; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs786204838Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0544171 – 361Missing in isoform 2. 1 PublicationAdd BLAST361
    Alternative sequenceiVSP_054418159 – 303Missing in isoform 3. 1 PublicationAdd BLAST145

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF282619 mRNA. Translation: AAK51671.1.
    AF311313 mRNA. Translation: AAK63205.1.
    AF284815 mRNA. Translation: AAK91134.1.
    DQ378059 mRNA. Translation: ABD23013.1.
    AC005033 Genomic DNA. No translation available.
    AC005041 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAW99615.1.
    CH471053 Genomic DNA. Translation: EAW99616.1.
    BC071865 mRNA. Translation: AAH71865.1.
    CCDSiCCDS1953.1. [P58215-1]
    CCDS74527.1. [P58215-3]
    RefSeqiNP_001276093.1. NM_001289164.2. [P58215-3]
    NP_001276094.1. NM_001289165.1. [P58215-2]
    NP_115992.1. NM_032603.4. [P58215-1]
    XP_011531436.1. XM_011533134.2. [P58215-1]
    XP_016860601.1. XM_017005112.1. [P58215-2]
    UniGeneiHs.469045.

    Genome annotation databases

    EnsembliENST00000264094; ENSP00000264094; ENSG00000115318. [P58215-1]
    ENST00000393937; ENSP00000377512; ENSG00000115318. [P58215-3]
    GeneIDi84695.
    KEGGihsa:84695.
    UCSCiuc002smp.3. human. [P58215-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF282619 mRNA. Translation: AAK51671.1.
    AF311313 mRNA. Translation: AAK63205.1.
    AF284815 mRNA. Translation: AAK91134.1.
    DQ378059 mRNA. Translation: ABD23013.1.
    AC005033 Genomic DNA. No translation available.
    AC005041 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAW99615.1.
    CH471053 Genomic DNA. Translation: EAW99616.1.
    BC071865 mRNA. Translation: AAH71865.1.
    CCDSiCCDS1953.1. [P58215-1]
    CCDS74527.1. [P58215-3]
    RefSeqiNP_001276093.1. NM_001289164.2. [P58215-3]
    NP_001276094.1. NM_001289165.1. [P58215-2]
    NP_115992.1. NM_032603.4. [P58215-1]
    XP_011531436.1. XM_011533134.2. [P58215-1]
    XP_016860601.1. XM_017005112.1. [P58215-2]
    UniGeneiHs.469045.

    3D structure databases

    ProteinModelPortaliP58215.
    SMRiP58215.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi124210. 11 interactors.
    IntActiP58215. 3 interactors.
    MINTiMINT-1427254.
    STRINGi9606.ENSP00000264094.

    PTM databases

    iPTMnetiP58215.
    PhosphoSitePlusiP58215.

    Polymorphism and mutation databases

    BioMutaiLOXL3.
    DMDMi14916616.

    Proteomic databases

    EPDiP58215.
    PaxDbiP58215.
    PeptideAtlasiP58215.
    PRIDEiP58215.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000264094; ENSP00000264094; ENSG00000115318. [P58215-1]
    ENST00000393937; ENSP00000377512; ENSG00000115318. [P58215-3]
    GeneIDi84695.
    KEGGihsa:84695.
    UCSCiuc002smp.3. human. [P58215-1]

    Organism-specific databases

    CTDi84695.
    DisGeNETi84695.
    GeneCardsiLOXL3.
    HGNCiHGNC:13869. LOXL3.
    HPAiHPA035281.
    MIMi607163. gene.
    neXtProtiNX_P58215.
    OpenTargetsiENSG00000115318.
    PharmGKBiPA30430.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiENOG410IE2X. Eukaryota.
    ENOG410XSN1. LUCA.
    GeneTreeiENSGT00870000136394.
    HOGENOMiHOG000220841.
    HOVERGENiHBG052336.
    InParanoidiP58215.
    KOiK00280.
    OMAiTWYWDSG.
    OrthoDBiEOG091G02XD.
    PhylomeDBiP58215.
    TreeFamiTF326061.

    Enzyme and pathway databases

    BRENDAi1.4.3.13. 2681.
    ReactomeiR-HSA-1566948. Elastic fibre formation.
    R-HSA-2243919. Crosslinking of collagen fibrils.

    Miscellaneous databases

    ChiTaRSiLOXL3. human.
    GeneWikiiLOXL3.
    GenomeRNAii84695.
    PROiPR:P58215.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000115318.
    CleanExiHS_LOXL3.
    ExpressionAtlasiP58215. baseline and differential.
    GenevisibleiP58215. HS.

    Family and domain databases

    Gene3Di3.10.250.10. 1 hit.
    InterProiView protein in InterPro
    IPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    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. 1 hit.
    PS50287. SRCR_2. 4 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiLOXL3_HUMAN
    AccessioniPrimary (citable) accession number: P58215
    Secondary accession number(s): D6W5J1
    , Q2EHP2, Q6IPL7, Q96RS1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2001
    Last sequence update: July 11, 2001
    Last modified: April 12, 2017
    This is version 144 of the entry and version 1 of the sequence. See 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 2
      Human chromosome 2: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.