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Protein

Lysozyme C

Gene

LYZ

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

Functioni

Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

Miscellaneous

Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.

Catalytic activityi

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei531
Active sitei711

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • lysozyme activity Source: UniProtKB

GO - Biological processi

  • antimicrobial humoral response Source: Reactome
  • cellular protein metabolic process Source: Reactome
  • cell wall macromolecule catabolic process Source: GO_Central
  • cytolysis Source: UniProtKB-KW
  • defense response to bacterium Source: UniProtKB
  • defense response to Gram-negative bacterium Source: GO_Central
  • defense response to Gram-positive bacterium Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • killing of cells of other organism Source: UniProtKB
  • neutrophil degranulation Source: Reactome
  • retina homeostasis Source: UniProtKB

Keywordsi

Molecular functionAntimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.17 2681
ReactomeiR-HSA-6798695 Neutrophil degranulation
R-HSA-6803157 Antimicrobial peptides
R-HSA-977225 Amyloid fiber formation
SIGNORiP61626

Protein family/group databases

CAZyiGH22 Glycoside Hydrolase Family 22

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ
Synonyms:LZM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000090382.6
HGNCiHGNC:6740 LYZ
MIMi153450 gene
neXtProtiNX_P61626

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Secreted

Pathology & Biotechi

Involvement in diseasei

Amyloidosis 8 (AMYL8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of hereditary generalized amyloidosis. Clinical features include extensive visceral amyloid deposits, renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. There is no involvement of the nervous system.
See also OMIM:105200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00428074I → T in AMYL8. 1 PublicationCorresponds to variant dbSNP:rs121913547EnsemblClinVar.1
Natural variantiVAR_00428185D → H in AMYL8. 1 PublicationCorresponds to variant dbSNP:rs121913548Ensembl.1

Keywords - Diseasei

Amyloidosis, Disease mutation

Organism-specific databases

DisGeNETi4069
MalaCardsiLYZ
MIMi105200 phenotype
OpenTargetsiENSG00000090382
Orphaneti93561 Familial renal amyloidosis due to lysozyme variant
PharmGKBiPA30503

Chemistry databases

DrugBankiDB02159 (R)-Propylene glycol
DB03175 1-Proponol
DB03487 3-Aminosuccinimide
DB02759 4-Methylumbelliferyl Chitobiose
DB03006 Arsanilic acid
DB04194 Chitotriose
DB02250 Cu-Bicyclam
DB03189 Cu-Cyclam
DB03013 Di(N-Acetyl-D-Glucosamine)
DB03967 Dodecyl Sulfate
DB00128 L-Aspartic Acid
DB04268 Methylumbelliferyl Chitotriose
DB03120 Para-Toluene Sulfonate
DB02772 Sucrose

Polymorphism and mutation databases

BioMutaiLYZ
DMDMi48428995

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 185 PublicationsAdd BLAST18
ChainiPRO_000001846719 – 148Lysozyme CAdd BLAST130

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 146
Disulfide bondi48 ↔ 134
Disulfide bondi83 ↔ 99
Disulfide bondi95 ↔ 113

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP61626
MaxQBiP61626
PaxDbiP61626
PeptideAtlasiP61626
PRIDEiP61626
ProteomicsDBi12683
57328
TopDownProteomicsiP61626

2D gel databases

UCD-2DPAGEiP61626

PTM databases

iPTMnetiP61626
PhosphoSitePlusiP61626

Expressioni

Gene expression databases

BgeeiENSG00000090382
CleanExiHS_LYZ
ExpressionAtlasiP61626 baseline and differential
GenevisibleiP61626 HS

Organism-specific databases

HPAiCAB000055
HPA048284
HPA066182

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-355360,EBI-355360

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi110247, 35 interactors
IntActiP61626, 10 interactors
MINTiP61626
STRINGi9606.ENSP00000261267

Structurei

Secondary structure

1148
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 32Combined sources10
Helixi38 – 40Combined sources3
Helixi43 – 54Combined sources12
Beta strandi55 – 57Combined sources3
Beta strandi61 – 63Combined sources3
Turni65 – 67Combined sources3
Beta strandi70 – 72Combined sources3
Turni73 – 76Combined sources4
Turni79 – 81Combined sources3
Beta strandi82 – 84Combined sources3
Beta strandi88 – 90Combined sources3
Helixi99 – 103Combined sources5
Beta strandi104 – 106Combined sources3
Helixi108 – 119Combined sources12
Beta strandi120 – 122Combined sources3
Helixi123 – 126Combined sources4
Helixi128 – 133Combined sources6
Turni134 – 136Combined sources3
Helixi140 – 142Combined sources3
Turni143 – 145Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
133LX-ray1.77A19-148[»]
134LX-ray1.77A19-148[»]
1B5UX-ray1.80A19-148[»]
1B5VX-ray2.17A19-148[»]
1B5WX-ray2.17A19-148[»]
1B5XX-ray2.00A19-148[»]
1B5YX-ray2.20A19-148[»]
1B5ZX-ray2.20A/B19-148[»]
1B7LX-ray1.80A19-148[»]
1B7MX-ray2.20A19-148[»]
1B7NX-ray1.80A19-148[»]
1B7OX-ray1.80A19-148[»]
1B7PX-ray2.00A19-148[»]
1B7QX-ray2.00A19-148[»]
1B7RX-ray1.80A19-148[»]
1B7SX-ray2.00A19-148[»]
1BB3X-ray1.80A/B19-148[»]
1BB4X-ray2.23A/B19-148[»]
1BB5X-ray1.80A/B19-148[»]
1C43X-ray1.80A19-148[»]
1C45X-ray1.80A19-148[»]
1C46X-ray2.20A19-148[»]
1C7PX-ray2.40A16-148[»]
1CJ6X-ray1.80A19-148[»]
1CJ7X-ray1.80A19-148[»]
1CJ8X-ray1.80A19-148[»]
1CJ9X-ray1.80A19-148[»]
1CKCX-ray1.80A19-148[»]
1CKDX-ray1.80A19-148[»]
1CKFX-ray1.80A19-148[»]
1CKGX-ray2.20A/B19-148[»]
1CKHX-ray2.00A19-148[»]
1D6PX-ray2.23A19-148[»]
1D6QX-ray1.96A19-148[»]
1DI3X-ray1.80A19-148[»]
1DI4X-ray2.00A19-148[»]
1DI5X-ray2.20A19-148[»]
1EQ4X-ray1.80A19-148[»]
1EQ5X-ray1.80A19-148[»]
1EQEX-ray1.80A19-148[»]
1GAYX-ray1.80A19-148[»]
1GAZX-ray1.80A19-148[»]
1GB0X-ray1.80A19-148[»]
1GB2X-ray1.80A19-148[»]
1GB3X-ray1.80A19-148[»]
1GB5X-ray1.80A19-148[»]
1GB6X-ray1.80A19-148[»]
1GB7X-ray1.80A19-148[»]
1GB8X-ray1.80A19-148[»]
1GB9X-ray1.80A19-148[»]
1GBOX-ray1.80A19-148[»]
1GBWX-ray1.80A19-148[»]
1GBXX-ray1.80A19-148[»]
1GBYX-ray1.80A19-148[»]
1GBZX-ray1.80A19-148[»]
1GDWX-ray1.80A19-148[»]
1GDXX-ray1.80A19-148[»]
1GE0X-ray1.80A19-148[»]
1GE1X-ray1.70A19-148[»]
1GE2X-ray2.00A19-148[»]
1GE3X-ray1.80A19-148[»]
1GE4X-ray1.80A19-148[»]
1GEVX-ray2.10A19-148[»]
1GEZX-ray1.80A19-148[»]
1GF0X-ray1.80A19-148[»]
1GF3X-ray1.80A19-148[»]
1GF4X-ray1.80A19-148[»]
1GF5X-ray1.80A19-148[»]
1GF6X-ray1.80A19-148[»]
1GF7X-ray1.80A19-148[»]
1GF8X-ray1.80A19-148[»]
1GF9X-ray1.80A19-148[»]
1GFAX-ray1.80A19-148[»]
1GFEX-ray1.80A19-148[»]
1GFGX-ray1.80A19-148[»]
1GFHX-ray1.80A19-148[»]
1GFJX-ray1.80A19-148[»]
1GFKX-ray1.80A19-148[»]
1GFRX-ray1.80A19-148[»]
1GFTX-ray1.80A19-148[»]
1GFUX-ray1.80A19-148[»]
1GFVX-ray1.80A19-148[»]
1HNLX-ray1.80A19-148[»]
1I1ZX-ray1.80A19-148[»]
1I20X-ray1.90A19-148[»]
1I22X-ray1.80A/B/C/D19-148[»]
1INUX-ray1.80A19-148[»]
1IOCX-ray2.40A19-148[»]
1IP1X-ray1.80A19-148[»]
1IP2X-ray1.80A19-148[»]
1IP3X-ray1.80A/B19-148[»]
1IP4X-ray1.80A19-148[»]
1IP5X-ray1.80A19-148[»]
1IP6X-ray1.80A19-148[»]
1IP7X-ray1.90A/B19-146[»]
1IWTX-ray1.40A19-148[»]
1IWUX-ray1.40A19-148[»]
1IWVX-ray1.40A19-148[»]
1IWWX-ray1.40A19-148[»]
1IWXX-ray1.40A19-148[»]
1IWYX-ray1.40A19-148[»]
1IWZX-ray1.48A19-148[»]
1IX0X-ray1.80A19-148[»]
1IY3NMR-A19-148[»]
1IY4NMR-A19-148[»]
1JKAX-ray1.66A19-148[»]
1JKBX-ray1.66A19-148[»]
1JKCX-ray1.60A19-148[»]
1JKDX-ray1.80A19-148[»]
1JSFX-ray1.15A19-148[»]
1JWRX-ray1.40A19-148[»]
1LAAX-ray1.77A19-148[»]
1LHHX-ray1.80A19-148[»]
1LHIX-ray1.80A19-148[»]
1LHJX-ray1.80A19-148[»]
1LHKX-ray1.80A19-148[»]
1LHLX-ray1.80A19-148[»]
1LHMX-ray1.80A19-148[»]
1LMTX-ray1.60A19-148[»]
1LOZX-ray1.80A19-148[»]
1LYYX-ray1.80A19-148[»]
1LZ1X-ray1.50A19-148[»]
1LZ4X-ray1.80A19-148[»]
1LZ5X-ray1.80A19-144[»]
1LZ6X-ray1.80A19-140[»]
1LZRX-ray1.50A19-148[»]
1LZSX-ray1.60A/B19-148[»]
1OP9X-ray1.86B19-148[»]
1OUAX-ray1.80A19-148[»]
1OUBX-ray1.80A19-148[»]
1OUCX-ray1.80A19-148[»]
1OUDX-ray1.80A19-148[»]
1OUEX-ray1.80A19-148[»]
1OUFX-ray1.80A19-147[»]
1OUGX-ray1.80A19-148[»]
1OUHX-ray1.80A19-148[»]
1OUIX-ray1.80A19-148[»]
1OUJX-ray1.80A19-148[»]
1QSWX-ray1.85A/B/C/D19-148[»]
1RE2X-ray2.30A19-148[»]
1REMX-ray2.10A19-148[»]
1REXX-ray1.50A19-148[»]
1REYX-ray1.70A19-148[»]
1REZX-ray1.70A19-148[»]
1TAYX-ray1.70A19-148[»]
1TBYX-ray1.77A19-148[»]
1TCYX-ray1.70A19-148[»]
1TDYX-ray1.70A19-148[»]
1UBZX-ray2.00A19-148[»]
1W08X-ray2.50A19-148[»]
1WQMX-ray1.80A19-148[»]
1WQNX-ray1.80A19-148[»]
1WQOX-ray1.80A19-148[»]
1WQPX-ray1.80A19-148[»]
1WQQX-ray1.80A19-148[»]
1WQRX-ray1.80A19-148[»]
1YAMX-ray1.80A19-148[»]
1YANX-ray1.80A19-148[»]
1YAOX-ray1.80A19-148[»]
1YAPX-ray1.80A19-148[»]
1YAQX-ray1.80A19-148[»]
207LX-ray1.80A19-148[»]
208LX-ray2.20A19-148[»]
2BQAX-ray1.80A19-148[»]
2BQBX-ray1.80A19-148[»]
2BQCX-ray1.80A19-148[»]
2BQDX-ray1.80A19-148[»]
2BQEX-ray1.80A19-148[»]
2BQFX-ray1.80A19-148[»]
2BQGX-ray1.80A19-148[»]
2BQHX-ray1.80A19-148[»]
2BQIX-ray1.80A19-148[»]
2BQJX-ray1.80A19-148[»]
2BQKX-ray1.80A19-147[»]
2BQLX-ray1.80A19-148[»]
2BQMX-ray1.80A19-148[»]
2BQNX-ray1.80A19-148[»]
2BQOX-ray1.80A19-148[»]
2HEAX-ray1.80A19-148[»]
2HEBX-ray2.20A19-148[»]
2HECX-ray1.80A19-148[»]
2HEDX-ray1.80A19-148[»]
2HEEX-ray1.80A19-148[»]
2HEFX-ray1.80A19-148[»]
2LHMX-ray1.80A19-148[»]
2MEAX-ray2.20A/B19-148[»]
2MEBX-ray1.80A19-148[»]
2MECX-ray2.20A/B19-148[»]
2MEDX-ray1.80A19-148[»]
2MEEX-ray1.80A19-148[»]
2MEFX-ray1.80A19-148[»]
2MEGX-ray1.80A19-148[»]
2MEHX-ray1.80A19-148[»]
2MEIX-ray1.80A19-148[»]
2NWDX-ray1.04X19-148[»]
2ZIJX-ray1.90A19-148[»]
2ZIKX-ray1.81A19-148[»]
2ZILX-ray1.80A19-148[»]
2ZWBneutron diffraction1.80A19-148[»]
3EBAX-ray1.85B19-148[»]
3FE0X-ray1.50A19-148[»]
3LHMX-ray1.80A19-148[»]
3LN2X-ray2.04A/B19-148[»]
4I0CX-ray1.95A/B19-148[»]
4ML7X-ray1.80A/C19-148[»]
4R0PX-ray1.52A74-79[»]
5LSHX-ray1.06A19-148[»]
5LVKX-ray2.49A/B19-148[»]
ProteinModelPortaliP61626
SMRiP61626
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61626

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IXGD Eukaryota
ENOG4111QHM LUCA
GeneTreeiENSGT00550000074398
HOGENOMiHOG000037357
HOVERGENiHBG052297
InParanoidiP61626
KOiK13915
OMAiKWESNYN
OrthoDBiEOG091G0R9V
PhylomeDBiP61626
TreeFamiTF324882

Family and domain databases

CDDicd00119 LYZ1, 1 hit
InterProiView protein in InterPro
IPR001916 Glyco_hydro_22
IPR019799 Glyco_hydro_22_CS
IPR000974 Glyco_hydro_22_lys
IPR023346 Lysozyme-like_dom_sf
IPR030056 Lysozyme_C
PANTHERiPTHR11407:SF28 PTHR11407:SF28, 1 hit
PfamiView protein in Pfam
PF00062 Lys, 1 hit
PRINTSiPR00137 LYSOZYME
PR00135 LYZLACT
SMARTiView protein in SMART
SM00263 LYZ1, 1 hit
SUPFAMiSSF53955 SSF53955, 1 hit
PROSITEiView protein in PROSITE
PS00128 LACTALBUMIN_LYSOZYME_1, 1 hit
PS51348 LACTALBUMIN_LYSOZYME_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P61626-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALIVLGLV LLSVTVQGKV FERCELARTL KRLGMDGYRG ISLANWMCLA
60 70 80 90 100
KWESGYNTRA TNYNAGDRST DYGIFQINSR YWCNDGKTPG AVNACHLSCS
110 120 130 140
ALLQDNIADA VACAKRVVRD PQGIRAWVAW RNRCQNRDVR QYVQGCGV
Length:148
Mass (Da):16,537
Last modified:June 7, 2004 - v1
Checksum:i8ECFD276BEB2678A
GO

Sequence cautioni

The sequence CAA32175 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10V → A in AAC63078 (Ref. 5) Curated1
Sequence conflicti41I → M in AAA36188 (PubMed:2971592).Curated1
Sequence conflicti111V → A in AAC63078 (Ref. 5) Curated1
Sequence conflicti124I → V in AAC63078 (Ref. 5) Curated1
Sequence conflicti128V → A in AAC63078 (Ref. 5) Curated1
Sequence conflicti136N → D in AAC63078 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00428074I → T in AMYL8. 1 PublicationCorresponds to variant dbSNP:rs121913547EnsemblClinVar.1
Natural variantiVAR_00428185D → H in AMYL8. 1 PublicationCorresponds to variant dbSNP:rs121913548Ensembl.1
Natural variantiVAR_01205088T → N. Corresponds to variant dbSNP:rs1800973EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21119 mRNA Translation: AAA36188.1
J03801 mRNA Translation: AAA59535.1
M19045 mRNA Translation: AAA59536.1
X14008 Genomic DNA Translation: CAA32175.1 Different initiation.
U25677 mRNA Translation: AAC63078.1
BC004147 mRNA Translation: AAH04147.1
CCDSiCCDS8989.1
PIRiS04938 LZHU
RefSeqiNP_000230.1, NM_000239.2
UniGeneiHs.524579

Genome annotation databases

EnsembliENST00000261267; ENSP00000261267; ENSG00000090382
GeneIDi4069
KEGGihsa:4069
UCSCiuc001suw.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLYSC_HUMAN
AccessioniPrimary (citable) accession number: P61626
Secondary accession number(s): P00695, Q13170, Q9UCF8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2004
Last modified: June 20, 2018
This is version 160 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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