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Protein

Lysozyme C

Gene

LYZ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

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

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciZFISH:HS01687-MONOMER.
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

HGNCiHGNC:6740. LYZ.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
Complete GO annotation...

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 rs121913547dbSNPEnsembl.1
Natural variantiVAR_00428185D → H in AMYL8. 1 PublicationCorresponds to variant rs121913548dbSNPEnsembl.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

DrugBankiDB00128. L-Aspartic Acid.

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.
TopDownProteomicsiP61626.

2D gel databases

UCD-2DPAGEP61626.

PTM databases

iPTMnetiP61626.
PhosphoSitePlusiP61626.

Expressioni

Gene expression databases

BgeeiENSG00000090382.
CleanExiHS_LYZ.
ExpressionAtlasiP61626. baseline and differential.
GenevisibleiP61626. HS.

Organism-specific databases

HPAiCAB000055.
HPA048284.

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. 28 interactors.
IntActiP61626. 10 interactors.
MINTiMINT-5002660.
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[»]
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.
OMAiHCFRRRH.
OrthoDBiEOG091G0R9V.
PhylomeDBiP61626.
TreeFamiTF324882.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

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 rs121913547dbSNPEnsembl.1
Natural variantiVAR_00428185D → H in AMYL8. 1 PublicationCorresponds to variant rs121913548dbSNPEnsembl.1
Natural variantiVAR_01205088T → N.Corresponds to variant rs1800973dbSNPEnsembl.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

Cross-referencesi

Web resourcesi

Wikipedia

Lysozyme entry

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.

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[»]
5LVKX-ray2.49A/B19-148[»]
ProteinModelPortaliP61626.
SMRiP61626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110247. 28 interactors.
IntActiP61626. 10 interactors.
MINTiMINT-5002660.
STRINGi9606.ENSP00000261267.

Chemistry databases

DrugBankiDB00128. L-Aspartic Acid.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

PTM databases

iPTMnetiP61626.
PhosphoSitePlusiP61626.

Polymorphism and mutation databases

BioMutaiLYZ.
DMDMi48428995.

2D gel databases

UCD-2DPAGEP61626.

Proteomic databases

EPDiP61626.
MaxQBiP61626.
PaxDbiP61626.
PeptideAtlasiP61626.
PRIDEiP61626.
TopDownProteomicsiP61626.

Protocols and materials databases

DNASUi4069.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4069.
DisGeNETi4069.
GeneCardsiLYZ.
HGNCiHGNC:6740. LYZ.
HPAiCAB000055.
HPA048284.
MalaCardsiLYZ.
MIMi105200. phenotype.
153450. gene.
neXtProtiNX_P61626.
OpenTargetsiENSG00000090382.
Orphaneti93561. Familial renal amyloidosis due to lysozyme variant.
PharmGKBiPA30503.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS01687-MONOMER.
BRENDAi3.2.1.17. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-6803157. Antimicrobial peptides.
R-HSA-977225. Amyloid fiber formation.
SIGNORiP61626.

Miscellaneous databases

ChiTaRSiLYZ. human.
EvolutionaryTraceiP61626.
GeneWikiiLysozyme.
GenomeRNAii4069.
PROiP61626.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000090382.
CleanExiHS_LYZ.
ExpressionAtlasiP61626. baseline and differential.
GenevisibleiP61626. HS.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLYSC_HUMAN
AccessioniPrimary (citable) accession number: P61626
Secondary accession number(s): P00695, Q13170, Q9UCF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2004
Last modified: November 30, 2016
This is version 147 of the entry and version 1 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

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.

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

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.