LYSC_PAPAN
ID LYSC_PAPAN Reviewed; 148 AA.
AC P61629; P00696; P79163; P79844;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE Flags: Precursor;
GN Name=LYZ; Synonyms=LZM;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=8990116; DOI=10.1038/385151a0;
RA Messier W., Stewart C.B.;
RT "Episodic adaptive evolution of primate lysozymes.";
RL Nature 385:151-154(1997).
RN [2]
RP PROTEIN SEQUENCE OF 19-148.
RC TISSUE=Milk;
RX PubMed=4202218; DOI=10.1016/0022-2836(73)90408-7;
RA Hermann J., Jolles J., Buss D.H., Jolles P.;
RT "Amino acid sequence of lysozyme from baboon milk.";
RL J. Mol. Biol. 79:587-595(1973).
CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC tissues and body fluids are associated with the monocyte-macrophage
CC system and enhance the activity of immunoagents.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC transglycosylation; it shows also a slight esterase activity. It acts
CC rapidly on both peptide-substituted and unsubstituted peptidoglycan,
CC and slowly on chitin oligosaccharides.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; U76919; AAB41207.1; -; mRNA.
DR PIR; A00850; LZBA.
DR RefSeq; NP_001106112.1; NM_001112642.1.
DR AlphaFoldDB; P61629; -.
DR SMR; P61629; -.
DR STRING; 9555.ENSPANP00000012261; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR Ensembl; ENSPANT00000067097; ENSPANP00000060558; ENSPANG00000047975.
DR GeneID; 100126730; -.
DR KEGG; panu:100126730; -.
DR CTD; 4069; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR GeneTree; ENSGT00940000153832; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR OMA; WVAWKAH; -.
DR OrthoDB; 1551203at2759; -.
DR Proteomes; UP000028761; Chromosome 9.
DR Bgee; ENSPANG00000010682; Expressed in lung and 65 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR019799; Glyco_hydro_22_CS.
DR InterPro; IPR000974; Glyco_hydro_22_lys.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR030056; Lysozyme_C.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:4202218"
FT CHAIN 19..148
FT /note="Lysozyme C"
FT /id="PRO_0000018477"
FT DOMAIN 19..148
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 24..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 48..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 83..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 95..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT CONFLICT 85
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="A -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16409 MW; 41AE0FB34335ED6F CRC64;
MKAVIILGLV LLSVTVQGKI FERCELARTL KRLGLDGYRG ISLANWVCLA KWESDYNTQA
TNYNPGDQST DYGIFQINSH YWCNNGKTPG AVNACHISCN ALLQDNIADA VTCAKRVVSD
PQGIRAWVAW RNHCQNRDVS QYVQGCGV
