ID   LYZL6_HUMAN             Reviewed;         148 AA.
AC   O75951; Q6UW30;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 169.
DE   RecName: Full=Lysozyme-like protein 6;
DE            EC=3.2.1.17;
DE   Flags: Precursor;
GN   Name=LYZL6; Synonyms=LYC1; ORFNames=UNQ754/PRO1485;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10213461; DOI=10.1089/107999099314153;
RA   Nomiyama H., Fukuda S., Iio M., Tanase S., Miura R., Yoshie O.;
RT   "Organization of the chemokine gene cluster on human chromosome 17q11.2
RT   containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and RANTES.";
RL   J. Interferon Cytokine Res. 19:227-234(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=16014814; DOI=10.1095/biolreprod.105.041889;
RA   Zhang K., Gao R., Zhang H., Cai X., Shen C., Wu C., Zhao S., Yu L.;
RT   "Molecular cloning and characterization of three novel lysozyme-like genes,
RT   predominantly expressed in the male reproductive system of humans,
RT   belonging to the c-type lysozyme/alpha-lactalbumin family.";
RL   Biol. Reprod. 73:1064-1071(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-139.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   BACTERIOLYTIC ACTIVITY.
RX   PubMed=24013621; DOI=10.1038/aja.2013.93;
RA   Wei J., Li S.J., Shi H., Wang H.Y., Rong C.T., Zhu P., Jin S.H., Liu J.,
RA   Li J.Y.;
RT   "Characterisation of Lyzls in mice and antibacterial properties of human
RT   LYZL6.";
RL   Asian J. Androl. 15:824-830(2013).
RN   [6]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND FUNCTION.
RX   PubMed=28182716; DOI=10.1371/journal.pone.0171452;
RA   Huang P., Li W., Yang Z., Zhang N., Xu Y., Bao J., Jiang D., Dong X.;
RT   "LYZL6, an acidic, bacteriolytic, human sperm-related protein, plays a role
RT   in fertilization.";
RL   PLoS ONE 12:E0171452-E0171452(2017).
CC   -!- FUNCTION: May be involved sperm-egg plasma membrane adhesion and fusion
CC       during fertilization (PubMed:28182716). Exhibits bacteriolytic activity
CC       in vitro against Micrococcus luteus and Staphylococcus aureus
CC       (PubMed:28182716, PubMed:24013621). Shows weak bacteriolytic activity
CC       against Gram-positive bacteria at physiological pH (PubMed:28182716).
CC       Bacteriolytic activity is pH-dependent, with a maximum at around pH 5.6
CC       (PubMed:28182716). {ECO:0000269|PubMed:24013621,
CC       ECO:0000269|PubMed:28182716}.
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. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28182716}. Cell
CC       surface {ECO:0000269|PubMed:28182716}. Cell projection, cilium,
CC       flagellum {ECO:0000250|UniProtKB:Q9DA11}. Note=Detected on the
CC       postacrosomal membrane of mature spermatozoa (PubMed:28182716).
CC       {ECO:0000269|PubMed:28182716}.
CC   -!- TISSUE SPECIFICITY: Expressed in testis, epididymis and spermatozoa (at
CC       protein level) (PubMed:16014814, PubMed:28182716). Expressed in late-
CC       stage spermatocytes and round spermatids (PubMed:28182716).
CC       {ECO:0000269|PubMed:16014814, ECO:0000269|PubMed:28182716}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   EMBL; AF088219; AAC63332.1; -; Genomic_DNA.
DR   EMBL; AY742214; AAU93343.1; -; mRNA.
DR   EMBL; AY359018; AAQ89377.1; -; mRNA.
DR   EMBL; BC054481; AAH54481.1; -; mRNA.
DR   CCDS; CCDS11302.1; -.
DR   RefSeq; NP_001186880.1; NM_001199951.2.
DR   RefSeq; NP_065159.1; NM_020426.3.
DR   AlphaFoldDB; O75951; -.
DR   SMR; O75951; -.
DR   BioGRID; 121408; 41.
DR   IntAct; O75951; 1.
DR   MINT; O75951; -.
DR   STRING; 9606.ENSP00000483897; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   iPTMnet; O75951; -.
DR   PhosphoSitePlus; O75951; -.
DR   BioMuta; LYZL6; -.
DR   MassIVE; O75951; -.
DR   PaxDb; 9606-ENSP00000483897; -.
DR   PeptideAtlas; O75951; -.
DR   ProteomicsDB; 50312; -.
DR   Antibodypedia; 72609; 174 antibodies from 24 providers.
DR   DNASU; 57151; -.
DR   Ensembl; ENST00000612374.2; ENSP00000483358.1; ENSG00000277042.2.
DR   Ensembl; ENST00000615905.5; ENSP00000483897.1; ENSG00000275722.5.
DR   Ensembl; ENST00000618542.4; ENSP00000482955.1; ENSG00000275722.5.
DR   Ensembl; ENST00000632590.1; ENSP00000488304.1; ENSG00000277042.2.
DR   GeneID; 57151; -.
DR   KEGG; hsa:57151; -.
DR   MANE-Select; ENST00000615905.5; ENSP00000483897.1; NM_020426.4; NP_065159.1.
DR   UCSC; uc002hkk.3; human.
DR   AGR; HGNC:29614; -.
DR   CTD; 57151; -.
DR   GeneCards; LYZL6; -.
DR   HGNC; HGNC:29614; LYZL6.
DR   HPA; ENSG00000275722; Tissue enriched (testis).
DR   MIM; 612751; gene.
DR   neXtProt; NX_O75951; -.
DR   OpenTargets; ENSG00000275722; -.
DR   PharmGKB; PA134942111; -.
DR   VEuPathDB; HostDB:ENSG00000275722; -.
DR   eggNOG; ENOG502SCGK; Eukaryota.
DR   GeneTree; ENSGT00940000161690; -.
DR   HOGENOM; CLU_111620_1_1_1; -.
DR   InParanoid; O75951; -.
DR   OMA; EWRLHCA; -.
DR   OrthoDB; 5344399at2759; -.
DR   PhylomeDB; O75951; -.
DR   TreeFam; TF324882; -.
DR   PathwayCommons; O75951; -.
DR   BioGRID-ORCS; 57151; 29 hits in 1132 CRISPR screens.
DR   GenomeRNAi; 57151; -.
DR   Pharos; O75951; Tbio.
DR   PRO; PR:O75951; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O75951; Protein.
DR   Bgee; ENSG00000275722; Expressed in left testis and 40 other cell types or tissues.
DR   ExpressionAtlas; O75951; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0036126; C:sperm flagellum; IBA:GO_Central.
DR   GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR   GO; GO:0097524; C:sperm plasma membrane; IDA:UniProtKB.
DR   GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR   GO; GO:0009566; P:fertilization; IMP:UniProtKB.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IMP:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd16897; LYZ_C; 1.
DR   Gene3D; 1.10.530.10; -; 1.
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   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   PANTHER; PTHR11407:SF9; LYSOZYME-LIKE PROTEIN 6; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
DR   Genevisible; O75951; HS.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Cell projection; Cilium;
KW   Disulfide bond; Fertilization; Flagellum; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..148
FT                   /note="Lysozyme-like protein 6"
FT                   /id="PRO_0000240640"
FT   DOMAIN          20..148
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        25..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        49..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        83..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        94..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   VARIANT         139
FT                   /note="F -> S (in dbSNP:rs9754)"
FT                   /evidence="ECO:0000269|PubMed:12975309"
FT                   /id="VAR_026819"
SQ   SEQUENCE   148 AA;  16956 MW;  C79DEC3B68ADF117 CRC64;
     MTKALLIYLV SSFLALNQAS LISRCDLAQV LQLEDLDGFE GYSLSDWLCL AFVESKFNIS
     KINENADGSF DYGLFQINSH YWCNDYKSYS ENLCHVDCQD LLNPNLLAGI HCAKRIVSGA
     RGMNNWVEWR LHCSGRPLFY WLTGCRLR
//