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   13-FEB-2019, entry version 143.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   17q11.2 containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and
RT   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
RT   genes, predominantly expressed in the male reproductive system of
RT   humans, 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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics 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
RT   project: 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.,
RA   Liu J., Li J.Y.;
RT   "Characterisation of Lyzls in mice and antibacterial properties of
RT   human 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
RT   role in fertilization.";
RL   PLoS ONE 12:E0171452-E0171452(2017).
CC   -!- FUNCTION: May be involved sperm-egg plasma membrane adhesion and
CC       fusion during fertilization (PubMed:28182716). Exhibits
CC       bacteriolytic activity in vitro against Micrococcus luteus and
CC       Staphylococcus aureus (PubMed:28182716, PubMed:24013621). Shows
CC       weak bacteriolytic activity against Gram-positive bacteria at
CC       physiological pH (PubMed:28182716). Bacteriolytic activity is pH-
CC       dependent, with a maximum at around pH 5.6 (PubMed:28182716).
CC       {ECO:0000269|PubMed:24013621, ECO:0000269|PubMed:28182716}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-
CC         acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC         peptidoglycan and between N-acetyl-D-glucosamine residues in
CC         chitodextrins.; 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
CC       spermatozoa (at protein level) (PubMed:16014814, PubMed:28182716).
CC       Expressed in late-stage spermatocytes and round spermatids
CC       (PubMed:28182716). {ECO:0000269|PubMed:16014814,
CC       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   UniGene; Hs.97477; -.
DR   ProteinModelPortal; O75951; -.
DR   SMR; O75951; -.
DR   STRING; 9606.ENSP00000293274; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   iPTMnet; O75951; -.
DR   PhosphoSitePlus; O75951; -.
DR   BioMuta; LYZL6; -.
DR   PaxDb; O75951; -.
DR   PeptideAtlas; O75951; -.
DR   PRIDE; O75951; -.
DR   ProteomicsDB; 50312; -.
DR   DNASU; 57151; -.
DR   Ensembl; ENST00000612374; ENSP00000483358; ENSG00000277042.
DR   Ensembl; ENST00000615905; ENSP00000483897; ENSG00000275722.
DR   Ensembl; ENST00000618542; ENSP00000482955; ENSG00000275722.
DR   Ensembl; ENST00000632590; ENSP00000488304; ENSG00000277042.
DR   GeneID; 57151; -.
DR   KEGG; hsa:57151; -.
DR   UCSC; uc002hkk.3; human.
DR   CTD; 57151; -.
DR   EuPathDB; HostDB:ENSG00000275722.4; -.
DR   GeneCards; LYZL6; -.
DR   HGNC; HGNC:29614; LYZL6.
DR   HPA; HPA025734; -.
DR   HPA; HPA053073; -.
DR   MIM; 612751; gene.
DR   neXtProt; NX_O75951; -.
DR   OpenTargets; ENSG00000275722; -.
DR   PharmGKB; PA134942111; -.
DR   eggNOG; ENOG410JC6R; Eukaryota.
DR   eggNOG; ENOG4111501; LUCA.
DR   GeneTree; ENSGT00940000161690; -.
DR   HOGENOM; HOG000037357; -.
DR   HOVERGEN; HBG052297; -.
DR   InParanoid; O75951; -.
DR   KO; K01185; -.
DR   OMA; FRHWNGW; -.
DR   OrthoDB; 1551203at2759; -.
DR   PhylomeDB; O75951; -.
DR   TreeFam; TF324882; -.
DR   GenomeRNAi; 57151; -.
DR   PRO; PR:O75951; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000275722; Expressed in 47 organ(s), highest expression level in right testis.
DR   ExpressionAtlas; O75951; baseline and differential.
DR   Genevisible; O75951; HS.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00119; LYZ1; 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   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; LACTALBUMIN_LYSOZYME_1; 1.
DR   PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Cell projection; Cilium;
KW   Complete proteome; Disulfide bond; Fertilization; Flagellum;
KW   Glycosidase; Hydrolase; Polymorphism; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    148       Lysozyme-like protein 6.
FT                                /FTId=PRO_0000240640.
FT   ACT_SITE     54     54       {ECO:0000255|PROSITE-ProRule:PRU00680}.
FT   ACT_SITE     71     71       {ECO:0000255|PROSITE-ProRule:PRU00680}.
FT   DISULFID     25    145       {ECO:0000255|PROSITE-ProRule:PRU00680}.
FT   DISULFID     49    133       {ECO:0000255|PROSITE-ProRule:PRU00680}.
FT   DISULFID     83     98       {ECO:0000255|PROSITE-ProRule:PRU00680}.
FT   DISULFID     94    112       {ECO:0000255|PROSITE-ProRule:PRU00680}.
FT   VARIANT     139    139       F -> S (in dbSNP:rs9754).
FT                                {ECO:0000269|PubMed:12975309}.
FT                                /FTId=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
//