LYZL6_MOUSE
ID LYZL6_MOUSE Reviewed; 148 AA.
AC Q9DA11;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Lysozyme-like protein 6;
DE EC=3.2.1.17;
DE Flags: Precursor;
GN Name=Lyzl6; Synonyms=Lyc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Zhang K., Dang Y., Yu L.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: May be involved sperm-egg plasma membrane adhesion and fusion
CC during fertilization. Exhibits bacteriolytic activity in vitro against
CC Micrococcus luteus and Staphylococcus aureus. Shows weak bacteriolytic
CC activity against Gram-positive bacteria at physiological pH.
CC Bacteriolytic activity is pH-dependent, with a maximum at around pH 5.6
CC (By similarity). {ECO:0000250|UniProtKB:O75951}.
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:0000250|UniProtKB:O75951}. Cell
CC surface {ECO:0000250|UniProtKB:O75951}. Cell projection, cilium,
CC flagellum {ECO:0000269|PubMed:24013621}. Note=Detected in the
CC postacrosomal area and midpiece of mature spermatozoa
CC (PubMed:24013621). {ECO:0000269|PubMed:24013621}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in testis and epididymis and
CC weakly in seminal vesicle, vas deferens, kidney and spleen
CC (PubMed:24013621). Highly expressed in primary spermatocytes and round
CC spermatids (at protein level) (PubMed:24013621).
CC {ECO:0000269|PubMed:24013621}.
CC -!- DEVELOPMENTAL STAGE: In testis expressed from day 21 during postnatal
CC development (PubMed:24013621). In the epidydimis, first detected at day
CC 28 and high expression is maintained until day 35. Thereafter, level
CC declines gradually (PubMed:24013621). {ECO:0000269|PubMed:24013621}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; AY566284; AAS68631.1; -; mRNA.
DR EMBL; AK006279; BAB24499.1; -; mRNA.
DR EMBL; BC048617; AAH48617.1; -; mRNA.
DR CCDS; CCDS25519.1; -.
DR RefSeq; NP_081359.1; NM_027083.1.
DR RefSeq; XP_006534178.1; XM_006534115.3.
DR AlphaFoldDB; Q9DA11; -.
DR SMR; Q9DA11; -.
DR STRING; 10090.ENSMUSP00000021328; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR GlyGen; Q9DA11; 1 site.
DR PhosphoSitePlus; Q9DA11; -.
DR MaxQB; Q9DA11; -.
DR PaxDb; Q9DA11; -.
DR PeptideAtlas; Q9DA11; -.
DR PRIDE; Q9DA11; -.
DR ProteomicsDB; 290207; -.
DR Antibodypedia; 72609; 161 antibodies from 22 providers.
DR DNASU; 69444; -.
DR Ensembl; ENSMUST00000021328; ENSMUSP00000021328; ENSMUSG00000020945.
DR Ensembl; ENSMUST00000107014; ENSMUSP00000102628; ENSMUSG00000020945.
DR GeneID; 69444; -.
DR KEGG; mmu:69444; -.
DR UCSC; uc007lvl.1; mouse.
DR CTD; 57151; -.
DR MGI; MGI:1916694; Lyzl6.
DR VEuPathDB; HostDB:ENSMUSG00000020945; -.
DR eggNOG; ENOG502SCGK; Eukaryota.
DR GeneTree; ENSGT00940000161690; -.
DR HOGENOM; CLU_111620_1_1_1; -.
DR InParanoid; Q9DA11; -.
DR OMA; HWLCLAF; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; Q9DA11; -.
DR TreeFam; TF324882; -.
DR BioGRID-ORCS; 69444; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9DA11; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DA11; protein.
DR Bgee; ENSMUSG00000020945; Expressed in spermatid and 20 other tissues.
DR ExpressionAtlas; Q9DA11; baseline and differential.
DR Genevisible; Q9DA11; MM.
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; IDA:UniProtKB.
DR GO; GO:0097524; C:sperm plasma membrane; ISS:UniProtKB.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; ISS:UniProtKB.
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; IPR030063; LYZL6.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF9; PTHR11407:SF9; 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; Cell projection; Cilium;
KW Disulfide bond; Fertilization; Flagellum; Glycoprotein; Glycosidase;
KW Hydrolase; 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_0000240641"
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 CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 148 AA; 16818 MW; 81C6F74A2387D97A CRC64;
MLKALFICVA SCLLVVNDGN IIHRCSLAKI LYEEDLDGFE GYSLPDWLCL AFVESNFNIS
KVNENVDGSF DYGIFQINSR YWCNDYQSHS ENFCHVDCQE LLSPNLISTI HCAKKIVSGP
GGMKNWVEWK LHCLGRPLSY WMTGCHLG
