LYZL4_MOUSE
ID LYZL4_MOUSE Reviewed; 145 AA.
AC Q9D925;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Lysozyme-like protein 4;
DE Short=Lysozyme-4;
DE Flags: Precursor;
GN Name=Lyzl4; Synonyms=Lyc4;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [2]
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP AND ABSENCE OF BACTERIOLYTIC ACTIVITY.
RX PubMed=21444326; DOI=10.1093/abbs/gmr017;
RA Sun R., Shen R., Li J., Xu G., Chi J., Li L., Ren J., Wang Z., Fei J.;
RT "Lyzl4, a novel mouse sperm-related protein, is involved in
RT fertilization.";
RL Acta Biochim. Biophys. Sin. 43:346-353(2011).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 in fertilization (PubMed:21444326). Has no
CC detectable bacteriolytic in vitro (PubMed:21444326). Has no lysozyme
CC activity in vitro (By similarity). {ECO:0000250|UniProtKB:D4ABW7,
CC ECO:0000269|PubMed:21444326}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21444326}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:21444326}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:21444326}. Note=Found in the principal piece of
CC sperm tail (PubMed:21444326). {ECO:0000269|PubMed:21444326}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in testis and in epididymis, and
CC weakly in brain and lung (PubMed:21444326, PubMed:24013621). Detected
CC in sperm (at protein level) (PubMed:21444326).
CC {ECO:0000269|PubMed:21444326, ECO:0000269|PubMed:24013621}.
CC -!- DEVELOPMENTAL STAGE: No expression in the testis of 2-weeks-old
CC neonates, the expression reaches a peak level at 12 weeks. After that,
CC the level gradually decreases as the age increases (PubMed:21444326,
CC PubMed:24013621). {ECO:0000269|PubMed:21444326,
CC ECO:0000269|PubMed:24013621}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
CC -!- CAUTION: Although it belongs to the glycosyl hydrolase 22 family, Gly-
CC 72 is present instead of the conserved Asp which is an active site
CC residue. It is therefore expected that this protein lacks hydrolase
CC activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25023.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK007412; BAB25023.2; ALT_INIT; mRNA.
DR CCDS; CCDS23632.1; -.
DR RefSeq; NP_081191.1; NM_026915.2.
DR RefSeq; XP_006512311.1; XM_006512248.2.
DR AlphaFoldDB; Q9D925; -.
DR SMR; Q9D925; -.
DR STRING; 10090.ENSMUSP00000076887; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PhosphoSitePlus; Q9D925; -.
DR PaxDb; Q9D925; -.
DR PRIDE; Q9D925; -.
DR ProteomicsDB; 292157; -.
DR Antibodypedia; 29191; 97 antibodies from 20 providers.
DR DNASU; 69032; -.
DR Ensembl; ENSMUST00000077706; ENSMUSP00000076887; ENSMUSG00000032530.
DR Ensembl; ENSMUST00000120918; ENSMUSP00000113034; ENSMUSG00000032530.
DR GeneID; 69032; -.
DR KEGG; mmu:69032; -.
DR UCSC; uc009sdi.1; mouse.
DR CTD; 131375; -.
DR MGI; MGI:1916282; Lyzl4.
DR VEuPathDB; HostDB:ENSMUSG00000032530; -.
DR eggNOG; ENOG502SSER; Eukaryota.
DR GeneTree; ENSGT00940000162293; -.
DR HOGENOM; CLU_111620_1_1_1; -.
DR InParanoid; Q9D925; -.
DR OMA; AWPSWSL; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; Q9D925; -.
DR TreeFam; TF324882; -.
DR BioGRID-ORCS; 69032; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Lyzl4; mouse.
DR PRO; PR:Q9D925; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9D925; protein.
DR Bgee; ENSMUSG00000032530; Expressed in spermatid and 35 other tissues.
DR ExpressionAtlas; Q9D925; baseline and differential.
DR Genevisible; Q9D925; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR GO; GO:0009566; P:fertilization; IMP:UniProtKB.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IBA:GO_Central.
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; IPR030062; LYZL4.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF21; PTHR11407:SF21; 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 Cell projection; Cilium; Cytoplasmic vesicle; Disulfide bond;
KW Fertilization; Flagellum; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..145
FT /note="Lysozyme-like protein 4"
FT /id="PRO_0000240639"
FT DOMAIN 20..145
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 25..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 49..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 84..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 91..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 145 AA; 16198 MW; 2AC71B4AB7EE96BD CRC64;
MQLYLVLLLI SYLLTPIGAS ILGRCTVAKM LYDGGLNYFE GYSLENWVCL AYFESKFNPS
AVYEDPQDGS TGFGLFQIRD NEWCGHGKNL CSVSCTALLN PNLKDTIQCA KKIVKGKHGM
GAWPIWSKNC QLSDVLDRWL DGCDL
