LYZL2_HUMAN
ID LYZL2_HUMAN Reviewed; 148 AA.
AC Q7Z4W2; Q6NZ69;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Lysozyme-like protein 2;
DE Short=Lysozyme-2;
DE EC=3.2.1.17;
DE Flags: Precursor;
GN Name=LYZL2;
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 [MRNA] (ISOFORM 1), VARIANT GLY-144, AND TISSUE
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
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:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z4W2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4W2-2; Sequence=VSP_019717;
CC -!- TISSUE SPECIFICITY: Expressed in testis, epididymis and placenta.
CC {ECO:0000269|PubMed:16014814}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; AF139543; AAP97272.1; -; mRNA.
DR EMBL; AL451107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066294; AAH66294.1; -; mRNA.
DR CCDS; CCDS7167.2; -. [Q7Z4W2-1]
DR RefSeq; NP_898881.2; NM_183058.2. [Q7Z4W2-1]
DR AlphaFoldDB; Q7Z4W2; -.
DR SMR; Q7Z4W2; -.
DR BioGRID; 125634; 94.
DR IntAct; Q7Z4W2; 54.
DR STRING; 9606.ENSP00000364467; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR GlyGen; Q7Z4W2; 1 site.
DR iPTMnet; Q7Z4W2; -.
DR PhosphoSitePlus; Q7Z4W2; -.
DR BioMuta; LYZL2; -.
DR DMDM; 109892575; -.
DR MassIVE; Q7Z4W2; -.
DR PaxDb; Q7Z4W2; -.
DR PeptideAtlas; Q7Z4W2; -.
DR PRIDE; Q7Z4W2; -.
DR ProteomicsDB; 69251; -. [Q7Z4W2-1]
DR ProteomicsDB; 69252; -. [Q7Z4W2-2]
DR Antibodypedia; 26283; 47 antibodies from 11 providers.
DR DNASU; 119180; -.
DR Ensembl; ENST00000375318.4; ENSP00000364467.2; ENSG00000151033.10. [Q7Z4W2-2]
DR Ensembl; ENST00000647634.2; ENSP00000497408.1; ENSG00000151033.10. [Q7Z4W2-1]
DR GeneID; 119180; -.
DR KEGG; hsa:119180; -.
DR MANE-Select; ENST00000647634.2; ENSP00000497408.1; NM_183058.3; NP_898881.3.
DR UCSC; uc001ivk.4; human. [Q7Z4W2-1]
DR CTD; 119180; -.
DR DisGeNET; 119180; -.
DR GeneCards; LYZL2; -.
DR HGNC; HGNC:29613; LYZL2.
DR HPA; ENSG00000151033; Tissue enriched (testis).
DR MIM; 612748; gene.
DR neXtProt; NX_Q7Z4W2; -.
DR OpenTargets; ENSG00000151033; -.
DR PharmGKB; PA134920379; -.
DR VEuPathDB; HostDB:ENSG00000151033; -.
DR eggNOG; ENOG502SCGK; Eukaryota.
DR GeneTree; ENSGT00940000159227; -.
DR HOGENOM; CLU_111620_0_0_1; -.
DR InParanoid; Q7Z4W2; -.
DR OMA; CNGRKMS; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; Q7Z4W2; -.
DR TreeFam; TF324882; -.
DR PathwayCommons; Q7Z4W2; -.
DR SignaLink; Q7Z4W2; -.
DR BioGRID-ORCS; 119180; 22 hits in 643 CRISPR screens.
DR GenomeRNAi; 119180; -.
DR Pharos; Q7Z4W2; Tdark.
DR PRO; PR:Q7Z4W2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q7Z4W2; protein.
DR Bgee; ENSG00000151033; Expressed in left testis and 20 other tissues.
DR ExpressionAtlas; Q7Z4W2; baseline and differential.
DR Genevisible; Q7Z4W2; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
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; IPR030057; LYZL1/LYZL2.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF62; PTHR11407:SF62; 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 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..148
FT /note="Lysozyme-like protein 2"
FT /id="PRO_0000240637"
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"
FT VAR_SEQ 1
FT /note="M -> MQDAPLSCLSPTKWSSVSSADSTEKSASAAGTRNLPFQFCLRQALRM
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019717"
FT VARIANT 144
FT /note="D -> G (in dbSNP:rs1054570)"
FT /evidence="ECO:0000269|PubMed:16014814"
FT /id="VAR_026818"
SQ SEQUENCE 148 AA; 16656 MW; 4674158A2A5912F2 CRC64;
MKAAGILTLI GCLVTGAESK IYTRCKLAKI FSRAGLDNYW GFSLGNWICM AYYESGYNTT
AQTVLDDGSI DYGIFQINSF AWCRRGKLKE NNHCHVACSA LVTDDLTDAI ICAKKIVKET
QGMNYWQGWK KHCEGRDLSD WKKDCEVS
