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LYZL1_BOVIN
ID   LYZL1_BOVIN             Reviewed;         148 AA.
AC   A0JNM6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Lysozyme-like protein 1;
DE            EC=3.2.1.17;
DE   Flags: Precursor;
GN   Name=LYZL1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR   EMBL; BC126794; AAI26795.1; -; mRNA.
DR   RefSeq; NP_001071378.1; NM_001077910.1.
DR   AlphaFoldDB; A0JNM6; -.
DR   SMR; A0JNM6; -.
DR   STRING; 9913.ENSBTAP00000013640; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   PaxDb; A0JNM6; -.
DR   Ensembl; ENSBTAT00000013640; ENSBTAP00000013640; ENSBTAG00000010330.
DR   GeneID; 512087; -.
DR   KEGG; bta:512087; -.
DR   CTD; 84569; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010330; -.
DR   eggNOG; ENOG502SCGK; Eukaryota.
DR   GeneTree; ENSGT00940000159227; -.
DR   HOGENOM; CLU_111620_0_1_1; -.
DR   InParanoid; A0JNM6; -.
DR   OMA; TWCRRAK; -.
DR   OrthoDB; 1551203at2759; -.
DR   TreeFam; TF324882; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000010330; Expressed in semen and 25 other tissues.
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   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..148
FT                   /note="Lysozyme-like protein 1"
FT                   /id="PRO_0000287123"
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;  16779 MW;  00DF85E11026F6D3 CRC64;
     MKAAGILALM GCLVTVVEPK VYTRCKLAKI FSRASLDNYR GFSLGNWICM AYYESHYNTT
     AQTQLEDGST DYGIFQINSD TWCRSTKLQE KNRCHVACSA LMTDDLTDAI ICAKKIVKET
     DGMNYWQGWK KNCEGRDLSE WKKGCEVS
 
 
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