ID   LECT2_BOVIN             Reviewed;         151 AA.
AC   O62644; Q3ZBQ8;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Leukocyte cell-derived chemotaxin-2;
DE            Short=LECT-2;
DE            Short=bLECT2;
DE   AltName: Full=Chondromodulin II;
DE            Short=ChM-II;
DE            Short=bChM-II;
DE   Flags: Precursor;
GN   Name=LECT2;
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 [MRNA], AND FUNCTION.
RC   TISSUE=Liver;
RX   PubMed=9524238; DOI=10.1016/s0167-4781(97)00181-4;
RA   Yamagoe S., Mizuno S., Suzuki K.;
RT   "Molecular cloning of human and bovine LECT2 having a neutrophil
RT   chemotactic activity and its specific expression in the liver.";
RL   Biochim. Biophys. Acta 1396:105-113(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Embryo;
RX   PubMed=10050029; DOI=10.1093/oxfordjournals.jbchem.a022305;
RA   Shukunami C., Kondo J., Wakai H., Takahashi K., Inoue H., Kamizono A.,
RA   Hiraki Y.;
RT   "Molecular cloning of mouse and bovine chondromodulin-II cDNAs and the
RT   growth-promoting actions of bovine recombinant protein.";
RL   J. Biochem. 125:436-442(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 19-151.
RC   TISSUE=Epiphyseal cartilage;
RX   PubMed=8798437; DOI=10.1074/jbc.271.37.22657;
RA   Hiraki Y., Inoue H., Kondo J., Kamizono A., Yoshitake Y., Shukunami C.,
RA   Suzuki F.;
RT   "A novel growth-promoting factor derived from fetal bovine cartilage,
RT   chondromodulin II. Purification and amino acid sequence.";
RL   J. Biol. Chem. 271:22657-22662(1996).
CC   -!- FUNCTION: Has a neutrophil chemotactic activity (PubMed:9524238). Also
CC       a positive regulator of chondrocyte proliferation (PubMed:10050029,
CC       PubMed:8798437). {ECO:0000269|PubMed:10050029,
CC       ECO:0000269|PubMed:8798437, ECO:0000269|PubMed:9524238}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O14960}.
CC   -!- SIMILARITY: Belongs to the LECT2/MIM-1 family. {ECO:0000305}.
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DR   EMBL; AB001350; BAA25302.1; -; mRNA.
DR   EMBL; D89011; BAB18616.1; -; mRNA.
DR   EMBL; BC103166; AAI03167.1; -; mRNA.
DR   PIR; JH0270; JH0270.
DR   RefSeq; NP_776805.1; NM_174380.2.
DR   AlphaFoldDB; O62644; -.
DR   SMR; O62644; -.
DR   STRING; 9913.ENSBTAP00000001648; -.
DR   PaxDb; O62644; -.
DR   PRIDE; O62644; -.
DR   Ensembl; ENSBTAT00000001648; ENSBTAP00000001648; ENSBTAG00000001247.
DR   GeneID; 281899; -.
DR   KEGG; bta:281899; -.
DR   CTD; 3950; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001247; -.
DR   VGNC; VGNC:30832; LECT2.
DR   eggNOG; ENOG502S16D; Eukaryota.
DR   GeneTree; ENSGT00390000015484; -.
DR   HOGENOM; CLU_144880_0_0_1; -.
DR   InParanoid; O62644; -.
DR   OMA; MCDSHGC; -.
DR   OrthoDB; 1298781at2759; -.
DR   TreeFam; TF331097; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000001247; Expressed in liver and 30 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR008663; LECT2.
DR   InterPro; IPR017381; LECT2_chordata.
DR   InterPro; IPR016047; Peptidase_M23.
DR   PANTHER; PTHR11329; PTHR11329; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   PIRSF; PIRSF038085; LECT3; 1.
PE   1: Evidence at protein level;
KW   Chemotaxis; Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:8798437"
FT   CHAIN           19..151
FT                   /note="Leukocyte cell-derived chemotaxin-2"
FT                   /id="PRO_0000017363"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   DISULFID        25..60
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   DISULFID        36..41
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
FT   DISULFID        99..142
FT                   /evidence="ECO:0000250|UniProtKB:O14960"
SQ   SEQUENCE   151 AA;  16320 MW;  2A1DE8FF5B28A3D8 CRC64;
     MFSTGTLLLA ALISPALAGP WAIICAGKSS NEIRTCDGHG CGQYTAQRNQ KLHQGVDVLC
     SDGSTVYAPF TGKIMGQEKP YKNKNAINNG VRISGGGFCI KMFYIKPIKY KGSIKKGEKL
     GTLLPLQKVY PGIQSHIHIE NCDLSDPTVY L