ID   LECT2_HUMAN             Reviewed;         151 AA.
AC   O14960; B2RA90; O14565; Q52M49;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Leukocyte cell-derived chemotaxin-2;
DE            Short=LECT-2;
DE            Short=hLECT2;
DE   Flags: Precursor;
GN   Name=LECT2;
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], VARIANT VAL-58, FUNCTION, INDUCTION BY
RP   PHYTOHEMAGGLUTININ, AND TISSUE SPECIFICITY.
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 [GENOMIC DNA], AND VARIANT VAL-58.
RC   TISSUE=Peripheral blood;
RX   PubMed=9545637; DOI=10.1006/geno.1997.5198;
RA   Yamagoe S., Kameoka Y., Hashimoto K., Mizuno S., Suzuki K.;
RT   "Molecular cloning, structural characterization, and chromosomal mapping of
RT   the human LECT2 gene.";
RL   Genomics 48:324-329(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-58, AND TISSUE SPECIFICITY.
RX   PubMed=9832057; DOI=10.1111/j.1440-1827.1998.tb03855.x;
RA   Nagai H., Hamada T., Uchida T., Yamagoe S., Suzuki K.;
RT   "Systemic expression of a newly recognized protein, LECT2, in the human
RT   body.";
RL   Pathol. Int. 48:882-886(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-58.
RC   TISSUE=Liver;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-58.
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-58.
RC   TISSUE=Liver;
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   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8877413; DOI=10.1016/0165-2478(96)02572-2;
RA   Yamagoe S., Yamakawa Y., Matsuo Y., Minowada J., Mizuno S., Suzuki K.;
RT   "Purification and primary amino acid sequence of a novel neutrophil
RT   chemotactic factor LECT2.";
RL   Immunol. Lett. 52:9-13(1996).
RN   [8]
RP   DISULFIDE BONDS.
RX   PubMed=20103838;
RA   Okumura A., Suzuki T., Dohmae N., Okabe T., Hashimoto Y., Nakazato K.,
RA   Ohno H., Miyazaki Y., Yamagoe S.;
RT   "Identification and assignment of three disulfide bonds in mammalian
RT   leukocyte cell-derived chemotaxin 2 by matrix-assisted laser
RT   desorption/ionization time-of-flight mass spectrometry.";
RL   Biosci. Trends 3:139-143(2009).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 19-151 IN COMPLEX WITH ZINC ION,
RP   DISULFIDE BONDS, MUTAGENESIS OF TYR-104, AND INTERACTION WITH MET.
RX   PubMed=27334921; DOI=10.1074/jbc.m116.720375;
RA   Zheng H., Miyakawa T., Sawano Y., Asano A., Okumura A., Yamagoe S.,
RA   Tanokura M.;
RT   "Crystal structure of human leukocyte cell-derived chemotaxin 2 (LECT2)
RT   reveals a mechanistic basis of functional evolution in a mammalian protein
RT   with an M23 metalloendopeptidase fold.";
RL   J. Biol. Chem. 291:17133-17142(2016).
CC   -!- FUNCTION: Has a neutrophil chemotactic activity. Also a positive
CC       regulator of chondrocyte proliferation (PubMed:9524238). Does not show
CC       metalloendopeptidase activity (PubMed:27334921).
CC       {ECO:0000269|PubMed:27334921, ECO:0000269|PubMed:9524238}.
CC   -!- SUBUNIT: Interacts with MET. {ECO:0000269|PubMed:27334921}.
CC   -!- INTERACTION:
CC       O14960; O14960: LECT2; NbExp=3; IntAct=EBI-8307271, EBI-8307271;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8877413}. Secreted
CC       {ECO:0000269|PubMed:8877413}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in adult and fetal liver and
CC       weakly in testis. Not expressed in bone marrow.
CC       {ECO:0000269|PubMed:9524238, ECO:0000269|PubMed:9832057}.
CC   -!- INDUCTION: By phytohemagglutinin (PHA). {ECO:0000269|PubMed:9524238}.
CC   -!- SIMILARITY: Belongs to the LECT2/MIM-1 family. {ECO:0000305}.
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DR   EMBL; D63521; BAA23609.1; -; mRNA.
DR   EMBL; AB007546; BAA25669.1; -; Genomic_DNA.
DR   EMBL; AK314092; BAG36787.1; -; mRNA.
DR   EMBL; AC004763; AAC17734.1; -; Genomic_DNA.
DR   EMBL; AC002428; AAB66905.1; -; Genomic_DNA.
DR   EMBL; BC093670; AAH93670.1; -; mRNA.
DR   EMBL; BC101579; AAI01580.1; -; mRNA.
DR   CCDS; CCDS4190.1; -.
DR   RefSeq; NP_002293.2; NM_002302.2.
DR   PDB; 5B0H; X-ray; 1.94 A; A/B=19-151.
DR   PDB; 7N2I; EM; 1.40 A; A=63-71.
DR   PDB; 8G2V; EM; 2.71 A; A/B/C/D/E/F/G/H/I/J=73-93.
DR   PDBsum; 5B0H; -.
DR   PDBsum; 7N2I; -.
DR   PDBsum; 8G2V; -.
DR   AlphaFoldDB; O14960; -.
DR   BMRB; O14960; -.
DR   EMDB; EMD-29682; -.
DR   SMR; O14960; -.
DR   BioGRID; 110142; 24.
DR   IntAct; O14960; 2.
DR   MINT; O14960; -.
DR   STRING; 9606.ENSP00000274507; -.
DR   PhosphoSitePlus; O14960; -.
DR   BioMuta; LECT2; -.
DR   MassIVE; O14960; -.
DR   PaxDb; 9606-ENSP00000274507; -.
DR   PeptideAtlas; O14960; -.
DR   ProteomicsDB; 48336; -.
DR   Antibodypedia; 26441; 292 antibodies from 22 providers.
DR   DNASU; 3950; -.
DR   Ensembl; ENST00000274507.6; ENSP00000274507.1; ENSG00000145826.9.
DR   GeneID; 3950; -.
DR   KEGG; hsa:3950; -.
DR   MANE-Select; ENST00000274507.6; ENSP00000274507.1; NM_002302.3; NP_002293.2.
DR   UCSC; uc003lbe.1; human.
DR   AGR; HGNC:6550; -.
DR   CTD; 3950; -.
DR   DisGeNET; 3950; -.
DR   GeneCards; LECT2; -.
DR   HGNC; HGNC:6550; LECT2.
DR   HPA; ENSG00000145826; Tissue enriched (liver).
DR   MIM; 602882; gene.
DR   neXtProt; NX_O14960; -.
DR   OpenTargets; ENSG00000145826; -.
DR   PharmGKB; PA30330; -.
DR   VEuPathDB; HostDB:ENSG00000145826; -.
DR   eggNOG; ENOG502S16D; Eukaryota.
DR   GeneTree; ENSGT00390000015484; -.
DR   InParanoid; O14960; -.
DR   OMA; MCDSHGC; -.
DR   OrthoDB; 5352706at2759; -.
DR   PhylomeDB; O14960; -.
DR   TreeFam; TF331097; -.
DR   PathwayCommons; O14960; -.
DR   SignaLink; O14960; -.
DR   BioGRID-ORCS; 3950; 9 hits in 1144 CRISPR screens.
DR   GeneWiki; LECT2; -.
DR   GenomeRNAi; 3950; -.
DR   Pharos; O14960; Tbio.
DR   PRO; PR:O14960; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; O14960; Protein.
DR   Bgee; ENSG00000145826; Expressed in buccal mucosa cell and 112 other cell types or tissues.
DR   ExpressionAtlas; O14960; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR008663; LECT2.
DR   InterPro; IPR017381; LECT2_chordata.
DR   InterPro; IPR016047; Peptidase_M23.
DR   PANTHER; PTHR11329; LEUKOCYTE CELL-DERIVED CHEMOTAXIN 2; 1.
DR   PANTHER; PTHR11329:SF0; LEUKOCYTE CELL-DERIVED CHEMOTAXIN-2; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   PIRSF; PIRSF038085; LECT3; 1.
DR   Genevisible; O14960; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Chemotaxis; Cytoplasm; Disulfide bond; Metal-binding;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250|UniProtKB:O62644"
FT   CHAIN           19..151
FT                   /note="Leukocyte cell-derived chemotaxin-2"
FT                   /id="PRO_0000017364"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:27334921,
FT                   ECO:0007744|PDB:5B0H"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:27334921,
FT                   ECO:0007744|PDB:5B0H"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:27334921,
FT                   ECO:0007744|PDB:5B0H"
FT   DISULFID        25..60
FT                   /evidence="ECO:0000269|PubMed:20103838,
FT                   ECO:0000269|PubMed:27334921, ECO:0007744|PDB:5B0H"
FT   DISULFID        36..41
FT                   /evidence="ECO:0000269|PubMed:20103838,
FT                   ECO:0000269|PubMed:27334921, ECO:0007744|PDB:5B0H"
FT   DISULFID        99..142
FT                   /evidence="ECO:0000269|PubMed:20103838,
FT                   ECO:0000269|PubMed:27334921, ECO:0007744|PDB:5B0H"
FT   VARIANT         58
FT                   /note="I -> V (in dbSNP:rs31517)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15372022, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9524238, ECO:0000269|PubMed:9545637,
FT                   ECO:0000269|PubMed:9832057"
FT                   /id="VAR_011386"
FT   MUTAGEN         104
FT                   /note="Y->H: No metalloendopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:27334921"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   STRAND          55..59
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   STRAND          69..77
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:8G2V"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   STRAND          98..108
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   STRAND          118..123
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   STRAND          136..141
FT                   /evidence="ECO:0007829|PDB:5B0H"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:5B0H"
SQ   SEQUENCE   151 AA;  16390 MW;  3C1DFCA1B4F8792F CRC64;
     MFSTKALLLA GLISTALAGP WANICAGKSS NEIRTCDRHG CGQYSAQRSQ RPHQGVDILC
     SAGSTVYAPF TGMIVGQEKP YQNKNAINNG VRISGRGFCV KMFYIKPIKY KGPIKKGEKL
     GTLLPLQKVY PGIQSHVHIE NCDSSDPTAY L
//