LECT2_HUMAN
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 03-AUG-2022, entry version 153.
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 PDBsum; 5B0H; -.
DR AlphaFoldDB; O14960; -.
DR BMRB; O14960; -.
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; O14960; -.
DR PeptideAtlas; O14960; -.
DR PRIDE; O14960; -.
DR ProteomicsDB; 48336; -.
DR Antibodypedia; 26441; 283 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 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; 1298781at2759; -.
DR PhylomeDB; O14960; -.
DR TreeFam; TF331097; -.
DR PathwayCommons; O14960; -.
DR SignaLink; O14960; -.
DR BioGRID-ORCS; 3950; 9 hits in 1066 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 110 other tissues.
DR ExpressionAtlas; O14960; baseline and differential.
DR Genevisible; O14960; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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; -; 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 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 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
