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 13-FEB-2019, entry version 135. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT mapping of 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 RT human 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA 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 RT project: 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 RP ION, DISULFIDE BONDS, MUTAGENESIS OF TYR-104, AND INTERACTION WITH RP 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 RT (LECT2) reveals a mechanistic basis of functional evolution in a RT mammalian protein 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 CC show 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 Self; NbExp=3; IntAct=EBI-8307271, EBI-8307271; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8877413}. CC Secreted {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). CC {ECO:0000269|PubMed:9524238}. CC -!- SIMILARITY: Belongs to the LECT2/MIM-1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 UniGene; Hs.512580; -. DR PDB; 5B0H; X-ray; 1.94 A; A/B=19-151. DR PDBsum; 5B0H; -. DR ProteinModelPortal; O14960; -. DR SMR; O14960; -. DR IntAct; O14960; 2. DR MINT; O14960; -. DR STRING; 9606.ENSP00000274507; -. DR PhosphoSitePlus; O14960; -. DR BioMuta; LECT2; -. DR PaxDb; O14960; -. DR PeptideAtlas; O14960; -. DR PRIDE; O14960; -. DR ProteomicsDB; 48336; -. DR Ensembl; ENST00000274507; ENSP00000274507; ENSG00000145826. DR GeneID; 3950; -. DR KEGG; hsa:3950; -. DR UCSC; uc003lbe.1; human. DR CTD; 3950; -. DR DisGeNET; 3950; -. DR EuPathDB; HostDB:ENSG00000145826.8; -. DR GeneCards; LECT2; -. DR H-InvDB; HIX0032112; -. DR HGNC; HGNC:6550; LECT2. DR HPA; HPA043883; -. DR MIM; 602882; gene. DR neXtProt; NX_O14960; -. DR OpenTargets; ENSG00000145826; -. DR PharmGKB; PA30330; -. DR eggNOG; ENOG410IJ84; Eukaryota. DR eggNOG; ENOG410XVAU; LUCA. DR GeneTree; ENSGT00390000015484; -. DR HOGENOM; HOG000113312; -. DR HOVERGEN; HBG052320; -. DR InParanoid; O14960; -. DR OMA; SHGCGQY; -. DR OrthoDB; 1298781at2759; -. DR PhylomeDB; O14960; -. DR TreeFam; TF331097; -. DR GeneWiki; LECT2; -. DR GenomeRNAi; 3950; -. DR PRO; PR:O14960; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000145826; Expressed in 81 organ(s), highest expression level in liver. DR ExpressionAtlas; O14960; baseline and differential. DR Genevisible; O14960; HS. 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; -; 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; Complete proteome; Cytoplasm; KW Disulfide bond; Metal-binding; Polymorphism; Reference proteome; KW Secreted; Signal; Zinc. FT SIGNAL 1 18 {ECO:0000250|UniProtKB:O62644}. FT CHAIN 19 151 Leukocyte cell-derived chemotaxin-2. FT /FTId=PRO_0000017364. FT METAL 53 53 Zinc. {ECO:0000244|PDB:5B0H, FT ECO:0000269|PubMed:27334921}. FT METAL 57 57 Zinc. {ECO:0000244|PDB:5B0H, FT ECO:0000269|PubMed:27334921}. FT METAL 138 138 Zinc. {ECO:0000244|PDB:5B0H, FT ECO:0000269|PubMed:27334921}. FT DISULFID 25 60 {ECO:0000244|PDB:5B0H, FT ECO:0000269|PubMed:20103838, FT ECO:0000269|PubMed:27334921}. FT DISULFID 36 41 {ECO:0000244|PDB:5B0H, FT ECO:0000269|PubMed:20103838, FT ECO:0000269|PubMed:27334921}. FT DISULFID 99 142 {ECO:0000244|PDB:5B0H, FT ECO:0000269|PubMed:20103838, FT ECO:0000269|PubMed:27334921}. FT VARIANT 58 58 I -> V (in dbSNP:rs31517). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15372022, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9524238, FT ECO:0000269|PubMed:9545637, FT ECO:0000269|PubMed:9832057}. FT /FTId=VAR_011386. FT MUTAGEN 104 104 Y->H: No metalloendopeptidase activity. FT {ECO:0000269|PubMed:27334921}. FT STRAND 49 51 {ECO:0000244|PDB:5B0H}. FT STRAND 55 59 {ECO:0000244|PDB:5B0H}. FT STRAND 65 67 {ECO:0000244|PDB:5B0H}. FT STRAND 69 77 {ECO:0000244|PDB:5B0H}. FT STRAND 90 95 {ECO:0000244|PDB:5B0H}. FT STRAND 98 108 {ECO:0000244|PDB:5B0H}. FT STRAND 110 114 {ECO:0000244|PDB:5B0H}. FT STRAND 118 123 {ECO:0000244|PDB:5B0H}. FT HELIX 126 129 {ECO:0000244|PDB:5B0H}. FT STRAND 136 141 {ECO:0000244|PDB:5B0H}. FT HELIX 148 150 {ECO:0000244|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 //