ID   LECT2_MOUSE             Reviewed;         151 AA.
AC   O88803; O88804; Q3V287; Q8K181; Q9QWN3; Q9Z337;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Leukocyte cell-derived chemotaxin-2;
DE            Short=LECT-2;
DE   AltName: Full=Chondromodulin II;
DE            Short=ChM-II;
DE   Flags: Precursor;
GN   Name=Lect2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   VAL-129.
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=9714793; DOI=10.1016/s0378-1119(98)00294-7;
RA   Yamagoe S., Watanabe T., Mizuno S., Suzuki K.;
RT   "The mouse Lect2 gene: cloning of cDNA and genomic DNA, structural
RT   characterization and chromosomal localization.";
RL   Gene 216:171-178(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster / NIH; TISSUE=Embryo, and Liver;
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] (ISOFORM 1), AND VARIANT VAL-129.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-129.
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-129.
RC   STRAIN=FVB/N; 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   [6]
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).
CC   -!- FUNCTION: Has a neutrophil chemotactic activity. Also a positive
CC       regulator of chondrocyte proliferation. {ECO:0000269|PubMed:10050029}.
CC   -!- INTERACTION:
CC       O88803; O88803: Lect2; NbExp=8; IntAct=EBI-8307190, EBI-8307190;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O14960}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=LECT2;
CC         IsoId=O88803-1; Sequence=Displayed;
CC       Name=2; Synonyms=LECT2Q;
CC         IsoId=O88803-2; Sequence=VSP_003051;
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and weakly in testis. Not
CC       expressed in heart, brain, spleen, lung, skeletal muscle and kidney.
CC       {ECO:0000269|PubMed:10050029}.
CC   -!- SIMILARITY: Belongs to the LECT2/MIM-1 family. {ECO:0000305}.
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DR   EMBL; AB009687; BAA33383.1; -; mRNA.
DR   EMBL; AB009688; BAA33384.1; -; mRNA.
DR   EMBL; AB009689; BAA33385.1; -; Genomic_DNA.
DR   EMBL; AB009689; BAA33386.1; -; Genomic_DNA.
DR   EMBL; AF035161; AAF13302.1; -; mRNA.
DR   EMBL; AK131971; BAE20911.1; -; mRNA.
DR   EMBL; CH466546; EDL41242.1; -; Genomic_DNA.
DR   EMBL; BC027753; AAH27753.1; -; mRNA.
DR   CCDS; CCDS26564.1; -. [O88803-1]
DR   RefSeq; NP_034832.2; NM_010702.2.
DR   AlphaFoldDB; O88803; -.
DR   SMR; O88803; -.
DR   MINT; O88803; -.
DR   STRING; 10090.ENSMUSP00000060495; -.
DR   iPTMnet; O88803; -.
DR   PhosphoSitePlus; O88803; -.
DR   CPTAC; non-CPTAC-3988; -.
DR   MaxQB; O88803; -.
DR   PaxDb; 10090-ENSMUSP00000060495; -.
DR   PeptideAtlas; O88803; -.
DR   ProteomicsDB; 265057; -. [O88803-1]
DR   ProteomicsDB; 265058; -. [O88803-2]
DR   DNASU; 16841; -.
DR   GeneID; 16841; -.
DR   KEGG; mmu:16841; -.
DR   UCSC; uc007qst.2; mouse. [O88803-1]
DR   UCSC; uc011zad.1; mouse. [O88803-2]
DR   AGR; MGI:1278342; -.
DR   CTD; 3950; -.
DR   MGI; MGI:1278342; Lect2.
DR   eggNOG; ENOG502S16D; Eukaryota.
DR   InParanoid; O88803; -.
DR   OrthoDB; 5352706at2759; -.
DR   PhylomeDB; O88803; -.
DR   TreeFam; TF331097; -.
DR   BioGRID-ORCS; 16841; 1 hit in 77 CRISPR screens.
DR   PRO; PR:O88803; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O88803; Protein.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:MGI.
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   PANTHER; PTHR11329; LEUKOCYTE CELL-DERIVED CHEMOTAXIN 2; 1.
DR   PANTHER; PTHR11329:SF0; LEUKOCYTE CELL-DERIVED CHEMOTAXIN-2; 1.
DR   PIRSF; PIRSF038085; LECT3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chemotaxis; 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_0000017365"
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:0000269|PubMed:20103838"
FT   DISULFID        36..41
FT                   /evidence="ECO:0000269|PubMed:20103838"
FT   DISULFID        99..142
FT                   /evidence="ECO:0000269|PubMed:20103838"
FT   VAR_SEQ         98..151
FT                   /note="FCVKIFYIKPIKYKGSIKKGEKLGTLLPLQKIYPGIQSHVHVENCDSSDPTA
FT                   YL -> QRLQAHTTTLNVFTCYWDKIQIPRPTRFLCQNFLH (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9714793"
FT                   /id="VSP_003051"
FT   VARIANT         129
FT                   /note="I -> V"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:9714793,
FT                   ECO:0000269|Ref.4"
FT   CONFLICT        100
FT                   /note="V -> F (in Ref. 5; AAH27753)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  16405 MW;  18AF444046B7AE8E CRC64;
     MIPTTILISA ALLSSALAGP WANICASKSS NEIRTCDSYG CGQYSAQRTQ RHHPGVDVLC
     SDGSVVYAPF TGKIVGQEKP YRNKNAINDG IRLSGRGFCV KIFYIKPIKY KGSIKKGEKL
     GTLLPLQKIY PGIQSHVHVE NCDSSDPTAY L
//