LECT2_MOUSE
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 03-AUG-2022, entry version 140.
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; O88803; -.
DR PeptideAtlas; O88803; -.
DR PRIDE; 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 CTD; 3950; -.
DR MGI; MGI:1278342; Lect2.
DR eggNOG; ENOG502S16D; Eukaryota.
DR InParanoid; O88803; -.
DR OrthoDB; 1298781at2759; -.
DR PhylomeDB; O88803; -.
DR TreeFam; TF331097; -.
DR BioGRID-ORCS; 16841; 1 hit in 72 CRISPR screens.
DR PRO; PR:O88803; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88803; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR008663; LECT2.
DR InterPro; IPR017381; LECT2_chordata.
DR PANTHER; PTHR11329; PTHR11329; 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
