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LIT2_MOUSE
ID   LIT2_MOUSE              Reviewed;         173 AA.
AC   Q08731;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Lithostathine-2;
DE   AltName: Full=Islet of Langerhans regenerating protein 2;
DE            Short=REG-2;
DE   AltName: Full=Pancreatic stone protein 2;
DE            Short=PSP;
DE   AltName: Full=Pancreatic thread protein 2;
DE            Short=PTP;
DE   Flags: Precursor;
GN   Name=Reg2;
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=8340418; DOI=10.1016/s0021-9258(18)82347-x;
RA   Unno M., Yonekura H., Nakagawara K., Watanabe T., Miyashita H.,
RA   Moriizumi S., Okamoto H., Itoh T., Teraoka H.;
RT   "Structure, chromosomal localization, and expression of mouse reg genes,
RT   reg I and reg II. A novel type of reg gene, reg II, exists in the mouse
RT   genome.";
RL   J. Biol. Chem. 268:15974-15982(1993).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate
CC       precipitation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed only in regenerating islets and normal
CC       exocrine pancreas, but not in normal pancreatic islets. Expressed
CC       strongly in pancreas, weakly in liver, but not at all in gall bladder.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Litho/Reg 1beta;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_183";
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DR   EMBL; D14011; BAA03112.1; -; Genomic_DNA.
DR   CCDS; CCDS20256.1; -.
DR   PIR; B47148; B47148.
DR   RefSeq; NP_033069.1; NM_009043.1.
DR   AlphaFoldDB; Q08731; -.
DR   SMR; Q08731; -.
DR   STRING; 10090.ENSMUSP00000023906; -.
DR   MEROPS; I63.002; -.
DR   iPTMnet; Q08731; -.
DR   PhosphoSitePlus; Q08731; -.
DR   PaxDb; Q08731; -.
DR   PeptideAtlas; Q08731; -.
DR   PRIDE; Q08731; -.
DR   ProteomicsDB; 292336; -.
DR   DNASU; 19693; -.
DR   Ensembl; ENSMUST00000023906; ENSMUSP00000023906; ENSMUSG00000023140.
DR   GeneID; 19693; -.
DR   KEGG; mmu:19693; -.
DR   UCSC; uc009cjz.1; mouse.
DR   CTD; 19693; -.
DR   MGI; MGI:97896; Reg2.
DR   VEuPathDB; HostDB:ENSMUSG00000023140; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000162393; -.
DR   HOGENOM; CLU_049894_18_0_1; -.
DR   InParanoid; Q08731; -.
DR   OMA; QTNSFFM; -.
DR   OrthoDB; 1509611at2759; -.
DR   PhylomeDB; Q08731; -.
DR   BioGRID-ORCS; 19693; 0 hits in 74 CRISPR screens.
DR   ChiTaRS; Reg2; mouse.
DR   PRO; PR:Q08731; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q08731; protein.
DR   Bgee; ENSMUSG00000023140; Expressed in pyloric antrum and 34 other tissues.
DR   ExpressionAtlas; Q08731; baseline and differential.
DR   Genevisible; Q08731; MM.
DR   GO; GO:0045178; C:basal part of cell; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0042588; C:zymogen granule; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0070492; F:oligosaccharide binding; IBA:GO_Central.
DR   GO; GO:0042834; F:peptidoglycan binding; IBA:GO_Central.
DR   GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR   GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR   GO; GO:0044278; P:cell wall disruption in another organism; IBA:GO_Central.
DR   GO; GO:0042552; P:myelination; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:1904699; P:positive regulation of acinar cell proliferation; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; ISO:MGI.
DR   GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
DR   GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Lectin; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..173
FT                   /note="Lithostathine-2"
FT                   /id="PRO_0000017427"
FT   DOMAIN          41..171
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        43..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        71..169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        144..161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   173 AA;  19407 MW;  7D34C4DAB232F25C CRC64;
     MAQNNVYLIL FLCLMFLSYS QGQVAEEDFP LAEKDLPSAK INCPEGANAY GSYCYYLIED
     RLTWGEADLF CQNMNAGHLV SILSQAESNF VASLVKESGT TASNVWTGLH DPKSNRRWHW
     SSGSLFLFKS WATGAPSTAN RGYCVSLTSN TAYKKWKDEN CEAQYSFVCK FRA
 
 
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