REG3B_MOUSE
ID REG3B_MOUSE Reviewed; 175 AA.
AC P35230;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Regenerating islet-derived protein 3-beta;
DE Short=REG-3-beta;
DE AltName: Full=Pancreatitis-associated protein 1;
DE AltName: Full=Regenerating islet-derived protein III-beta;
DE Short=Reg III-beta;
DE Contains:
DE RecName: Full=Regenerating islet-derived protein 3-beta 16.5 kDa form;
DE Contains:
DE RecName: Full=Regenerating islet-derived protein 3-beta 15 kDa form;
DE Flags: Precursor;
GN Name=Reg3b; Synonyms=Pap, Pap1;
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 [MRNA].
RC TISSUE=Pancreas, and Small intestine;
RX PubMed=7679928; DOI=10.1016/0167-4781(93)90290-t;
RA Itoh T., Teraoka H.;
RT "Cloning and tissue-specific expression of cDNAs for the human and mouse
RT homologues of rat pancreatitis-associated protein (PAP).";
RL Biochim. Biophys. Acta 1172:184-186(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=9055810; DOI=10.1016/s0378-1119(96)00589-6;
RA Narushima Y., Unno M., Nakagawara K., Mori M., Miyashita H., Suzuki Y.,
RA Noguchi N., Takasawa S., Kumagai T., Yonekura H., Okamoto H.;
RT "Structure, chromosomal localization and expression of mouse genes encoding
RT type III Reg, RegIII alpha, RegIII beta, RegIII gamma.";
RL Gene 185:159-168(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
RN [5]
RP FUNCTION, INDUCTION, AND PROTEOLYTIC PROCESSING.
RX PubMed=21694778; DOI=10.1371/journal.pone.0020749;
RA Stelter C., Kaeppeli R., Koenig C., Krah A., Hardt W.D., Stecher B.,
RA Bumann D.;
RT "Salmonella-induced mucosal lectin RegIII? kills competing gut
RT microbiota.";
RL PLoS ONE 6:E20749-E20749(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22252863; DOI=10.1128/iai.06165-11;
RA van Ampting M.T., Loonen L.M., Schonewille A.J., Konings I., Vink C.,
RA Iovanna J., Chamaillard M., Dekker J., van der Meer R., Wells J.M.,
RA Bovee-Oudenhoven I.M.;
RT "Intestinally secreted C-type lectin Reg3b attenuates salmonellosis but not
RT listeriosis in mice.";
RL Infect. Immun. 80:1115-1120(2012).
CC -!- FUNCTION: Bactericidal C-type lectin which acts against several
CC intestinal Gram-positive and Gram-negative bacteria. Lacks
CC antibacterial activity against S.typhimurium. May play a role in
CC protection against infection with S.enteritidis by inhibiting its
CC translocation from the gut lumen into intestinal tissues and further
CC extraintestinal tissues. {ECO:0000269|PubMed:21694778,
CC ECO:0000269|PubMed:22252863}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Found in the apical region of
CC pancreatic acinar cells. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in the small intestine,
CC moderately in colon and at an extremely low level in healthy pancreas.
CC -!- INDUCTION: Up-regulated in the intestine by S.typhimurium infection (at
CC protein level). Appears in pancreatic juice after induction of
CC pancreatic inflammation. {ECO:0000269|PubMed:21694778}.
CC -!- DOMAIN: The EPN motif is essential for recognition of the peptidoglycan
CC carbohydrate backbone and for efficient bacterial killing with Glu-114
CC playing a key role in peptidoglycan binding and bactericidal activity.
CC {ECO:0000250}.
CC -!- PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal
CC propeptide and is essential for peptidoglycan binding and antibacterial
CC activity. {ECO:0000269|PubMed:21694778}.
CC -!- DISEASE: Note=Overexpressed during the acute phase of pancreatitis.
CC -!- DISRUPTION PHENOTYPE: Mice are more susceptible to salmonellosis, but
CC not listeriosis. {ECO:0000269|PubMed:22252863}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Pancreatitis-associated protein 1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_184";
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DR EMBL; D13509; BAA02727.1; -; mRNA.
DR EMBL; D63359; BAA18928.1; -; mRNA.
DR EMBL; D63360; BAA18929.1; -; Genomic_DNA.
DR EMBL; BC027525; AAH27525.1; -; mRNA.
DR CCDS; CCDS20253.1; -.
DR PIR; S29822; S29822.
DR RefSeq; NP_035166.1; NM_011036.1.
DR AlphaFoldDB; P35230; -.
DR SMR; P35230; -.
DR STRING; 10090.ENSMUSP00000094667; -.
DR MaxQB; P35230; -.
DR PaxDb; P35230; -.
DR PeptideAtlas; P35230; -.
DR PRIDE; P35230; -.
DR ProteomicsDB; 255060; -.
DR DNASU; 18489; -.
DR Ensembl; ENSMUST00000096904; ENSMUSP00000094667; ENSMUSG00000071356.
DR GeneID; 18489; -.
DR KEGG; mmu:18489; -.
DR UCSC; uc009cjw.1; mouse.
DR CTD; 18489; -.
DR MGI; MGI:97478; Reg3b.
DR VEuPathDB; HostDB:ENSMUSG00000071356; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154447; -.
DR HOGENOM; CLU_049894_18_0_1; -.
DR InParanoid; P35230; -.
DR OMA; NCDVRLP; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; P35230; -.
DR BioGRID-ORCS; 18489; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Reg3b; mouse.
DR PRO; PR:P35230; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P35230; protein.
DR Bgee; ENSMUSG00000071356; Expressed in paneth cell and 62 other tissues.
DR ExpressionAtlas; P35230; baseline and differential.
DR Genevisible; P35230; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042588; C:zymogen granule; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070492; F:oligosaccharide binding; ISO:MGI.
DR GO; GO:0042834; F:peptidoglycan binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0044278; P:cell wall disruption in another organism; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
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 Acute phase; Antimicrobial; Disulfide bond; Inflammatory response; Lectin;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..175
FT /note="Regenerating islet-derived protein 3-beta 16.5 kDa
FT form"
FT /id="PRO_0000017432"
FT PROPEP 27..37
FT /evidence="ECO:0000250"
FT /id="PRO_0000422747"
FT CHAIN 38..175
FT /note="Regenerating islet-derived protein 3-beta 15 kDa
FT form"
FT /id="PRO_0000422748"
FT DOMAIN 47..172
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 114..116
FT /note="EPN"
FT /evidence="ECO:0000250"
FT DISULFID 40..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 68..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 146..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 175 AA; 19476 MW; 44B3101171E79775 CRC64;
MLPPTACSVM SWMLLSCLML LSQVQGEDSL KNIPSARISC PKGSQAYGSY CYALFQIPQT
WFDAELACQK RPGGHLVSVL NSAEASFLSS MVKRTGNSYQ YTWIGLHDPT LGAEPNGGGW
EWSNNDVMNY FNWERNPSTA LDRAFCGSLS RASGFLKWRD MTCEVKLPYV CKFTG
