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Regenerating islet-derived protein 3-beta (REG-3-beta) (Pancreatitis-associated protein 1) (Regenerating islet-derived protein III-beta) (Reg III-beta) [Cleaved into: Regenerating islet-derived protein 3-beta 16.5 kDa form; Regenerating islet-derived protein 3-beta 15 kDa form]

 REG3B_MOUSE             Reviewed;         175 AA.
P35230;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
20-DEC-2017, entry version 131.
RecName: Full=Regenerating islet-derived protein 3-beta;
Short=REG-3-beta;
AltName: Full=Pancreatitis-associated protein 1;
AltName: Full=Regenerating islet-derived protein III-beta;
Short=Reg III-beta;
Contains:
RecName: Full=Regenerating islet-derived protein 3-beta 16.5 kDa form;
Contains:
RecName: Full=Regenerating islet-derived protein 3-beta 15 kDa form;
Flags: Precursor;
Name=Reg3b; Synonyms=Pap, Pap1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas, and Small intestine;
PubMed=7679928; DOI=10.1016/0167-4781(93)90290-T;
Itoh T., Teraoka H.;
"Cloning and tissue-specific expression of cDNAs for the human and
mouse homologues of rat pancreatitis-associated protein (PAP).";
Biochim. Biophys. Acta 1172:184-186(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=9055810; DOI=10.1016/S0378-1119(96)00589-6;
Narushima Y., Unno M., Nakagawara K., Mori M., Miyashita H.,
Suzuki Y., Noguchi N., Takasawa S., Kumagai T., Yonekura H.,
Okamoto H.;
"Structure, chromosomal localization and expression of mouse genes
encoding type III Reg, RegIII alpha, RegIII beta, RegIII gamma.";
Gene 185:159-168(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
FUNCTION, INDUCTION, AND PROTEOLYTIC PROCESSING.
PubMed=21694778; DOI=10.1371/journal.pone.0020749;
Stelter C., Kaeppeli R., Koenig C., Krah A., Hardt W.D., Stecher B.,
Bumann D.;
"Salmonella-induced mucosal lectin RegIII? kills competing gut
microbiota.";
PLoS ONE 6:E20749-E20749(2011).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22252863; DOI=10.1128/IAI.06165-11;
van Ampting M.T., Loonen L.M., Schonewille A.J., Konings I., Vink C.,
Iovanna J., Chamaillard M., Dekker J., van der Meer R., Wells J.M.,
Bovee-Oudenhoven I.M.;
"Intestinally secreted C-type lectin Reg3b attenuates salmonellosis
but not listeriosis in mice.";
Infect. Immun. 80:1115-1120(2012).
-!- FUNCTION: Bactericidal C-type lectin which acts against several
intestinal Gram-positive and Gram-negative bacteria. Lacks
antibacterial activity against S.typhimurium. May play a role in
protection against infection with S.enteritidis by inhibiting its
translocation from the gut lumen into intestinal tissues and
further extraintestinal tissues. {ECO:0000269|PubMed:21694778,
ECO:0000269|PubMed:22252863}.
-!- SUBCELLULAR LOCATION: Secreted. Note=Found in the apical region of
pancreatic acinar cells. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Constitutively expressed in the small
intestine, moderately in colon and at an extremely low level in
healthy pancreas.
-!- INDUCTION: Up-regulated in the intestine by S.typhimurium
infection (at protein level). Appears in pancreatic juice after
induction of pancreatic inflammation.
{ECO:0000269|PubMed:21694778}.
-!- DOMAIN: The EPN motif is essential for recognition of the
peptidoglycan carbohydrate backbone and for efficient bacterial
killing with Glu-114 playing a key role in peptidoglycan binding
and bactericidal activity. {ECO:0000250}.
-!- PTM: Proteolytic processing by trypsin removes an inhibitory N-
terminal propeptide and is essential for peptidoglycan binding and
antibacterial activity. {ECO:0000269|PubMed:21694778}.
-!- DISEASE: Note=Overexpressed during the acute phase of
pancreatitis.
-!- DISRUPTION PHENOTYPE: Mice are more susceptible to salmonellosis,
but not listeriosis. {ECO:0000269|PubMed:22252863}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Pancreatitis-associated protein 1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_184";
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EMBL; D13509; BAA02727.1; -; mRNA.
EMBL; D63359; BAA18928.1; -; mRNA.
EMBL; D63360; BAA18929.1; -; Genomic_DNA.
EMBL; BC027525; AAH27525.1; -; mRNA.
CCDS; CCDS20253.1; -.
PIR; S29822; S29822.
RefSeq; NP_035166.1; NM_011036.1.
UniGene; Mm.2553; -.
ProteinModelPortal; P35230; -.
SMR; P35230; -.
STRING; 10090.ENSMUSP00000094667; -.
MaxQB; P35230; -.
PaxDb; P35230; -.
PeptideAtlas; P35230; -.
PRIDE; P35230; -.
DNASU; 18489; -.
Ensembl; ENSMUST00000096904; ENSMUSP00000094667; ENSMUSG00000071356.
GeneID; 18489; -.
KEGG; mmu:18489; -.
UCSC; uc009cjw.1; mouse.
CTD; 18489; -.
MGI; MGI:97478; Reg3b.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00700000104249; -.
HOGENOM; HOG000010281; -.
HOVERGEN; HBG004151; -.
InParanoid; P35230; -.
OMA; VKLPYVC; -.
OrthoDB; EOG091G0MDY; -.
PhylomeDB; P35230; -.
Reactome; R-MMU-6803157; Antimicrobial peptides.
PRO; PR:P35230; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000071356; -.
CleanEx; MM_REG3B; -.
ExpressionAtlas; P35230; baseline and differential.
Genevisible; P35230; MM.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
Acute phase; Antimicrobial; Complete proteome; Disulfide bond;
Inflammatory response; Lectin; Reference proteome; Secreted; Signal.
SIGNAL 1 26 {ECO:0000250}.
CHAIN 27 175 Regenerating islet-derived protein 3-beta
16.5 kDa form.
/FTId=PRO_0000017432.
PROPEP 27 37 {ECO:0000250}.
/FTId=PRO_0000422747.
CHAIN 38 175 Regenerating islet-derived protein 3-beta
15 kDa form.
/FTId=PRO_0000422748.
DOMAIN 47 172 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
MOTIF 114 116 EPN. {ECO:0000250}.
DISULFID 40 51 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 68 171 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 146 163 {ECO:0000255|PROSITE-ProRule:PRU00040}.
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


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