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Regenerating islet-derived protein 3-beta (REG-3-beta) (Pancreatitis-associated protein 1) (Peptide 23) (REG-2) (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_RAT               Reviewed;         175 AA.
P25031; Q64102; Q64231;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
22-NOV-2017, entry version 133.
RecName: Full=Regenerating islet-derived protein 3-beta;
Short=REG-3-beta;
AltName: Full=Pancreatitis-associated protein 1;
AltName: Full=Peptide 23;
AltName: Full=REG-2;
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, Reg2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 27-39.
STRAIN=Sprague-Dawley; TISSUE=Pancreas;
PubMed=1722211;
Iovanna J., Orelle B., Keim V., Dagorn J.-C.;
"Messenger RNA sequence and expression of rat pancreatitis-associated
protein, a lectin-related protein overexpressed during acute
experimental pancreatitis.";
J. Biol. Chem. 266:24664-24669(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Intestine;
PubMed=8238345;
Iovanna J.L., Keim V., Bosshard A., Orelle B., Frigerio J.-M.,
Dusetti N., Dagorn J.-C.;
"PAP, a pancreatic secretory protein induced during acute
pancreatitis, is expressed in rat intestine.";
Am. J. Physiol. 265:G611-G618(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Wistar; TISSUE=Liver;
PubMed=8314803;
Dusetti N.J., Frigerio J.-M., Keim V., Dagorn J.-C., Iovanna J.;
"Structural organization of the gene encoding the rat pancreatitis-
associated protein. Analysis of its evolutionary history reveals an
ancient divergence from the other carbohydrate-recognition domain-
containing genes.";
J. Biol. Chem. 268:14470-14475(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1511905; DOI=10.1016/0378-1119(92)90206-5;
Kamimura T., West C., Beutler E.;
"Sequence of a cDNA clone encoding a rat Reg-2 protein.";
Gene 118:299-300(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Sprague-Dawley; TISSUE=Pituitary;
PubMed=7895644; DOI=10.1210/endo.136.4.7895644;
Katsumata N., Chakraborty C., Myal Y., Schroedter I.C., Murphy L.J.,
Shiu R.P., Friesen H.G.;
"Molecular cloning and expression of peptide 23, a growth hormone-
releasing hormone-inducible pituitary protein.";
Endocrinology 136:1332-1339(1995).
-!- FUNCTION: Bactericidal C-type lectin which acts against several
intestinal Gram-positive bacteria 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 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Note=Found in the apical region of
pancreatic acinar cells.
-!- TISSUE SPECIFICITY: Constitutively expressed in intestine.
-!- INDUCTION: Appears in pancreatic juice after induction of
pancreatic inflammation. Secreted also by pituitary cells; the
secretion there is stimulated by GH-releasing hormone and
inhibited by somatostatin.
-!- 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:0000250}.
-!- DISEASE: Note=Overexpressed during the acute phase of
pancreatitis.
-!- SEQUENCE CAUTION:
Sequence=AAA41805.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M55149; AAA41807.1; -; mRNA.
EMBL; M98049; AAA16341.1; -; mRNA.
EMBL; L07127; AAA41805.1; ALT_INIT; Genomic_DNA.
EMBL; S43715; AAB23103.1; -; mRNA.
EMBL; S77413; AAB33848.2; -; mRNA.
PIR; A37456; A41719.
RefSeq; NP_445741.1; NM_053289.1.
UniGene; Rn.9727; -.
ProteinModelPortal; P25031; -.
SMR; P25031; -.
STRING; 10116.ENSRNOP00000008212; -.
MEROPS; I63.002; -.
PaxDb; P25031; -.
PRIDE; P25031; -.
GeneID; 24618; -.
KEGG; rno:24618; -.
UCSC; RGD:3254; rat.
CTD; 18489; -.
RGD; 3254; Reg3b.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
HOGENOM; HOG000010281; -.
HOVERGEN; HBG004151; -.
InParanoid; P25031; -.
OrthoDB; EOG091G0MDY; -.
PhylomeDB; P25031; -.
PRO; PR:P25031; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P25031; RN.
GO; GO:0045177; C:apical part of cell; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0042588; C:zymogen granule; IDA:RGD.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; IPI:RGD.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:1903577; P:cellular response to L-arginine; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
GO; GO:0044849; P:estrous cycle; IEP:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0007494; P:midgut development; IEP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IEP:RGD.
GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IDA:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0042594; P:response to starvation; IEP:RGD.
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;
Direct protein sequencing; Disulfide bond; Inflammatory response;
Lectin; Reference proteome; Secreted; Signal.
SIGNAL 1 26 {ECO:0000269|PubMed:1722211}.
CHAIN 27 175 Regenerating islet-derived protein 3-beta
16.5 kDa form.
/FTId=PRO_0000017433.
PROPEP 27 37 {ECO:0000250}.
/FTId=PRO_0000422749.
CHAIN 38 175 Regenerating islet-derived protein 3-beta
15 kDa form.
/FTId=PRO_0000422750.
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}.
CONFLICT 7 7 F -> S (in Ref. 4; AAB23103).
{ECO:0000305}.
CONFLICT 123 123 S -> T (in Ref. 5; AAB33848).
{ECO:0000305}.
SEQUENCE 175 AA; 19617 MW; C43892BF31B0B525 CRC64;
MLHRLAFPVM SWMLLSCLML LSQVQGEDSP KKIPSARISC PKGSQAYGSY CYALFQIPQT
WFDAELACQK RPEGHLVSVL NVAEASFLAS MVKNTGNSYQ YTWIGLHDPT LGGEPNGGGW
EWSNNDIMNY VNWERNPSTA LDRGFCGSLS RSSGFLRWRD TTCEVKLPYV CKFTG


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