REG3B_RAT
ID REG3B_RAT Reviewed; 175 AA.
AC P25031; Q64102; Q64231;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Regenerating islet-derived protein 3-beta;
DE Short=REG-3-beta;
DE AltName: Full=Pancreatitis-associated protein 1;
DE AltName: Full=Peptide 23;
DE AltName: Full=REG-2;
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, Reg2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 27-39.
RC STRAIN=Sprague-Dawley; TISSUE=Pancreas;
RX PubMed=1722211; DOI=10.1016/s0021-9258(18)54281-2;
RA Iovanna J., Orelle B., Keim V., Dagorn J.-C.;
RT "Messenger RNA sequence and expression of rat pancreatitis-associated
RT protein, a lectin-related protein overexpressed during acute experimental
RT pancreatitis.";
RL J. Biol. Chem. 266:24664-24669(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Intestine;
RX PubMed=8238345; DOI=10.1152/ajpgi.1993.265.4.g611;
RA Iovanna J.L., Keim V., Bosshard A., Orelle B., Frigerio J.-M., Dusetti N.,
RA Dagorn J.-C.;
RT "PAP, a pancreatic secretory protein induced during acute pancreatitis, is
RT expressed in rat intestine.";
RL Am. J. Physiol. 265:G611-G618(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8314803; DOI=10.1016/s0021-9258(19)85262-6;
RA Dusetti N.J., Frigerio J.-M., Keim V., Dagorn J.-C., Iovanna J.;
RT "Structural organization of the gene encoding the rat pancreatitis-
RT associated protein. Analysis of its evolutionary history reveals an ancient
RT divergence from the other carbohydrate-recognition domain-containing
RT genes.";
RL J. Biol. Chem. 268:14470-14475(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1511905; DOI=10.1016/0378-1119(92)90206-5;
RA Kamimura T., West C., Beutler E.;
RT "Sequence of a cDNA clone encoding a rat Reg-2 protein.";
RL Gene 118:299-300(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RX PubMed=7895644; DOI=10.1210/endo.136.4.7895644;
RA Katsumata N., Chakraborty C., Myal Y., Schroedter I.C., Murphy L.J.,
RA Shiu R.P., Friesen H.G.;
RT "Molecular cloning and expression of peptide 23, a growth hormone-releasing
RT hormone-inducible pituitary protein.";
RL Endocrinology 136:1332-1339(1995).
CC -!- FUNCTION: Bactericidal C-type lectin which acts against several
CC intestinal Gram-positive bacteria 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Found in the apical region of
CC pancreatic acinar cells.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in intestine.
CC -!- INDUCTION: Appears in pancreatic juice after induction of pancreatic
CC inflammation. Secreted also by pituitary cells; the secretion there is
CC stimulated by GH-releasing hormone and inhibited by somatostatin.
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:0000250}.
CC -!- DISEASE: Note=Overexpressed during the acute phase of pancreatitis.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41805.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M55149; AAA41807.1; -; mRNA.
DR EMBL; M98049; AAA16341.1; -; mRNA.
DR EMBL; L07127; AAA41805.1; ALT_INIT; Genomic_DNA.
DR EMBL; S43715; AAB23103.1; -; mRNA.
DR EMBL; S77413; AAB33848.2; -; mRNA.
DR PIR; A37456; A41719.
DR RefSeq; NP_445741.1; NM_053289.1.
DR AlphaFoldDB; P25031; -.
DR SMR; P25031; -.
DR STRING; 10116.ENSRNOP00000008212; -.
DR MEROPS; I63.002; -.
DR PaxDb; P25031; -.
DR GeneID; 24618; -.
DR KEGG; rno:24618; -.
DR UCSC; RGD:3254; rat.
DR CTD; 18489; -.
DR RGD; 3254; Reg3b.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_049894_18_0_1; -.
DR InParanoid; P25031; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; P25031; -.
DR PRO; PR:P25031; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P25031; RN.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042588; C:zymogen granule; IDA:RGD.
DR GO; GO:0019838; F:growth factor binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0070492; F:oligosaccharide binding; IBA:GO_Central.
DR GO; GO:0042834; F:peptidoglycan binding; IBA:GO_Central.
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:1903577; P:cellular response to L-arginine; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0007494; P:midgut development; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEP:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IDA:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
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; Direct protein sequencing; Disulfide bond;
KW Inflammatory response; Lectin; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:1722211"
FT CHAIN 27..175
FT /note="Regenerating islet-derived protein 3-beta 16.5 kDa
FT form"
FT /id="PRO_0000017433"
FT PROPEP 27..37
FT /evidence="ECO:0000250"
FT /id="PRO_0000422749"
FT CHAIN 38..175
FT /note="Regenerating islet-derived protein 3-beta 15 kDa
FT form"
FT /id="PRO_0000422750"
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"
FT CONFLICT 7
FT /note="F -> S (in Ref. 4; AAB23103)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="S -> T (in Ref. 5; AAB33848)"
FT /evidence="ECO:0000305"
SQ 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
