REG3G_RAT
ID REG3G_RAT Reviewed; 174 AA.
AC P42854;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Regenerating islet-derived protein 3-gamma;
DE Short=REG-3-gamma;
DE AltName: Full=Pancreatitis-associated protein 3;
DE AltName: Full=Regenerating islet-derived protein III-gamma;
DE Short=Reg III-gamma;
DE Contains:
DE RecName: Full=Regenerating islet-derived protein 3-gamma 16.5 kDa form;
DE Contains:
DE RecName: Full=Regenerating islet-derived protein 3-gamma 15 kDa form;
DE Flags: Precursor;
GN Name=Reg3g; Synonyms=Pap3;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Intestine;
RX PubMed=8241280; DOI=10.1016/0167-4781(93)90167-c;
RA Frigerio J.-M., Dusetti N.J., Garrido P., Dagorn J.-C., Iovanna J.L.;
RT "The pancreatitis associated protein III (PAP III), a new member of the PAP
RT gene family.";
RL Biochim. Biophys. Acta 1216:329-331(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=7717998; DOI=10.1042/bj3070009;
RA Dusetti N.J., Frigerio J.-M., Szpirer C., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, expression and chromosomal localization of the rat pancreatitis-
RT associated protein III gene.";
RL Biochem. J. 307:9-16(1995).
RN [3]
RP SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=23588857; DOI=10.1002/mus.23877;
RA Klasan G.S., Ivanac D., Erzen D.J., Picard A., Takasawa S., Peharec S.,
RA Arbanas J., Girotto D., Jerkovic R.;
RT "Reg3G gene expression in regenerating skeletal muscle and corresponding
RT nerve.";
RL Muscle Nerve 49:61-68(2014).
CC -!- FUNCTION: Bactericidal C-type lectin which acts exclusively against
CC Gram-positive bacteria and mediates bacterial killing by binding to
CC surface-exposed carbohydrate moieties of peptidoglycan. Restricts
CC bacterial colonization of the intestinal epithelial surface and
CC consequently limits activation of adaptive immune responses by the
CC microbiota. The uncleaved form has bacteriostatic activity, whereas the
CC cleaved form has bactericidal activity against L.monocytogenes and
CC methicillin-resistant S.aureus. Regulates keratinocyte proliferation
CC and differentiation after skin injury (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23588857}. Cytoplasm
CC {ECO:0000269|PubMed:23588857}.
CC -!- TISSUE SPECIFICITY: Expressed in injured skeletal muscles and sciatic
CC nerve (at protein level). Expressed in the pancreas. Expression
CC increases during the acute phase of pancreatitis.
CC {ECO:0000269|PubMed:23588857, ECO:0000269|PubMed:7717998}.
CC -!- INDUCTION: Up-regulated in injured skeletal muscles and peripheral
CC nerve. {ECO:0000269|PubMed:23588857}.
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}.
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DR EMBL; L20869; AAA41809.1; -; mRNA.
DR EMBL; U09193; AAA79231.1; -; Genomic_DNA.
DR PIR; S54979; S54979.
DR RefSeq; NP_775120.1; NM_173097.1.
DR AlphaFoldDB; P42854; -.
DR SMR; P42854; -.
DR STRING; 10116.ENSRNOP00000008665; -.
DR MEROPS; I63.002; -.
DR PaxDb; P42854; -.
DR Ensembl; ENSRNOT00000008665; ENSRNOP00000008665; ENSRNOG00000006579.
DR GeneID; 24620; -.
DR KEGG; rno:24620; -.
DR UCSC; RGD:3256; rat.
DR CTD; 130120; -.
DR RGD; 3256; Reg3g.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154447; -.
DR HOGENOM; CLU_049894_18_0_1; -.
DR InParanoid; P42854; -.
DR OMA; WEWSNAD; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; P42854; -.
DR Reactome; R-RNO-6803157; Antimicrobial peptides.
DR PRO; PR:P42854; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000006579; Expressed in jejunum and 13 other tissues.
DR Genevisible; P42854; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0070492; F:oligosaccharide binding; ISO:RGD.
DR GO; GO:0042834; F:peptidoglycan binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0044278; P:cell wall disruption in another organism; ISO:RGD.
DR GO; GO:0051838; P:cytolysis by host of symbiont cells; ISO:RGD.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045617; P:negative regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
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; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Acute phase; Antimicrobial; Cytoplasm; Disulfide bond;
KW Inflammatory response; Lectin; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..174
FT /note="Regenerating islet-derived protein 3-gamma 16.5 kDa
FT form"
FT /id="PRO_0000017436"
FT PROPEP 27..37
FT /evidence="ECO:0000250"
FT /id="PRO_0000422755"
FT CHAIN 38..174
FT /note="Regenerating islet-derived protein 3-gamma 15 kDa
FT form"
FT /id="PRO_0000422756"
FT DOMAIN 47..171
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..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 145..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 174 AA; 19144 MW; 5CED2E887C46E45C CRC64;
MLPRVALTTM SWMLLSSLML LSQVQGEDAK EDVPTSRISC PKGSRAYGSY CYALFSVSKS
WFDADLACQK RPSGHLVSVL SGSEASFVSS LIKSSGNSGQ NVWIGLHDPT LGQEPNRGGW
EWSNADVMNY FNWETNPSSV SGSHCGTLTR ASGFLRWREN NCISELPYVC KFKA
