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Protein

Regenerating islet-derived protein 3-gamma

Gene

Reg3g

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune responses by the microbiota. The uncleaved form has bacteriostatic activity, whereas the cleaved form has bactericidal activity against L.monocytogenes and methicillin-resistant S.aureus. Regulates keratinocyte proliferation and differentiation after skin injury.7 Publications

GO - Molecular functioni

GO - Biological processi

  • acute-phase response Source: UniProtKB-KW
  • defense response to Gram-positive bacterium Source: UniProtKB
  • MyD88-dependent toll-like receptor signaling pathway Source: UniProtKB
  • negative regulation of keratinocyte differentiation Source: UniProtKB
  • positive regulation of keratinocyte proliferation Source: UniProtKB
  • positive regulation of wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial

Keywords - Biological processi

Acute phase, Inflammatory response

Keywords - Ligandi

Lectin

Protein family/group databases

MEROPSiI63.002.
TCDBi1.C.111.1.1. the regiii (regiii) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Regenerating islet-derived protein 3-gamma
Short name:
REG-3-gamma
Alternative name(s):
Pancreatitis-associated protein 3
Regenerating islet-derived protein III-gamma
Short name:
Reg III-gamma
Cleaved into the following 2 chains:
Gene namesi
Name:Reg3g
Synonyms:Pap3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:109406. Reg3g.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at normal Mendelian ratios. They appear healthy and show no signs of enteropathy, but exhibit a marked increase in the number of mucosa-associated bacteria, predominantly Gram-positive, relative to cohoused wild-type littermates in distal small intestine.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 174148Regenerating islet-derived protein 3-gamma 16.5 kDa formPRO_0000017435Add
BLAST
Propeptidei27 – 37111 PublicationPRO_0000422753Add
BLAST
Chaini38 – 174137Regenerating islet-derived protein 3-gamma 15 kDa formPRO_0000422754Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 51PROSITE-ProRule annotation
Disulfide bondi68 ↔ 170PROSITE-ProRule annotation
Disulfide bondi145 ↔ 162PROSITE-ProRule annotation

Post-translational modificationi

Proteolytic processing by trypsin removes an inhibitory N-terminal propeptide and is essential for peptidoglycan binding and antibacterial activity.1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO09049.
PRIDEiO09049.

Expressioni

Tissue specificityi

Predominantly expressed in the small intestine, including Paneth cells (at protein level). Hardly detectable in the colon (at protein level). Highly expressed in the lung epithelium during methicillin-resistant S.aureus infection (at protein level). Skin injury increases its epidermal expression. Also expressed in the pancreas.7 Publications

Developmental stagei

In mid-small intestine, very low levels at birth. Expression levels rise dramatically during the weaning period (P17-P22) and remain high into adulthood in conventionally raised but not germfree animals.1 Publication

Inductioni

Up-regulated in Paneth cells by intestinal microbiota (at protein level). MyD88-mediated signals are essential for its induction in intestinal epithelial cells. Induction in the lung is dependent on IL6ST-induced STAT3 signaling. IL17A induces its expression in primary keratinocytes and skin wounds.4 Publications

Gene expression databases

BgeeiO09049.
CleanExiMM_REG3G.
ExpressionAtlasiO09049. baseline and differential.
GenevisibleiO09049. MM.

Interactioni

Protein-protein interaction databases

IntActiO09049. 2 interactions.
MINTiMINT-4106557.
STRINGi10090.ENSMUSP00000032089.

Structurei

3D structure databases

ProteinModelPortaliO09049.
SMRiO09049. Positions 40-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 171125C-type lectinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi114 – 1163EPNBy similarity

Domaini

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.By similarity

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JQFS. Eukaryota.
ENOG4111DBG. LUCA.
HOGENOMiHOG000010281.
HOVERGENiHBG004151.
InParanoidiO09049.
OMAiWEWSNAD.
OrthoDBiEOG738067.
PhylomeDBiO09049.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O09049-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPRITITIM SWMLLSCLML LSQVQGEVAK KDAPSSRSSC PKGSRAYGSY
60 70 80 90 100
CYALFSVSKN WYDADMACQK RPSGHLVSVL SGAEASFLSS MIKSSGNSGQ
110 120 130 140 150
YVWIGLHDPT LGYEPNRGGW EWSNADVMNY INWETNPSSS SGNHCGTLSR
160 170
ASGFLKWREN YCNLELPYVC KFKA
Length:174
Mass (Da):19,307
Last modified:July 1, 1997 - v1
Checksum:i5575E9E56A4D8CEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63361 mRNA. Translation: BAA18930.1.
D63362 Genomic DNA. Translation: BAA18931.1.
BC061139 mRNA. Translation: AAH61139.1.
CCDSiCCDS20258.1.
RefSeqiNP_035390.1. NM_011260.1.
UniGeneiMm.252385.

Genome annotation databases

EnsembliENSMUST00000032089; ENSMUSP00000032089; ENSMUSG00000030017.
GeneIDi19695.
KEGGimmu:19695.
UCSCiuc009ckb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63361 mRNA. Translation: BAA18930.1.
D63362 Genomic DNA. Translation: BAA18931.1.
BC061139 mRNA. Translation: AAH61139.1.
CCDSiCCDS20258.1.
RefSeqiNP_035390.1. NM_011260.1.
UniGeneiMm.252385.

3D structure databases

ProteinModelPortaliO09049.
SMRiO09049. Positions 40-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO09049. 2 interactions.
MINTiMINT-4106557.
STRINGi10090.ENSMUSP00000032089.

Protein family/group databases

MEROPSiI63.002.
TCDBi1.C.111.1.1. the regiii (regiii) family.

Proteomic databases

PaxDbiO09049.
PRIDEiO09049.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032089; ENSMUSP00000032089; ENSMUSG00000030017.
GeneIDi19695.
KEGGimmu:19695.
UCSCiuc009ckb.1. mouse.

Organism-specific databases

CTDi130120.
MGIiMGI:109406. Reg3g.

Phylogenomic databases

eggNOGiENOG410JQFS. Eukaryota.
ENOG4111DBG. LUCA.
HOGENOMiHOG000010281.
HOVERGENiHBG004151.
InParanoidiO09049.
OMAiWEWSNAD.
OrthoDBiEOG738067.
PhylomeDBiO09049.

Miscellaneous databases

ChiTaRSiReg3g. mouse.
NextBioi297040.
PROiO09049.
SOURCEiSearch...

Gene expression databases

BgeeiO09049.
CleanExiMM_REG3G.
ExpressionAtlasiO09049. baseline and differential.
GenevisibleiO09049. MM.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure, chromosomal localization and expression of mouse genes encoding type III Reg, RegIII alpha, RegIII beta, RegIII gamma."
    Narushima Y., Unno M., Nakagawara K., Mori M., Miyashita H., Suzuki Y., Noguchi N., Takasawa S., Kumagai T., Yonekura H., Okamoto H.
    Gene 185:159-168(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Liver and Pancreas.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart and Lung.
  3. "Regulation of C-type lectin antimicrobial activity by a flexible N-terminal prosegment."
    Mukherjee S., Partch C.L., Lehotzky R.E., Whitham C.V., Chu H., Bevins C.L., Gardner K.H., Hooper L.V.
    J. Biol. Chem. 284:4881-4888(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, PROTEOLYTIC PROCESSING.
  4. "Refolding, purification, and characterization of human and murine RegIII proteins expressed in Escherichia coli."
    Cash H.L., Whitham C.V., Hooper L.V.
    Protein Expr. Purif. 48:151-159(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  5. "Symbiotic bacteria direct expression of an intestinal bactericidal lectin."
    Cash H.L., Whitham C.V., Behrendt C.L., Hooper L.V.
    Science 313:1126-1130(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MANNAN- AND PEPTIDOGLYCAN-BINDING, TISSUE SPECIFICITY, INDUCTION, DEVELOPMENTAL STAGE.
  6. "MyD88-mediated signals induce the bactericidal lectin RegIII gamma and protect mice against intestinal Listeria monocytogenes infection."
    Brandl K., Plitas G., Schnabl B., DeMatteo R.P., Pamer E.G.
    J. Exp. Med. 204:1891-1900(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung, Pancreas and Testis.
  8. "The antibacterial lectin RegIIIgamma promotes the spatial segregation of microbiota and host in the intestine."
    Vaishnava S., Yamamoto M., Severson K.M., Ruhn K.A., Yu X., Koren O., Ley R., Wakeland E.K., Hooper L.V.
    Science 334:255-258(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  9. "The antimicrobial protein REG3A regulates keratinocyte proliferation and differentiation after skin injury."
    Lai Y., Li D., Li C., Muehleisen B., Radek K.A., Park H.J., Jiang Z., Li Z., Lei H., Quan Y., Zhang T., Wu Y., Kotol P., Morizane S., Hata T.R., Iwatsuki K., Tang C., Gallo R.L.
    Immunity 37:74-84(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  10. "Innate Stat3-mediated induction of the antimicrobial protein Reg3gamma is required for host defense against MRSA pneumonia."
    Choi S.M., McAleer J.P., Zheng M., Pociask D.A., Kaplan M.H., Qin S., Reinhart T.A., Kolls J.K.
    J. Exp. Med. 210:551-561(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiREG3G_MOUSE
AccessioniPrimary (citable) accession number: O09049
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: March 16, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.