REG3A_MOUSE
ID REG3A_MOUSE Reviewed; 175 AA.
AC O09037;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Regenerating islet-derived protein 3-alpha;
DE Short=REG-3-alpha;
DE AltName: Full=Islet of Langerhans regenerating protein 3;
DE AltName: Full=Lithostathine 3;
DE AltName: Full=Pancreatitis-associated protein 2;
DE AltName: Full=Regenerating islet-derived protein III-alpha;
DE Short=Reg III-alpha;
DE Contains:
DE RecName: Full=Regenerating islet-derived protein 3-alpha 16.5 kDa form;
DE Contains:
DE RecName: Full=Regenerating islet-derived protein 3-alpha 15 kDa form;
DE Flags: Precursor;
GN Name=Reg3a; Synonyms=Pap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Pancreas;
RX PubMed=9055810; DOI=10.1016/s0378-1119(96)00589-6;
RA Narushima Y., Unno M., Nakagawara K., Mori M., Miyashita H., Suzuki Y.,
RA Noguchi N., Takasawa S., Kumagai T., Yonekura H., Okamoto H.;
RT "Structure, chromosomal localization and expression of mouse genes encoding
RT type III Reg, RegIII alpha, RegIII beta, RegIII gamma.";
RL Gene 185:159-168(1997).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP ABSENCE OF PEPTIDOGLYCAN BINDING.
RX PubMed=20382864; DOI=10.1073/pnas.0909449107;
RA Lehotzky R.E., Partch C.L., Mukherjee S., Cash H.L., Goldman W.E.,
RA Gardner K.H., Hooper L.V.;
RT "Molecular basis for peptidoglycan recognition by a bactericidal lectin.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7722-7727(2010).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=22727489; DOI=10.1016/j.immuni.2012.04.010;
RA Lai Y., Li D., Li C., Muehleisen B., Radek K.A., Park H.J., Jiang Z.,
RA Li Z., Lei H., Quan Y., Zhang T., Wu Y., Kotol P., Morizane S., Hata T.R.,
RA Iwatsuki K., Tang C., Gallo R.L.;
RT "The antimicrobial protein REG3A regulates keratinocyte proliferation and
RT differentiation after skin injury.";
RL Immunity 37:74-84(2012).
CC -!- FUNCTION: Bactericidal C-type lectin (By similarity). Regulates
CC keratinocyte proliferation and differentiation after skin injury via
CC activation of EXTL3-PI3K-AKT signaling pathway. {ECO:0000250,
CC ECO:0000269|PubMed:22727489}.
CC -!- SUBUNIT: Interacts with EXTL3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Small intestine and pancreas.
CC -!- INDUCTION: IL17A induces its expression in primary keratinocytes and
CC skin wounds. {ECO:0000269|PubMed:22727489}.
CC -!- DOMAIN: Lacks the EPN motif and the presence of Gln instead of Glu at
CC amino-acid position 114 may explain its inability to bind
CC peptidoglycan.
CC -!- PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal
CC propeptide and is essential for its antimicrobial activity.
CC {ECO:0000250}.
CC -!- DISEASE: Note=Overexpressed during the acute phase of pancreatitis.
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DR EMBL; D63356; BAA18925.1; -; mRNA.
DR EMBL; D63357; BAA18926.1; -; mRNA.
DR EMBL; D63358; BAA18927.1; -; Genomic_DNA.
DR CCDS; CCDS20255.1; -.
DR RefSeq; NP_035389.1; NM_011259.1.
DR AlphaFoldDB; O09037; -.
DR SMR; O09037; -.
DR STRING; 10090.ENSMUSP00000098829; -.
DR PaxDb; O09037; -.
DR PeptideAtlas; O09037; -.
DR PRIDE; O09037; -.
DR ProteomicsDB; 255177; -.
DR DNASU; 19694; -.
DR Ensembl; ENSMUST00000101272; ENSMUSP00000098829; ENSMUSG00000079516.
DR GeneID; 19694; -.
DR KEGG; mmu:19694; -.
DR UCSC; uc009cjy.1; mouse.
DR CTD; 5068; -.
DR MGI; MGI:109408; Reg3a.
DR VEuPathDB; HostDB:ENSMUSG00000079516; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154447; -.
DR HOGENOM; CLU_049894_18_0_1; -.
DR InParanoid; O09037; -.
DR OMA; LPFVCKF; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; O09037; -.
DR BioGRID-ORCS; 19694; 2 hits in 72 CRISPR screens.
DR PRO; PR:O09037; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O09037; protein.
DR Bgee; ENSMUSG00000079516; Expressed in small intestine Peyer's patch and 17 other tissues.
DR ExpressionAtlas; O09037; baseline and differential.
DR Genevisible; O09037; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070492; F:oligosaccharide binding; ISO:MGI.
DR GO; GO:0042834; F:peptidoglycan binding; ISO:MGI.
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:0045617; P:negative regulation of keratinocyte differentiation; IDA: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; IDA:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; IDA:UniProtKB.
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; 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; Disulfide bond; Inflammatory response; Lectin;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..175
FT /note="Regenerating islet-derived protein 3-alpha 16.5 kDa
FT form"
FT /id="PRO_0000017430"
FT PROPEP 27..37
FT /evidence="ECO:0000250"
FT /id="PRO_0000422743"
FT CHAIN 38..175
FT /note="Regenerating islet-derived protein 3-alpha 15 kDa
FT form"
FT /id="PRO_0000422744"
FT DOMAIN 47..172
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
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"
SQ SEQUENCE 175 AA; 19539 MW; 3E311B3976E80F11 CRC64;
MLPHLVLNSI SWMLLSCLLF VFQVQGEDFQ KEVPSPRTSC PMGYKAYRSH CYALVMTPKS
WFQADLVCQK RPSGHLVSIL SGGEASFVSS LVNGRVDNYQ DIWIGLHDPT MGQQPNGGGW
EWSNSDVLNY LNWDGDPSST VNRGHCGSLT ASSGFLKWGD YYCDGTLPFV CKFKQ
