REG3A_RAT
ID REG3A_RAT Reviewed; 174 AA.
AC P35231;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Regenerating islet-derived protein 3-alpha;
DE Short=REG-3-alpha;
DE AltName: Full=Islet of Langerhans regenerating protein 3;
DE Short=REG 3;
DE AltName: Full=Lithostathine 3;
DE AltName: Full=Pancreatitis-associated protein 2;
DE AltName: Full=RegIII;
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, Reg3;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Pancreas;
RX PubMed=8369291; DOI=10.1021/bi00086a032;
RA Frigerio J.-M., Dusetti N.J., Keim V., Dagorn J.-C., Iovanna J.L.;
RT "Identification of a second rat pancreatitis-associated protein. Messenger
RT RNA cloning, gene structure, and expression during acute pancreatitis.";
RL Biochemistry 32:9236-9241(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Wistar;
RX PubMed=8039722; DOI=10.1016/0378-1119(94)90399-9;
RA Suzuki Y., Yonekura H., Watanabe T., Unno M., Moriizumi S., Miyashita H.,
RA Okamoto H.;
RT "Structure and expression of a novel rat RegIII gene.";
RL Gene 144:315-316(1994).
CC -!- FUNCTION: Bactericidal C-type lectin. Regulates keratinocyte
CC proliferation and differentiation after skin injury via activation of
CC EXTL3-PI3K-AKT signaling pathway (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Low expression found in healthy pancreas.
CC -!- INDUCTION: Appears in pancreatic juice after induction of pancreatic
CC inflammation.
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 antibacterial activity.
CC {ECO:0000250}.
CC -!- DISEASE: Note=Overexpressed during the acute phase of pancreatitis.
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DR EMBL; L10230; AAA41808.1; -; Genomic_DNA.
DR EMBL; L10229; AAA02980.1; -; mRNA.
DR EMBL; D26078; BAA05071.1; -; Genomic_DNA.
DR EMBL; D23676; BAA04904.1; -; mRNA.
DR PIR; A48689; A48689.
DR PIR; I60296; I83377.
DR RefSeq; NP_001139318.1; NM_001145846.2.
DR RefSeq; NP_742074.2; NM_172077.2.
DR AlphaFoldDB; P35231; -.
DR SMR; P35231; -.
DR STRING; 10116.ENSRNOP00000008468; -.
DR PaxDb; P35231; -.
DR GeneID; 171162; -.
DR KEGG; rno:171162; -.
DR UCSC; RGD:621401; rat.
DR CTD; 5068; -.
DR RGD; 621401; Reg3a.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P35231; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; P35231; -.
DR PRO; PR:P35231; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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: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: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 2: Evidence at transcript level;
KW Acute phase; Antimicrobial; Disulfide bond; Inflammatory response; Lectin;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..174
FT /note="Regenerating islet-derived protein 3-alpha 16.5 kDa
FT form"
FT /id="PRO_0000017431"
FT PROPEP 26..36
FT /evidence="ECO:0000250"
FT /id="PRO_0000422745"
FT CHAIN 37..174
FT /note="Regenerating islet-derived protein 3-alpha 15 kDa
FT form"
FT /id="PRO_0000422746"
FT DOMAIN 46..171
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 39..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 67..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 145..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 104
FT /note="W -> G (in Ref. 2; BAA05071/BAA04904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 19599 MW; 4530E884496E5888 CRC64;
MLPRLSFNNV SWTLLYYLFI FQVRGEDSQK AVPSTRTSCP MGSKAYRSYC YTLVTTLKSW
FQADLACQKR PSGHLVSILS GGEASFVSSL VTGRVNNNQD IWIWLHDPTM GQQPNGGGWE
WSNSDVLNYL NWDGDPSSTV NRGNCGSLTA TSEFLKWGDH HCDVELPFVC KFKQ
