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Regenerating islet-derived protein 3-alpha (REG-3-alpha) (Hepatointestinal pancreatic protein) (HIP/PAP) (Human proislet peptide) (Pancreatitis-associated protein 1) (Regenerating islet-derived protein III-alpha) (Reg III-alpha) [Cleaved into: Regenerating islet-derived protein 3-alpha 16.5 kDa form; Regenerating islet-derived protein 3-alpha 15 kDa form]

 REG3A_HUMAN             Reviewed;         175 AA.
Q06141;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
22-NOV-2017, entry version 156.
RecName: Full=Regenerating islet-derived protein 3-alpha;
Short=REG-3-alpha;
AltName: Full=Hepatointestinal pancreatic protein;
Short=HIP/PAP;
AltName: Full=Human proislet peptide;
AltName: Full=Pancreatitis-associated protein 1;
AltName: Full=Regenerating islet-derived protein III-alpha;
Short=Reg III-alpha;
Contains:
RecName: Full=Regenerating islet-derived protein 3-alpha 16.5 kDa form;
Contains:
RecName: Full=Regenerating islet-derived protein 3-alpha 15 kDa form;
Flags: Precursor;
Name=REG3A; Synonyms=HIP, PAP, PAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas, and Small intestine;
PubMed=7679928; DOI=10.1016/0167-4781(93)90290-T;
Itoh T., Teraoka H.;
"Cloning and tissue-specific expression of cDNAs for the human and
mouse homologues of rat pancreatitis-associated protein (PAP).";
Biochim. Biophys. Acta 1172:184-186(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Pancreas;
PubMed=1469087; DOI=10.1172/JCI116115;
Orelle B., Keim V., Masciotra L., Dagorn J.-C., Iovanna J.-L.;
"Human pancreatitis-associated protein. Messenger RNA cloning and
expression in pancreatic diseases.";
J. Clin. Invest. 90:2284-2291(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1325291;
Lasserre C., Christa L., Simon M.T., Vernier P., Brechot C.;
"A novel gene (HIP) activated in human primary liver cancer.";
Cancer Res. 52:5089-5095(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
PubMed=8188210; DOI=10.1006/geno.1994.1019;
Dusetti N.J., Frigerio J.-M., Fox M.F., Swallow D.M., Dagorn J.-C.,
Iovanna J.L.;
"Molecular cloning, genomic organization, and chromosomal localization
of the human pancreatitis-associated protein (PAP) gene.";
Genomics 19:108-114(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8076648; DOI=10.1111/j.1432-1033.1994.tb19991.x;
Lasserre C., Simon M.T., Ishikawa H., Diriong S., Nguyen V.C.,
Christa L., Vernier P., Brechot C.;
"Structural organization and chromosomal localization of a human gene
(HIP/PAP) encoding a C-type lectin overexpressed in primary liver
cancer.";
Eur. J. Biochem. 224:29-38(1994).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF N-TERMINUS, AND PROTEOLYTIC PROCESSING.
PubMed=19254208; DOI=10.1042/BJ20090005;
Medveczky P., Szmola R., Sahin-Toth M.;
"Proteolytic activation of human pancreatitis-associated protein is
required for peptidoglycan binding and bacterial aggregation.";
Biochem. J. 420:335-343(2009).
[8]
FUNCTION, AND MANNAN- AND PEPTIDOGLYCAN-BINDING.
PubMed=16931762; DOI=10.1126/science.1127119;
Cash H.L., Whitham C.V., Behrendt C.L., Hooper L.V.;
"Symbiotic bacteria direct expression of an intestinal bactericidal
lectin.";
Science 313:1126-1130(2006).
[9]
TISSUE SPECIFICITY, AND INTERACTION WITH EXTL3.
PubMed=22727489; DOI=10.1016/j.immuni.2012.04.010;
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.;
"The antimicrobial protein REG3A regulates keratinocyte proliferation
and differentiation after skin injury.";
Immunity 37:74-84(2012).
[10]
STRUCTURE BY NMR, MOTIF EPN, AND MUTAGENESIS OF GLU-114 AND GLU-118.
PubMed=20382864; DOI=10.1073/pnas.0909449107;
Lehotzky R.E., Partch C.L., Mukherjee S., Cash H.L., Goldman W.E.,
Gardner K.H., Hooper L.V.;
"Molecular basis for peptidoglycan recognition by a bactericidal
lectin.";
Proc. Natl. Acad. Sci. U.S.A. 107:7722-7727(2010).
-!- FUNCTION: Bactericidal C-type lectin which acts exclusively
against Gram-positive bacteria and mediates bacterial killing by
binding to surface-exposed carbohydrate moieties of peptidoglycan.
Regulates keratinocyte proliferation and differentiation after
skin injury via activation of EXTL3-PI3K-AKT signaling pathway.
{ECO:0000269|PubMed:16931762}.
-!- SUBUNIT: Interacts with EXTL3. {ECO:0000269|PubMed:22727489}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-10223932, EBI-10223932;
Q99750:MDFI; NbExp=3; IntAct=EBI-10223932, EBI-724076;
-!- SUBCELLULAR LOCATION: Secreted. Note=Found in the apical region of
pancreatic acinar cells.
-!- TISSUE SPECIFICITY: Highly expressed in epidermal keratinocytes of
psoriasis patients (at protein level). Constitutively expressed in
intestine. Low expression is found in healthy pancreas.
Overexpressed during the acute phase of pancreatitis and in some
patients with chronic pancreatitis. {ECO:0000269|PubMed:1469087,
ECO:0000269|PubMed:22727489}.
-!- INDUCTION: Appears in pancreatic juice after induction of
pancreatic inflammation.
-!- DOMAIN: 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.
-!- PTM: Proteolytic processing by trypsin removes an inhibitory N-
terminal propeptide and is essential for peptidoglycan binding and
antibacterial activity. {ECO:0000269|PubMed:19254208}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Pancreatitis-associated protein 1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_256";
-----------------------------------------------------------------------
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EMBL; D13510; BAA02728.1; -; mRNA.
EMBL; M84337; AAA36415.1; -; mRNA.
EMBL; S51768; AAB24642.1; -; mRNA.
EMBL; X68641; CAA48605.1; -; mRNA.
EMBL; L15533; AAA60020.1; -; Genomic_DNA.
EMBL; BC036776; AAH36776.1; -; mRNA.
CCDS; CCDS1965.1; -.
PIR; A49616; A49616.
RefSeq; NP_002571.1; NM_002580.2.
RefSeq; NP_620354.1; NM_138937.2.
RefSeq; NP_620355.1; NM_138938.2.
UniGene; Hs.567312; -.
PDB; 1UV0; X-ray; 1.78 A; A=27-175.
PDB; 2GO0; NMR; -; A=39-175.
PDB; 4MTH; X-ray; 1.47 A; A=38-175.
PDBsum; 1UV0; -.
PDBsum; 2GO0; -.
PDBsum; 4MTH; -.
ProteinModelPortal; Q06141; -.
SMR; Q06141; -.
BioGrid; 111103; 7.
DIP; DIP-60688N; -.
IntAct; Q06141; 1.
STRING; 9606.ENSP00000304311; -.
MEROPS; I63.002; -.
TCDB; 1.C.111.1.2; the regiii (regiii) family.
BioMuta; REG3A; -.
DMDM; 464341; -.
EPD; Q06141; -.
PaxDb; Q06141; -.
PeptideAtlas; Q06141; -.
PRIDE; Q06141; -.
Ensembl; ENST00000305165; ENSP00000304311; ENSG00000172016.
Ensembl; ENST00000393878; ENSP00000377456; ENSG00000172016.
Ensembl; ENST00000409839; ENSP00000386630; ENSG00000172016.
GeneID; 5068; -.
KEGG; hsa:5068; -.
CTD; 5068; -.
DisGeNET; 5068; -.
EuPathDB; HostDB:ENSG00000172016.15; -.
GeneCards; REG3A; -.
HGNC; HGNC:8601; REG3A.
HPA; HPA047894; -.
HPA; HPA048334; -.
HPA; HPA060705; -.
MIM; 167805; gene.
neXtProt; NX_Q06141; -.
OpenTargets; ENSG00000172016; -.
PharmGKB; PA32931; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00700000104249; -.
HOGENOM; HOG000010281; -.
HOVERGEN; HBG004151; -.
InParanoid; Q06141; -.
OMA; VKLPYVC; -.
OrthoDB; EOG091G0MDY; -.
PhylomeDB; Q06141; -.
Reactome; R-HSA-6803157; Antimicrobial peptides.
ChiTaRS; REG3A; human.
EvolutionaryTrace; Q06141; -.
GeneWiki; REG3A; -.
GenomeRNAi; 5068; -.
PMAP-CutDB; Q06141; -.
PRO; PR:Q06141; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000172016; -.
CleanEx; HS_REG3A; -.
ExpressionAtlas; Q06141; baseline and differential.
Genevisible; Q06141; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:ProtInc.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0045617; P:negative regulation of keratinocyte differentiation; ISS:UniProtKB.
GO; GO:0010838; P:positive regulation of keratinocyte proliferation; ISS:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Antimicrobial; Complete proteome;
Direct protein sequencing; Disulfide bond; Inflammatory response;
Lectin; Reference proteome; Secreted; Signal.
SIGNAL 1 26 {ECO:0000250}.
CHAIN 27 175 Regenerating islet-derived protein 3-
alpha 16.5 kDa form.
/FTId=PRO_0000017429.
PROPEP 27 37 {ECO:0000269|PubMed:19254208}.
/FTId=PRO_0000422741.
CHAIN 38 175 Regenerating islet-derived protein 3-
alpha 15 kDa form.
/FTId=PRO_0000422742.
DOMAIN 47 172 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
MOTIF 114 116 EPN.
DISULFID 40 51 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 68 171 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 146 163 {ECO:0000255|PROSITE-ProRule:PRU00040}.
MUTAGEN 114 114 E->Q: Reduces peptidoglycan binding and
antibacterial activity.
{ECO:0000269|PubMed:20382864}.
MUTAGEN 118 118 E->Q: Reduces antibacterial activity but
no effect on peptidoglycan binding.
{ECO:0000269|PubMed:20382864}.
CONFLICT 173 175 FTD -> VH (in Ref. 2; AAA36415).
{ECO:0000305}.
STRAND 44 47 {ECO:0000244|PDB:4MTH}.
STRAND 50 59 {ECO:0000244|PDB:4MTH}.
HELIX 61 68 {ECO:0000244|PDB:4MTH}.
HELIX 82 92 {ECO:0000244|PDB:4MTH}.
STRAND 100 107 {ECO:0000244|PDB:4MTH}.
TURN 109 112 {ECO:0000244|PDB:4MTH}.
STRAND 114 116 {ECO:0000244|PDB:2GO0}.
TURN 123 125 {ECO:0000244|PDB:2GO0}.
STRAND 133 135 {ECO:0000244|PDB:4MTH}.
HELIX 137 139 {ECO:0000244|PDB:4MTH}.
STRAND 140 142 {ECO:0000244|PDB:4MTH}.
STRAND 145 150 {ECO:0000244|PDB:4MTH}.
HELIX 151 153 {ECO:0000244|PDB:4MTH}.
STRAND 157 161 {ECO:0000244|PDB:4MTH}.
STRAND 167 173 {ECO:0000244|PDB:4MTH}.
SEQUENCE 175 AA; 19395 MW; C51149FAC22EB68C CRC64;
MLPPMALPSV SWMLLSCLML LSQVQGEEPQ RELPSARIRC PKGSKAYGSH CYALFLSPKS
WTDADLACQK RPSGNLVSVL SGAEGSFVSS LVKSIGNSYS YVWIGLHDPT QGTEPNGEGW
EWSSSDVMNY FAWERNPSTI SSPGHCASLS RSTAFLRWKD YNCNVRLPYV CKFTD


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