LITH_RAT
ID LITH_RAT Reviewed; 165 AA.
AC P10758;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Lithostathine;
DE AltName: Full=Islet cells regeneration factor;
DE Short=ICRF;
DE AltName: Full=Islet of Langerhans regenerating protein;
DE Short=REG;
DE AltName: Full=Pancreatic stone protein;
DE Short=PSP;
DE AltName: Full=Pancreatic thread protein;
DE Short=PTP;
DE Flags: Precursor;
GN Name=Reg1; Synonyms=Reg;
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].
RX PubMed=1985964; DOI=10.1016/s0021-9258(17)35241-9;
RA Rouquier S., Verdier J.-M., Iovanna J., Dagorn J.-C., Giorgi D.;
RT "Rat pancreatic stone protein messenger RNA. Abundant expression in mature
RT exocrine cells, regulation by food content, and sequence identity with the
RT endocrine reg transcript.";
RL J. Biol. Chem. 266:786-791(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2963000; DOI=10.1016/s0021-9258(18)69176-8;
RA Terazono K., Yamamoto H., Takasawa S., Shiga K., Yonemura Y., Tochino Y.,
RA Okamoto H.;
RT "A novel gene activated in regenerating islets.";
RL J. Biol. Chem. 263:2111-2114(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7916640; DOI=10.1016/0167-4781(93)90100-r;
RA Dusetti N.J., Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Rapid PCR cloning and sequence determination of the rat lithostathine
RT gene.";
RL Biochim. Biophys. Acta 1174:99-102(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wistar;
RA Miyashita H., Suzuki Y., Watanabe T., Unno M., Moriizumi S., Yonekura H.,
RA Okamoto H.;
RT "Structure and characterization of rat Reg I gene.";
RL Seikagaku 65:1082-1082(1993).
RN [5]
RP PROTEIN SEQUENCE OF 22-69.
RC TISSUE=Pancreas;
RX PubMed=2680252; DOI=10.1016/0305-0491(89)90047-3;
RA Adrich Z., de Caro A.M., Guidoni A.A., Woudstra M.E., Rovery M.;
RT "Characterization in rat pancreatic juice of a protein homologous to the
RT human pancreatic stone protein.";
RL Comp. Biochem. Physiol. 93B:793-797(1989).
CC -!- FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate
CC precipitation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed only in regenerating islets, but not in
CC normal pancreatic islets, insulinomas or regenerating liver.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L07512; AAA41533.1; -; Genomic_DNA.
DR EMBL; M62930; AAA41974.1; -; mRNA.
DR EMBL; M18962; AAA42028.1; -; mRNA.
DR EMBL; D26164; BAA05149.1; -; Genomic_DNA.
DR PIR; A28351; A28351.
DR RefSeq; NP_036773.1; NM_012641.1.
DR AlphaFoldDB; P10758; -.
DR SMR; P10758; -.
DR STRING; 10116.ENSRNOP00000054678; -.
DR MEROPS; I63.002; -.
DR GlyGen; P10758; 1 site.
DR PaxDb; P10758; -.
DR Ensembl; ENSRNOT00000057869; ENSRNOP00000054678; ENSRNOG00000006486.
DR GeneID; 24714; -.
DR KEGG; rno:24714; -.
DR UCSC; RGD:3552; rat.
DR CTD; 5967; -.
DR RGD; 3552; Reg1.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162393; -.
DR HOGENOM; CLU_049894_18_0_1; -.
DR InParanoid; P10758; -.
DR OMA; YDLFWIG; -.
DR OrthoDB; 1509611at2759; -.
DR PhylomeDB; P10758; -.
DR PRO; PR:P10758; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000006486; Expressed in pancreas and 10 other tissues.
DR Genevisible; P10758; RN.
DR GO; GO:0045178; C:basal part of cell; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042588; C:zymogen granule; IDA:RGD.
DR GO; GO:0008083; F:growth factor activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0070492; F:oligosaccharide binding; IBA:GO_Central.
DR GO; GO:0042834; F:peptidoglycan binding; IBA:GO_Central.
DR GO; GO:0019902; F:phosphatase binding; IPI:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0055074; P:calcium ion homeostasis; IDA:RGD.
DR GO; GO:0044278; P:cell wall disruption in another organism; IBA:GO_Central.
DR GO; GO:1990869; P:cellular response to chemokine; IEP:RGD.
DR GO; GO:1990878; P:cellular response to gastrin; IEP:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0007494; P:midgut development; IEP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:1990798; P:pancreas regeneration; IEP:RGD.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:1904699; P:positive regulation of acinar cell proliferation; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; IMP:RGD.
DR GO; GO:1903492; P:response to acetylsalicylate; IEP:RGD.
DR GO; GO:1990867; P:response to gastrin; IEP:RGD.
DR GO; GO:1990864; P:response to growth hormone-releasing hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
DR GO; GO:1990785; P:response to water-immersion restraint stress; IEP:RGD.
DR GO; GO:0003309; P:type B pancreatic cell differentiation; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2680252"
FT CHAIN 22..165
FT /note="Lithostathine"
FT /id="PRO_0000017428"
FT DOMAIN 33..163
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P05451"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 63..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 136..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 165 AA; 18672 MW; 9B61EB236B82CF8A CRC64;
MTRNKYFILL SCLMVLSPSQ GQEAEEDLPS ARITCPEGSN AYSSYCYYFM EDHLSWAEAD
LFCQNMNSGY LVSVLSQAEG NFLASLIKES GTTAANVWIG LHDPKNNRRW HWSSGSLFLY
KSWDTGYPNN SNRGYCVSVT SNSGYKKWRD NSCDAQLSFV CKFKA
