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Lithostathine (Islet cells regeneration factor) (ICRF) (Islet of Langerhans regenerating protein) (REG) (Pancreatic stone protein) (PSP) (Pancreatic thread protein) (PTP)

 LITH_RAT                Reviewed;         165 AA.
P10758;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
23-MAY-2018, entry version 125.
RecName: Full=Lithostathine;
AltName: Full=Islet cells regeneration factor;
Short=ICRF;
AltName: Full=Islet of Langerhans regenerating protein;
Short=REG;
AltName: Full=Pancreatic stone protein;
Short=PSP;
AltName: Full=Pancreatic thread protein;
Short=PTP;
Flags: Precursor;
Name=Reg1; Synonyms=Reg;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1985964;
Rouquier S., Verdier J.-M., Iovanna J., Dagorn J.-C., Giorgi D.;
"Rat pancreatic stone protein messenger RNA. Abundant expression in
mature exocrine cells, regulation by food content, and sequence
identity with the endocrine reg transcript.";
J. Biol. Chem. 266:786-791(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2963000;
Terazono K., Yamamoto H., Takasawa S., Shiga K., Yonemura Y.,
Tochino Y., Okamoto H.;
"A novel gene activated in regenerating islets.";
J. Biol. Chem. 263:2111-2114(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7916640; DOI=10.1016/0167-4781(93)90100-R;
Dusetti N.J., Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
"Rapid PCR cloning and sequence determination of the rat lithostathine
gene.";
Biochim. Biophys. Acta 1174:99-102(1993).
[4]
NUCLEOTIDE SEQUENCE.
STRAIN=Wistar;
Miyashita H., Suzuki Y., Watanabe T., Unno M., Moriizumi S.,
Yonekura H., Okamoto H.;
"Structure and characterization of rat Reg I gene.";
Seikagaku 65:1082-1082(1993).
[5]
PROTEIN SEQUENCE OF 22-69.
TISSUE=Pancreas;
PubMed=2680252;
Adrich Z., de Caro A.M., Guidoni A.A., Woudstra M.E., Rovery M.;
"Characterization in rat pancreatic juice of a protein homologous to
the human pancreatic stone protein.";
Comp. Biochem. Physiol. 93B:793-797(1989).
-!- FUNCTION: Might act as an inhibitor of spontaneous calcium
carbonate precipitation.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed only in regenerating islets, but not
in normal pancreatic islets, insulinomas or regenerating liver.
-----------------------------------------------------------------------
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EMBL; L07512; AAA41533.1; -; Genomic_DNA.
EMBL; M62930; AAA41974.1; -; mRNA.
EMBL; M18962; AAA42028.1; -; mRNA.
EMBL; D26164; BAA05149.1; -; Genomic_DNA.
PIR; A28351; A28351.
RefSeq; NP_036773.1; NM_012641.1.
UniGene; Rn.11332; -.
ProteinModelPortal; P10758; -.
SMR; P10758; -.
STRING; 10116.ENSRNOP00000054678; -.
MEROPS; I63.002; -.
PaxDb; P10758; -.
Ensembl; ENSRNOT00000057869; ENSRNOP00000054678; ENSRNOG00000006486.
GeneID; 24714; -.
KEGG; rno:24714; -.
UCSC; RGD:3552; rat.
CTD; 5967; -.
RGD; 3552; Reg1.
eggNOG; ENOG410KDDW; Eukaryota.
eggNOG; ENOG410ZSJ1; LUCA.
GeneTree; ENSGT00700000104249; -.
HOGENOM; HOG000010281; -.
HOVERGEN; HBG004151; -.
InParanoid; P10758; -.
OMA; KSWGIGA; -.
OrthoDB; EOG091G0OLC; -.
PhylomeDB; P10758; -.
PRO; PR:P10758; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000006486; -.
Genevisible; P10758; RN.
GO; GO:0045178; C:basal part of cell; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0032590; C:dendrite membrane; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0042588; C:zymogen granule; IDA:RGD.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0008083; F:growth factor activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0055074; P:calcium ion homeostasis; IDA:RGD.
GO; GO:1990869; P:cellular response to chemokine; IEP:RGD.
GO; GO:1990878; P:cellular response to gastrin; IEP:RGD.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0007494; P:midgut development; IEP:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:RGD.
GO; GO:1990798; P:pancreas regeneration; IEP:RGD.
GO; GO:1904699; P:positive regulation of acinar cell proliferation; IDA:RGD.
GO; GO:1903861; P:positive regulation of dendrite extension; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IDA:RGD.
GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; IMP:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0051289; P:protein homotetramerization; IDA:RGD.
GO; GO:1903492; P:response to acetylsalicylate; IEP:RGD.
GO; GO:1990867; P:response to gastrin; IEP:RGD.
GO; GO:1990864; P:response to growth hormone-releasing hormone; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:1990785; P:response to water-immersion restraint stress; IEP:RGD.
GO; GO:0042060; P:wound healing; IEP:RGD.
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;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Lectin; Pyrrolidone carboxylic acid; Reference proteome;
Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:2680252}.
CHAIN 22 165 Lithostathine.
/FTId=PRO_0000017428.
DOMAIN 33 163 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
MOD_RES 22 22 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P05451}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 46 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 63 161 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 136 153 {ECO:0000255|PROSITE-ProRule:PRU00040}.
SEQUENCE 165 AA; 18672 MW; 9B61EB236B82CF8A CRC64;
MTRNKYFILL SCLMVLSPSQ GQEAEEDLPS ARITCPEGSN AYSSYCYYFM EDHLSWAEAD
LFCQNMNSGY LVSVLSQAEG NFLASLIKES GTTAANVWIG LHDPKNNRRW HWSSGSLFLY
KSWDTGYPNN SNRGYCVSVT SNSGYKKWRD NSCDAQLSFV CKFKA


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