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Lithostathine-1-alpha (Islet cells regeneration factor) (ICRF) (Islet of Langerhans regenerating protein) (REG) (Pancreatic stone protein) (PSP) (Pancreatic thread protein) (PTP) (Regenerating islet-derived protein 1-alpha) (REG-1-alpha) (Regenerating protein I alpha)

 REG1A_HUMAN             Reviewed;         166 AA.
P05451; P11379; Q4ZG28;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 3.
12-SEP-2018, entry version 191.
RecName: Full=Lithostathine-1-alpha;
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;
AltName: Full=Regenerating islet-derived protein 1-alpha;
Short=REG-1-alpha;
AltName: Full=Regenerating protein I alpha;
Flags: Precursor;
Name=REG1A; Synonyms=PSPS, PSPS1, REG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2332435;
Watanabe T., Yonekura H., Terazono K., Yamamoto H., Okamoto H.;
"Complete nucleotide sequence of human reg gene and its expression in
normal and tumoral tissues. The reg protein, pancreatic stone protein,
and pancreatic thread protein are one and the same product of the
gene.";
J. Biol. Chem. 265:7432-7439(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Pancreas;
PubMed=2525567; DOI=10.1172/JCI114128;
Giorgi D., Bernard J.-P., Rouquier S., Iovanna J., Sarles H.,
Dagorn J.-C.;
"Secretory pancreatic stone protein messenger RNA. Nucleotide sequence
and expression in chronic calcifying pancreatitis.";
J. Clin. Invest. 84:100-106(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Boonyasrisawat W., Tandhanand-Banchuin N., Vannasaeng S.,
Yenchitsomanus P.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
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).
[8]
PROTEIN SEQUENCE OF 34-166.
PubMed=3665916; DOI=10.1111/j.1432-1033.1987.tb13405.x;
de Caro A.M., Bonicel J.J., Rouimi P., de Caro J.D., Sarles H.,
Rovery M.;
"Complete amino acid sequence of an immunoreactive form of human
pancreatic stone protein isolated from pancreatic juice.";
Eur. J. Biochem. 168:201-207(1987).
[9]
PROTEIN SEQUENCE OF 34-98.
PubMed=3541906; DOI=10.1042/bj2380227;
Montalto G., Bonicel J.J., Multigner L., Rovery M., Sarles H.,
de Caro A.M.;
"Partial amino acid sequence of human pancreatic stone protein, a
novel pancreatic secretory protein.";
Biochem. J. 238:227-232(1986).
[10]
PROTEIN SEQUENCE OF 34-78.
PubMed=3908481; DOI=10.1172/JCI112216;
Gross J., Carlson R.I., Brauer A.W., Margolies M.N., Warshaw A.L.,
Wands J.R.;
"Isolation, characterization, and distribution of an unusual
pancreatic human secretory protein.";
J. Clin. Invest. 76:2115-2125(1985).
[11]
PROTEIN SEQUENCE OF 23-47, PYROGLUTAMATE FORMATION AT GLN-23, AND
GLYCOSYLATION AT THR-27.
PubMed=2493268; DOI=10.1016/0167-4838(89)90305-1;
de Caro A.M., Adrich Z., Fournet B., Capon C., Bonicel J.J.,
de Caro J.D., Rovery M.;
"N-terminal sequence extension in the glycosylated forms of human
pancreatic stone protein. The 5-oxoproline N-terminal chain is O-
glycosylated on the 5th amino acid residue.";
Biochim. Biophys. Acta 994:281-284(1989).
[12]
PROTEIN SEQUENCE OF 33-58.
PubMed=3108036; DOI=10.1016/0014-5793(87)80688-9;
Rouimi P., Bonicel J., Rovery M., de Caro A.;
"Cleavage of the Arg-Ile bond in the native polypeptide chain of human
pancreatic stone protein.";
FEBS Lett. 216:195-199(1987).
[13]
PROTEIN SEQUENCE OF 23-37.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[14]
IDENTITY OF REG WITH PSP.
PubMed=2764894; DOI=10.1042/bj2600622;
Stewart T.A.;
"The human reg gene encodes pancreatic stone protein.";
Biochem. J. 260:622-623(1989).
[15]
DISULFIDE BONDS.
PubMed=2226837; DOI=10.1016/0014-5793(90)80454-Q;
Itoh T., Tsuzuki H., Katoh T., Teraoka H., Matsumoto K., Yoshida N.,
Terazono K., Watanabe T., Yonekura H., Yamamoto H., Okamoto H.;
"Isolation and characterization of human reg protein produced in
Saccharomyces cerevisiae.";
FEBS Lett. 272:85-88(1990).
[16]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=2394826; DOI=10.1172/JCI114762;
de la Monte S.M., Ozturk M., Wands J.R.;
"Enhanced expression of an exocrine pancreatic protein in Alzheimer's
disease and the developing human brain.";
J. Clin. Invest. 86:1004-1013(1990).
[17]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed=8654365;
Bertrand J.A., Pignol D., Bernard J.-P., Verdier J.-M., Dagorn J.-C.,
Fontecilla-Camps J.-C.;
"Crystal structure of human lithostathine, the pancreatic inhibitor of
stone formation.";
EMBO J. 15:2678-2684(1996).
[18]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 23-166.
PubMed=10625646; DOI=10.1074/jbc.275.2.1057;
Gerbaud V., Pignol D., Loret E., Bertrand J.A., Berland Y.,
Fontecilla-Camps J.-C., Canselier J.P., Gabas N., Verdier J.-M.;
"Mechanism of calcite crystal growth inhibition by the N-terminal
undecapeptide of lithostathine.";
J. Biol. Chem. 275:1057-1064(2000).
[19]
STRUCTURE BY NMR OF 34-164.
PubMed=8961348; DOI=10.1093/protein/9.11.949;
Patard L., Stoven V., Gharib B., Bontems F., Lallemand J.-Y.,
de Reggi M.;
"What function for human lithostathine?: structural investigations by
three-dimensional structure modeling and high-resolution NMR
spectroscopy.";
Protein Eng. 9:949-957(1996).
-!- FUNCTION: Might act as an inhibitor of spontaneous calcium
carbonate precipitation. May be associated with neuronal sprouting
in brain, and with brain and pancreas regeneration.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: In pancreatic acinar cells and, in lower
levels, in brain. Enhanced expression of PSP-related transcripts
and intraneuronal accumulation of PSP-like proteins is found in
brain from Alzheimer disease and Down syndrome patients.
{ECO:0000269|PubMed:2394826}.
-!- DEVELOPMENTAL STAGE: High expression levels in fetal and infant
brains; much lower in adult brains. {ECO:0000269|PubMed:2394826}.
-!- PTM: The composition of the O-linked carbohydrate on Thr-27 is
complex and varied. In the crystallographic structure, the
attached sugar appears to be N-acetylglucosamine, typical of an
intracellular protein, rather than N-acetylgalactosamine.
{ECO:0000269|PubMed:2493268}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Lithostathine A;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_254";
-----------------------------------------------------------------------
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EMBL; M18963; AAA36558.1; -; mRNA.
EMBL; J05412; AAA36559.1; -; Genomic_DNA.
EMBL; M27190; AAA60546.1; -; mRNA.
EMBL; M27189; AAA60545.1; -; Genomic_DNA.
EMBL; AF172331; AAD51330.1; -; mRNA.
EMBL; AC017004; AAX88842.1; -; Genomic_DNA.
EMBL; CH471053; EAW99576.1; -; Genomic_DNA.
EMBL; CH471053; EAW99578.1; -; Genomic_DNA.
EMBL; BC005350; AAH05350.1; -; mRNA.
CCDS; CCDS1964.1; -.
PIR; A35197; RGHU1A.
PIR; A45751; A45751.
RefSeq; NP_002900.2; NM_002909.4.
UniGene; Hs.4158; -.
UniGene; Hs.49407; -.
UniGene; Hs.708865; -.
PDB; 1LIT; X-ray; 1.55 A; A=23-166.
PDB; 1QDD; X-ray; 1.30 A; A=23-166.
PDBsum; 1LIT; -.
PDBsum; 1QDD; -.
ProteinModelPortal; P05451; -.
SMR; P05451; -.
BioGrid; 111899; 6.
STRING; 9606.ENSP00000233735; -.
DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DrugBank; DB04522; Phosphonoserine.
MEROPS; I63.002; -.
iPTMnet; P05451; -.
PhosphoSitePlus; P05451; -.
BioMuta; REG1A; -.
DMDM; 131433; -.
PaxDb; P05451; -.
PeptideAtlas; P05451; -.
PRIDE; P05451; -.
ProteomicsDB; 51839; -.
DNASU; 5967; -.
Ensembl; ENST00000233735; ENSP00000233735; ENSG00000115386.
GeneID; 5967; -.
KEGG; hsa:5967; -.
UCSC; uc002snz.3; human.
CTD; 5967; -.
DisGeNET; 5967; -.
EuPathDB; HostDB:ENSG00000115386.5; -.
GeneCards; REG1A; -.
HGNC; HGNC:9951; REG1A.
HPA; CAB025138; -.
HPA; HPA045549; -.
HPA; HPA045579; -.
MIM; 167770; gene.
neXtProt; NX_P05451; -.
OpenTargets; ENSG00000115386; -.
PharmGKB; PA34318; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00700000104249; -.
HOGENOM; HOG000010281; -.
HOVERGEN; HBG004151; -.
InParanoid; P05451; -.
OMA; KSWGIGA; -.
OrthoDB; EOG091G0OLC; -.
PhylomeDB; P05451; -.
ChiTaRS; REG1A; human.
EvolutionaryTrace; P05451; -.
GeneWiki; REG1A; -.
GenomeRNAi; 5967; -.
PRO; PR:P05451; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115386; Expressed in 96 organ(s), highest expression level in islet of Langerhans.
CleanEx; HS_REG1A; -.
Genevisible; P05451; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0008083; F:growth factor activity; IDA:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
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; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Lectin; Pyrrolidone carboxylic acid;
Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:2493268}.
CHAIN 23 166 Lithostathine-1-alpha.
/FTId=PRO_0000017424.
DOMAIN 34 164 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
MOD_RES 23 23 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:2493268}.
CARBOHYD 27 27 O-linked (GlcNAc...) threonine.
{ECO:0000269|PubMed:2493268}.
DISULFID 36 47 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:2226837}.
DISULFID 64 162 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:2226837}.
DISULFID 137 154 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:2226837}.
CONFLICT 5 7 SSY -> NSF (in Ref. 3; AAA60546/
AAA60545). {ECO:0000305}.
CONFLICT 13 13 C -> S (in Ref. 3; AAA60546/AAA60545).
{ECO:0000305}.
CONFLICT 19 19 Q -> L (in Ref. 3; AAA60546).
{ECO:0000305}.
CONFLICT 101 101 G -> A (in Ref. 2; AAA36559).
{ECO:0000305}.
HELIX 31 33 {ECO:0000244|PDB:1QDD}.
STRAND 41 43 {ECO:0000244|PDB:1QDD}.
STRAND 46 55 {ECO:0000244|PDB:1QDD}.
HELIX 57 66 {ECO:0000244|PDB:1QDD}.
HELIX 78 90 {ECO:0000244|PDB:1QDD}.
STRAND 96 103 {ECO:0000244|PDB:1QDD}.
STRAND 107 109 {ECO:0000244|PDB:1QDD}.
STRAND 131 133 {ECO:0000244|PDB:1QDD}.
STRAND 136 141 {ECO:0000244|PDB:1QDD}.
HELIX 142 144 {ECO:0000244|PDB:1QDD}.
STRAND 148 152 {ECO:0000244|PDB:1QDD}.
STRAND 158 165 {ECO:0000244|PDB:1QDD}.
SEQUENCE 166 AA; 18731 MW; EF93C760DC2DBCC3 CRC64;
MAQTSSYFML ISCLMFLSQS QGQEAQTELP QARISCPEGT NAYRSYCYYF NEDRETWVDA
DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI GLHDPKKNRR WHWSSGSLVS
YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK DVPCEDKFSF VCKFKN


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