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Protein

Lithostathine-1-alpha

Gene

REG1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration.

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • growth factor activity Source: MGI

GO - Biological processi

  • positive regulation of cell proliferation Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Lectin

Protein family/group databases

MEROPSiI63.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Lithostathine-1-alpha
Alternative name(s):
Islet cells regeneration factor
Short name:
ICRF
Islet of Langerhans regenerating protein
Short name:
REG
Pancreatic stone protein
Short name:
PSP
Pancreatic thread protein
Short name:
PTP
Regenerating islet-derived protein 1-alpha
Short name:
REG-1-alpha
Regenerating protein I alpha
Gene namesi
Name:REG1A
Synonyms:PSPS, PSPS1, REG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9951. REG1A.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34318.

Polymorphism and mutation databases

BioMutaiREG1A.
DMDMi131433.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22222 PublicationsAdd
BLAST
Chaini23 – 166144Lithostathine-1-alphaPRO_0000017424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Pyrrolidone carboxylic acid1 Publication
Glycosylationi27 – 271O-linked (GlcNAc...)1 Publication
Disulfide bondi36 ↔ 47PROSITE-ProRule annotation1 Publication
Disulfide bondi64 ↔ 162PROSITE-ProRule annotation1 Publication
Disulfide bondi137 ↔ 154PROSITE-ProRule annotation1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP05451.
PeptideAtlasiP05451.
PRIDEiP05451.

PTM databases

PhosphoSiteiP05451.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

High expression levels in fetal and infant brains; much lower in adult brains.1 Publication

Gene expression databases

BgeeiP05451.
CleanExiHS_REG1A.
GenevisibleiP05451. HS.

Organism-specific databases

HPAiCAB025138.
HPA045549.
HPA045579.

Interactioni

GO - Molecular functioni

  • growth factor activity Source: MGI

Protein-protein interaction databases

BioGridi111899. 3 interactions.
STRINGi9606.ENSP00000233735.

Structurei

Secondary structure

1
166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 333Combined sources
Beta strandi41 – 433Combined sources
Beta strandi46 – 5510Combined sources
Helixi57 – 6610Combined sources
Helixi78 – 9013Combined sources
Beta strandi96 – 1038Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi136 – 1416Combined sources
Helixi142 – 1443Combined sources
Beta strandi148 – 1525Combined sources
Beta strandi158 – 1658Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LITX-ray1.55A23-166[»]
1QDDX-ray1.30A23-166[»]
ProteinModelPortaliP05451.
SMRiP05451. Positions 36-166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05451.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 164131C-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104249.
HOGENOMiHOG000010281.
HOVERGENiHBG004151.
InParanoidiP05451.
OMAiKSWGIGA.
OrthoDBiEOG79KPH7.
PhylomeDBiP05451.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05451-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQTSSYFML ISCLMFLSQS QGQEAQTELP QARISCPEGT NAYRSYCYYF
60 70 80 90 100
NEDRETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI
110 120 130 140 150
GLHDPKKNRR WHWSSGSLVS YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK
160
DVPCEDKFSF VCKFKN
Length:166
Mass (Da):18,731
Last modified:October 1, 1989 - v3
Checksum:iEF93C760DC2DBCC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 73SSY → NSF in AAA60546 (PubMed:2525567).Curated
Sequence conflicti5 – 73SSY → NSF in AAA60545 (PubMed:2525567).Curated
Sequence conflicti13 – 131C → S in AAA60546 (PubMed:2525567).Curated
Sequence conflicti13 – 131C → S in AAA60545 (PubMed:2525567).Curated
Sequence conflicti19 – 191Q → L in AAA60546 (PubMed:2525567).Curated
Sequence conflicti101 – 1011G → A in AAA36559 (PubMed:2332435).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18963 mRNA. Translation: AAA36558.1.
J05412 Genomic DNA. Translation: AAA36559.1.
M27190 mRNA. Translation: AAA60546.1.
M27189 Genomic DNA. Translation: AAA60545.1.
AF172331 mRNA. Translation: AAD51330.1.
AC017004 Genomic DNA. Translation: AAX88842.1.
CH471053 Genomic DNA. Translation: EAW99576.1.
CH471053 Genomic DNA. Translation: EAW99578.1.
BC005350 mRNA. Translation: AAH05350.1.
CCDSiCCDS1964.1.
PIRiA35197. RGHU1A.
A45751.
RefSeqiNP_002900.2. NM_002909.4.
UniGeneiHs.4158.
Hs.49407.
Hs.708865.

Genome annotation databases

EnsembliENST00000233735; ENSP00000233735; ENSG00000115386.
GeneIDi5967.
KEGGihsa:5967.
UCSCiuc002snz.3. human.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Lithostathine A

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18963 mRNA. Translation: AAA36558.1.
J05412 Genomic DNA. Translation: AAA36559.1.
M27190 mRNA. Translation: AAA60546.1.
M27189 Genomic DNA. Translation: AAA60545.1.
AF172331 mRNA. Translation: AAD51330.1.
AC017004 Genomic DNA. Translation: AAX88842.1.
CH471053 Genomic DNA. Translation: EAW99576.1.
CH471053 Genomic DNA. Translation: EAW99578.1.
BC005350 mRNA. Translation: AAH05350.1.
CCDSiCCDS1964.1.
PIRiA35197. RGHU1A.
A45751.
RefSeqiNP_002900.2. NM_002909.4.
UniGeneiHs.4158.
Hs.49407.
Hs.708865.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LITX-ray1.55A23-166[»]
1QDDX-ray1.30A23-166[»]
ProteinModelPortaliP05451.
SMRiP05451. Positions 36-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111899. 3 interactions.
STRINGi9606.ENSP00000233735.

Protein family/group databases

MEROPSiI63.002.

PTM databases

PhosphoSiteiP05451.

Polymorphism and mutation databases

BioMutaiREG1A.
DMDMi131433.

Proteomic databases

PaxDbiP05451.
PeptideAtlasiP05451.
PRIDEiP05451.

Protocols and materials databases

DNASUi5967.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233735; ENSP00000233735; ENSG00000115386.
GeneIDi5967.
KEGGihsa:5967.
UCSCiuc002snz.3. human.

Organism-specific databases

CTDi5967.
GeneCardsiREG1A.
HGNCiHGNC:9951. REG1A.
HPAiCAB025138.
HPA045549.
HPA045579.
MIMi167770. gene.
neXtProtiNX_P05451.
PharmGKBiPA34318.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104249.
HOGENOMiHOG000010281.
HOVERGENiHBG004151.
InParanoidiP05451.
OMAiKSWGIGA.
OrthoDBiEOG79KPH7.
PhylomeDBiP05451.

Miscellaneous databases

ChiTaRSiREG1A. human.
EvolutionaryTraceiP05451.
GeneWikiiREG1A.
GenomeRNAii5967.
NextBioi23230.
PROiP05451.
SOURCEiSearch...

Gene expression databases

BgeeiP05451.
CleanExiHS_REG1A.
GenevisibleiP05451. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel gene activated in regenerating islets."
    Terazono K., Yamamoto H., Takasawa S., Shiga K., Yonemura Y., Tochino Y., Okamoto H.
    J. Biol. Chem. 263:2111-2114(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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."
    Watanabe T., Yonekura H., Terazono K., Yamamoto H., Okamoto H.
    J. Biol. Chem. 265:7432-7439(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Secretory pancreatic stone protein messenger RNA. Nucleotide sequence and expression in chronic calcifying pancreatitis."
    Giorgi D., Bernard J.-P., Rouquier S., Iovanna J., Sarles H., Dagorn J.-C.
    J. Clin. Invest. 84:100-106(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Pancreas.
  4. Boonyasrisawat W., Tandhanand-Banchuin N., Vannasaeng S., Yenchitsomanus P.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    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.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  8. "Complete amino acid sequence of an immunoreactive form of human pancreatic stone protein isolated from pancreatic juice."
    de Caro A.M., Bonicel J.J., Rouimi P., de Caro J.D., Sarles H., Rovery M.
    Eur. J. Biochem. 168:201-207(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-166.
  9. "Partial amino acid sequence of human pancreatic stone protein, a novel pancreatic secretory protein."
    Montalto G., Bonicel J.J., Multigner L., Rovery M., Sarles H., de Caro A.M.
    Biochem. J. 238:227-232(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-98.
  10. "Isolation, characterization, and distribution of an unusual pancreatic human secretory protein."
    Gross J., Carlson R.I., Brauer A.W., Margolies M.N., Warshaw A.L., Wands J.R.
    J. Clin. Invest. 76:2115-2125(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-78.
  11. "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."
    de Caro A.M., Adrich Z., Fournet B., Capon C., Bonicel J.J., de Caro J.D., Rovery M.
    Biochim. Biophys. Acta 994:281-284(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-47, PYROGLUTAMATE FORMATION AT GLN-23, GLYCOSYLATION AT THR-27.
  12. "Cleavage of the Arg-Ile bond in the native polypeptide chain of human pancreatic stone protein."
    Rouimi P., Bonicel J., Rovery M., de Caro A.
    FEBS Lett. 216:195-199(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-58.
  13. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-37.
  14. "The human reg gene encodes pancreatic stone protein."
    Stewart T.A.
    Biochem. J. 260:622-623(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTITY OF REG WITH PSP.
  15. "Isolation and characterization of human reg protein produced in Saccharomyces cerevisiae."
    Itoh T., Tsuzuki H., Katoh T., Teraoka H., Matsumoto K., Yoshida N., Terazono K., Watanabe T., Yonekura H., Yamamoto H., Okamoto H.
    FEBS Lett. 272:85-88(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  16. "Enhanced expression of an exocrine pancreatic protein in Alzheimer's disease and the developing human brain."
    de la Monte S.M., Ozturk M., Wands J.R.
    J. Clin. Invest. 86:1004-1013(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  17. "Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation."
    Bertrand J.A., Pignol D., Bernard J.-P., Verdier J.-M., Dagorn J.-C., Fontecilla-Camps J.-C.
    EMBO J. 15:2678-2684(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  18. "Mechanism of calcite crystal growth inhibition by the N-terminal undecapeptide of lithostathine."
    Gerbaud V., Pignol D., Loret E., Bertrand J.A., Berland Y., Fontecilla-Camps J.-C., Canselier J.P., Gabas N., Verdier J.-M.
    J. Biol. Chem. 275:1057-1064(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 23-166.
  19. "What function for human lithostathine?: structural investigations by three-dimensional structure modeling and high-resolution NMR spectroscopy."
    Patard L., Stoven V., Gharib B., Bontems F., Lallemand J.-Y., de Reggi M.
    Protein Eng. 9:949-957(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 34-164.

Entry informationi

Entry nameiREG1A_HUMAN
AccessioniPrimary (citable) accession number: P05451
Secondary accession number(s): P11379, Q4ZG28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1989
Last modified: November 11, 2015
This is version 177 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.