P05451 (REG1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	REG1A
Synonyms:	PSPS, PSPS1, REG

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.14
Developmental stage	High expression levels in fetal and infant brains; much lower in adult brains. Ref.14
Post-translational modification	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.
Sequence similarities	Contains 1 C-type lectin domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Lectin
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of cell proliferation Traceable author statement. Source: ProtInc
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	growth factor activity Inferred from direct assay. Source: MGI sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.9 Ref.11

Chain

23 – 166

144

Lithostathine-1-alpha

PRO_0000017424

Regions

Domain

34 – 164

131

C-type lectin

Amino acid modifications

Modified residue

23

1

Pyrrolidone carboxylic acid

Glycosylation

27

1

O-linked (GlcNAc...)

Disulfide bond

36 ↔ 47

Ref.13

Disulfide bond

64 ↔ 162

Ref.13

Disulfide bond

137 ↔ 154

Ref.13

Experimental info

Sequence conflict

5 – 7

3

SSY → NSF in AAA60546. Ref.3

Sequence conflict

5 – 7

3

SSY → NSF in AAA60545. Ref.3

Sequence conflict

13

1

C → S in AAA60546. Ref.3

Sequence conflict

13

1

C → S in AAA60545. Ref.3

Sequence conflict

19

1

Q → L in AAA60546. Ref.3

Sequence conflict

101

1

G → A in AAA36559. Ref.2

Secondary structure

1

.

.

.

.

.

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.

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.

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.

.

.

.

166

Helix Strand Turn

Details...

Helix

31 – 33

3

Beta strand

41 – 43

3

Beta strand

46 – 55

10

Helix

57 – 66

10

Helix

78 – 90

13

Beta strand

96 – 103

8

Beta strand

107 – 109

3

Beta strand

131 – 133

3

Beta strand

136 – 141

6

Helix

142 – 144

3

Beta strand

148 – 152

5

Beta strand

158 – 165

8

Sequences

	Sequence		Length	Mass (Da)
	P05451 [UniParc]. Last modified October 1, 1989. Version 3. Checksum: EF93C760DC2DBCC3	FASTA	166	18,731
	10 20 30 40 50 60 MAQTSSYFML ISCLMFLSQS QGQEAQTELP QARISCPEGT NAYRSYCYYF NEDRETWVDA 70 80 90 100 110 120 DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI GLHDPKKNRR WHWSSGSLVS 130 140 150 160 YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK DVPCEDKFSF VCKFKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2963000] [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: 2332435] [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: 2525567] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[6]	"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: 3665916] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-166.
[7]	"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: 3541906] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-98.
[8]	"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: 3908481] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-78.
[9]	"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: 2493268] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-47.
[10]	"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: 3108036] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-58.
[11]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-37.
[12]	"The human reg gene encodes pancreatic stone protein." Stewart T.A. Biochem. J. 260:622-623(1989) [PubMed: 2764894] [Abstract] Cited for: IDENTITY OF REG WITH PSP.
[13]	"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: 2226837] [Abstract] Cited for: DISULFIDE BONDS.
[14]	"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: 2394826] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[15]	"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: 8654365] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[16]	"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: 10625646] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 23-166.
[17]	"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: 8961348] [Abstract] Cited for: STRUCTURE BY NMR OF 34-164.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

Lithostathine A

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
BC005350 mRNA. Translation: AAH05350.1.

IPI

IPI00009027.

PIR

RGHU1A. A35197.
A45751.

RefSeq

NP_002900.2. NM_002909.4.

UniGene

Hs.4158.
Hs.49407.
Hs.708865.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LIT	X-ray	1.55	A	23-166	[»]
1QDD	X-ray	1.30	A	23-166	[»]

ProteinModelPortal

P05451.

SMR

P05451. Positions 36-166.

ModBase

Search...

Protein-protein interaction databases

STRING

P05451.

Protein family/group databases

MEROPS

I63.002.

PTM databases

PhosphoSite

P05451.

Polymorphism databases

DMDM

131433.

Proteomic databases

PeptideAtlas

P05451.

PRIDE

P05451.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000233735; ENSP00000233735; ENSG00000115386.

GeneID

5967.

KEGG

hsa:5967.

UCSC

uc002snz.1. human.

Organism-specific databases

CTD

5967.

GeneCards

GC02P079259.

H-InvDB

HIX0002205.

HGNC

HGNC:9951. REG1A.

HPA

CAB025138.

MIM

167770. gene.

neXtProt

NX_P05451.

Orphanet

676. Hereditary chronic pancreatitis.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05288.

HOGENOM

HBG283257.

HOVERGEN

HBG004151.

InParanoid

P05451.

OMA

KSWGIGA.

OrthoDB

EOG498V22.

PhylomeDB

P05451.

Gene expression databases

ArrayExpress

P05451.

Bgee

P05451.

CleanEx

HS_REG1A.

Genevestigator

P05451.

GermOnline

ENSG00000115386. Homo sapiens.

Family and domain databases

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR003990. Pancreatis_ac.
[Graphical view]

Gene3D

G3DSA:3.10.100.10. C-type_lectin-like. 1 hit.

Pfam

PF00059. Lectin_C. 1 hit.
[Graphical view]

PRINTS

PR01504. PNCREATITSAP.

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

23230.

SOURCE

Search...

Entry information

Entry name

REG1A_HUMAN

Accession

Primary (citable) accession number: P05451
Secondary accession number(s): P11379

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	October 1, 1989
Last modified:	January 25, 2012
This is version 143 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.