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UniProtKB/Swiss-Prot entry P10997


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IAPP_HUMAN
Primary accession number P10997
Secondary accession number Q14598
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 99)
Name and origin of the protein
Protein name Islet amyloid polypeptide [Precursor]
Synonyms Amylin
Diabetes-associated peptide
DAP
Insulinoma amyloid peptide
Gene name
Name: IAPP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1016/0014-5793(89)81260-8; PubMed=2651160 [NCBI, ExPASy, EBI, Israel, Japan]
Mosselman S., Hoeppener J.W.M., Lips C.J.M., Jansz H.S.;
"The complete islet amyloid polypeptide precursor is encoded by two exons.";
FEBS Lett. 247:154-158(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2608057 [NCBI, ExPASy, EBI, Israel, Japan]
Nishi M., Sanke T., Seino S., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Bell G.I., Steiner D.F.;
"Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history.";
Mol. Endocrinol. 3:1775-1781(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=3053705 [NCBI, ExPASy, EBI, Israel, Japan]
Sanke T., Bell G.I., Sample C., Rubenstein A.H., Steiner D.F.;
"An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing.";
J. Biol. Chem. 263:17243-17246(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0014-5793(90)80314-9; PubMed=2365085 [NCBI, ExPASy, EBI, Israel, Japan]
Christmanson L., Rorsman F., Stenman G., Westermark P., Betsholtz C.;
"The human islet amyloid polypeptide (IAPP) gene. Organization, chromosomal localization and functional identification of a promoter region.";
FEBS Lett. 267:160-166(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0167-4781(90)90210-S; PubMed=2223885 [NCBI, ExPASy, EBI, Israel, Japan]
van Mansfeld A.D.M., Mosselman S., Hoeppener J.W.M., Zandberg J., van Teeffelen H.A.A.M., Baas P.D., Lips C.J.M., Jansz H.S.;
"Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man.";
Biochim. Biophys. Acta 1087:235-240(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0006-291X(92)90255-J; PubMed=1282806 [NCBI, ExPASy, EBI, Israel, Japan]
Hoeppener J.W.M., Oosterwijk C., Visser-Vernooy H.J., Lips C.J.M., Jansz H.S.;
"Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site.";
Biochem. Biophys. Res. Commun. 189:1569-1577(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-89.
DOI=10.1016/0014-5793(88)80922-0; PubMed=3181427 [NCBI, ExPASy, EBI, Israel, Japan]
Mosselman S., Hoeppener J.W.M., Zandberg J., van Mansfeld A.D.M., Geurts van Kessel A.H.M., Lips C.J.M., Jansz H.S.;
"Islet amyloid polypeptide: identification and chromosomal localization of the human gene.";
FEBS Lett. 239:227-232(1988).
[8]
PROTEIN SEQUENCE OF 34-70, AND DISULFIDE BOND.
DOI=10.1073/pnas.84.23.8628; PubMed=3317417 [NCBI, ExPASy, EBI, Israel, Japan]
Cooper G.J., Willis A.C., Clark A., Turner R.C., Sim R.B., Reid K.B.;
"Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.";
Proc. Natl. Acad. Sci. U.S.A. 84:8628-8632(1987).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 34-70, AND SYNTHESIS OF 53-62.
DOI=10.1016/0014-5793(89)81467-X; PubMed=2666169 [NCBI, ExPASy, EBI, Israel, Japan]
Betsholtz C., Christmansson L., Engstroem U., Rorsman F., Svensson V., Johnson K.H., Westermark P.;
"Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species.";
FEBS Lett. 251:261-264(1989).
[10]
PROTEIN SEQUENCE OF 34-70.
DOI=10.1016/0167-0115(90)90004-G; PubMed=2091067 [NCBI, ExPASy, EBI, Israel, Japan]
Nakazato M., Asai J., Miyazato M., Matsukura S., Kangawa K., Matsuo H.;
"Isolation and identification of islet amyloid polypeptide in normal human pancreas.";
Regul. Pept. 31:179-186(1990).
[11]
PROTEIN SEQUENCE OF 34-52.
DOI=10.1016/0006-291X(86)90708-4; PubMed=3535798 [NCBI, ExPASy, EBI, Israel, Japan]
Westermark P., Wernstedt C., Wilander E., Sletten K.;
"A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas.";
Biochem. Biophys. Res. Commun. 140:827-831(1986).
[12]
PROTEIN SEQUENCE OF 34-70.
DOI=10.1073/pnas.84.11.3881; PubMed=3035556 [NCBI, ExPASy, EBI, Israel, Japan]
Westermark P., Wernstedt C., Wilander E., Hayden D.W., O'Brien T.D., Johnson K.H.;
"Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.";
Proc. Natl. Acad. Sci. U.S.A. 84:3881-3885(1987).
[13]
PROTEIN SEQUENCE OF 30-89.
DOI=10.1073/pnas.86.24.9662; PubMed=2690069 [NCBI, ExPASy, EBI, Israel, Japan]
Roberts A.N., Leighton B., Todd J.A., Cockburn D., Schofield P.N., Sutton R., Holt S., Boyd Y., Day A.J., Foot E.A., Willis A.C., Reid K.B.M., Cooper G.J.S.;
"Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus.";
Proc. Natl. Acad. Sci. U.S.A. 86:9662-9666(1989).
[14]
STRUCTURE BY NMR OF IAPP.
PubMed=2039456 [NCBI, ExPASy, EBI, Israel, Japan]
Hubbard J.A.M., Martin S.R., Chaplin L.C., Bose C., Kelly S.M., Price N.C.;
"Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin.";
Biochem. J. 275:785-788(1991).
[15]
VARIANT GLY-53.
PubMed=8772735 [NCBI, ExPASy, EBI, Israel, Japan]
Sakagashira S., Sanke T., Hanabusa T., Shimomura H., Ohagi S., Kumagaye K.Y., Nakajima K., Nanjo K.;
"Missense mutation of amylin gene (S20G) in Japanese NIDDM patients.";
Diabetes 45:1279-1281(1996).
[16]
VARIANT GLY-53.
DOI=10.1007/s001250051060; PubMed=9794116 [NCBI, ExPASy, EBI, Israel, Japan]
Chuang L.M., Lee K.C., Huang C.N., Wu H.P., Tai T.Y., Lin B.J.;
"Role of S20G mutation of amylin gene in insulin secretion, insulin sensitivity, and type II diabetes mellitus in Taiwanese patients.";
Diabetologia 41:1250-1251(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M27503; AAA35524.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14904; CAA33032.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14905; CAA33033.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14902; CAA33031.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14903; CAB57804.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13859; CAB57803.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04422; AAA52281.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21785; AAA51728.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M26650; AAA35983.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52818; CAA37002.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52819; CAA37002.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56030; CAA39504.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X55634; CAA39504.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68830; CAA48724.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00023679; -.
PIR S04016; TCHUIA.
RefSeq NP_000406.1; -.
UniGene Hs.46835
3D structure databases
PDB
1KUW; NMR; -; A=53-62.[ExPASy / RCSB / EBI]
2G48; X-ray; 2.60 A; C/D=34-70.[ExPASy / RCSB / EBI]
2KB8; NMR; -; A=34-70.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1KUW; -.
2G48; -.
2KB8; -.
ModBase P10997.
Enzyme and pathway databases
Reactome REACT_13698; Regulation of beta-cell development.
Organism-specific databases
GeneCards GC12P021417; -.
H-InvDB HIX0036861; -.
HGNC HGNC:5329; IAPP.
GenAtlas IAPP.
HPA CAB000352; -.
MIM 147940; gene. [NCBI / EBI]
PharmGKB PA29579; -.
Gene expression databases
ArrayExpress P10997; -.
Bgee P10997; -.
CleanEx HS_IAPP; -.
GermOnline ENSG00000121351; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0005179; Molecular function: hormone activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006915; Biological process: apoptosis (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001693; Calcitonin-like.
IPR018360; Calcitonin_CS.
IPR000443; Islet_amyloid_polypep.
Graphical view of domain structure.
PANTHER PTHR10505; Calcitonin-like; 1.
Pfam PF00214; Calc_CGRP_IAPP; 1.
Pfam graphical view of domain structure.
PRINTS PR00818; ISLETAMYLOID.
SMART SM00113; CALCITONIN; 1.
SMART graphical view of domain structure.
PROSITE PS00258; CALCITONIN; 1.
Proteomic databases
PRIDE P10997; -.
Genome annotation databases
Ensembl ENSG00000121351; Homo sapiens. [Contig view]
GeneID 3375; -.
KEGG hsa:3375; -.
Phylogenomic databases
HOGENOM P10997; -.
HOVERGEN P10997; -.
OMA P10997; NTYGKRN.
Other
DrugBank DB00790; Perindopril.
NextBio 13352; -.
PMAP-CutDB P10997; -.
SOURCE IAPP; Homo sapiens.
ProtoNet P10997.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amidation; Amyloid; Cleavage on pair of basic residues; Direct protein sequencing; Disulfide bond; Hormone; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
SIGNAL   1   22  22     Potential. 
PROPEP   23   31  9      PRO_0000004105
PEPTIDE   34   70  37     Islet amyloid polypeptide. PRO_0000004106
PROPEP   74   89  16      PRO_0000004107
MOD_RES   70   70        Tyrosine amide. 
DISULFID   35   40         
VARIANT   53   53  1     S -> G (in dbSNP:rs1800203 [NCBI]). VAR_012080 
CONFLICT   53   53        S -> C (in Ref. 4; CAA39504). 
HELIX   36   38  3      
STRAND   47   50  4      
Sequence information
Length: 89 AA [This is the length of the unprocessed precursor] Molecular weight: 9806 Da [This is the MW of the unprocessed precursor] CRC64: AA8B1F7FD9FCB4BD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGILKLQVFL IVLSVALNHL KATPIESHQV EKRKCNTATC ATQRLANFLV HSSNNFGAIL 

        70         80 
SSTNVGSNTY GKRNAVEVLK REPLNYLPL 

P10997 in FASTA format

View entry in raw text format (no links)
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