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Protein

Islet amyloid polypeptide

Gene

IAPP

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

Functioni

Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • receptor binding Source: ProtInc

GO - Biological processi

  • apoptotic process Source: ProtInc
  • cell-cell signaling Source: ProtInc
  • cellular protein metabolic process Source: Reactome
  • eating behavior Source: Ensembl
  • negative regulation of bone resorption Source: Ensembl
  • negative regulation of cell differentiation Source: Ensembl
  • sensory perception of pain Source: Ensembl
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

BioCyciZFISH:ENSG00000121351-MONOMER.
ReactomeiR-HSA-210745. Regulation of gene expression in beta cells.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-419812. Calcitonin-like ligand receptors.
R-HSA-977225. Amyloid fiber formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Islet amyloid polypeptide
Alternative name(s):
Amylin
Diabetes-associated peptide
Short name:
DAP
Insulinoma amyloid peptide
Gene namesi
Name:IAPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:5329. IAPP.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi48F → A, D or S: Promotes formation of fibrillar aggregates. 1 Publication1

Organism-specific databases

DisGeNETi3375.
OpenTargetsiENSG00000121351.
PharmGKBiPA29579.

Chemistry databases

ChEMBLiCHEMBL1914266.

Polymorphism and mutation databases

BioMutaiIAPP.
DMDMi124006.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000000410523 – 319
PeptideiPRO_000000410634 – 70Islet amyloid polypeptideAdd BLAST37
PropeptideiPRO_000000410774 – 89Add BLAST16

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi35 ↔ 403 Publications
Modified residuei70Tyrosine amide2 Publications1

Post-translational modificationi

Amyloid fibrils are degraded by IDE.

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiP10997.
PeptideAtlasiP10997.
PRIDEiP10997.

PTM databases

iPTMnetiP10997.
PhosphoSitePlusiP10997.

Miscellaneous databases

PMAP-CutDBP10997.

Expressioni

Gene expression databases

BgeeiENSG00000121351.
CleanExiHS_IAPP.
ExpressionAtlasiP10997. baseline and differential.
GenevisibleiP10997. HS.

Organism-specific databases

HPAiCAB000352.
HPA053194.

Interactioni

Subunit structurei

Interacts with IDE and INS. Can form homodimers. Interaction with INS inhibits homodimerization and fibril formation.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-8526679,EBI-8526679

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • receptor binding Source: ProtInc

Protein-protein interaction databases

DIPiDIP-29913N.
MINTiMINT-8074874.
STRINGi9606.ENSP00000240652.

Structurei

Secondary structure

189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 38Combined sources3
Helixi43 – 49Combined sources7
Helixi53 – 60Combined sources8
Turni63 – 69Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KUWNMR-A53-62[»]
2G48X-ray2.60C/D34-70[»]
2KB8NMR-A34-70[»]
2L86NMR-A34-70[»]
3DG1X-ray1.66A61-66[»]
3FPOX-ray1.50A51-56[»]
3FR1X-ray1.85A47-52[»]
3FTHX-ray1.84A/B47-53[»]
3FTKX-ray1.50A64-70[»]
3FTLX-ray1.60A/B64-70[»]
3FTRX-ray1.61A61-66[»]
3G7VX-ray1.86A/B/C/D34-69[»]
3G7WX-ray1.75A34-55[»]
3HGZX-ray2.91D/E34-70[»]
ProteinModelPortaliP10997.
SMRiP10997.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10997.

Family & Domainsi

Domaini

The mature protein is largely unstructured in the absence of a cognate ligand, and has a strong tendency to form fibrillar aggregates. Homodimerization may be the first step of amyloid formation.3 Publications

Sequence similaritiesi

Belongs to the calcitonin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J0NB. Eukaryota.
ENOG410Z7V7. LUCA.
GeneTreeiENSGT00510000048671.
HOGENOMiHOG000038203.
HOVERGENiHBG096065.
InParanoidiP10997.
KOiK08039.
OMAiSHQMEKR.
OrthoDBiEOG091G15QG.
PhylomeDBiP10997.
TreeFamiTF330783.

Family and domain databases

InterProiIPR021117. Calcitonin-like.
IPR021116. Calcitonin/adrenomedullin.
IPR018360. Calcitonin_CS.
IPR001693. Calcitonin_peptide-like.
IPR000443. Pro-islet_amyloid_polypep.
[Graphical view]
PANTHERiPTHR10505. PTHR10505. 1 hit.
PfamiPF00214. Calc_CGRP_IAPP. 1 hit.
[Graphical view]
PRINTSiPR00818. ISLETAMYLOID.
SMARTiSM00113. CALCITONIN. 1 hit.
[Graphical view]
PROSITEiPS00258. CALCITONIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10997-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGILKLQVFL IVLSVALNHL KATPIESHQV EKRKCNTATC ATQRLANFLV
60 70 80
HSSNNFGAIL SSTNVGSNTY GKRNAVEVLK REPLNYLPL
Length:89
Mass (Da):9,806
Last modified:July 1, 1989 - v1
Checksum:iAA8B1F7FD9FCB4BD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53S → C in CAA39504 (PubMed:2365085).Curated1

Mass spectrometryi

Molecular mass is 3936 Da from positions 34 - 70. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01208053S → G.2 PublicationsCorresponds to variant rs1800203dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27503 Genomic DNA. Translation: AAA35524.1.
X14904 mRNA. Translation: CAA33032.1.
X14905 mRNA. Translation: CAA33033.1.
X14902 Genomic DNA. Translation: CAA33031.1.
X14903 Genomic DNA. Translation: CAB57804.1.
X13859 Genomic DNA. Translation: CAB57803.1.
J04422 mRNA. Translation: AAA52281.1.
M21785 Genomic DNA. Translation: AAA51728.1.
M26650 Genomic DNA. Translation: AAA35983.1.
X52818, X52819 Genomic DNA. Translation: CAA37002.1.
X56030, X55634 Genomic DNA. Translation: CAA39504.1.
X68830 Genomic DNA. Translation: CAA48724.1.
DQ516082 mRNA. Translation: ABG27010.1.
CH471094 Genomic DNA. Translation: EAW96426.1.
CCDSiCCDS8688.1.
PIRiS04016. TCHUIA.
RefSeqiNP_000406.1. NM_000415.2.
NP_001316130.1. NM_001329201.1.
UniGeneiHs.46835.

Genome annotation databases

EnsembliENST00000240652; ENSP00000240652; ENSG00000121351.
ENST00000539393; ENSP00000437357; ENSG00000121351.
GeneIDi3375.
KEGGihsa:3375.
UCSCiuc001rev.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Amylin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27503 Genomic DNA. Translation: AAA35524.1.
X14904 mRNA. Translation: CAA33032.1.
X14905 mRNA. Translation: CAA33033.1.
X14902 Genomic DNA. Translation: CAA33031.1.
X14903 Genomic DNA. Translation: CAB57804.1.
X13859 Genomic DNA. Translation: CAB57803.1.
J04422 mRNA. Translation: AAA52281.1.
M21785 Genomic DNA. Translation: AAA51728.1.
M26650 Genomic DNA. Translation: AAA35983.1.
X52818, X52819 Genomic DNA. Translation: CAA37002.1.
X56030, X55634 Genomic DNA. Translation: CAA39504.1.
X68830 Genomic DNA. Translation: CAA48724.1.
DQ516082 mRNA. Translation: ABG27010.1.
CH471094 Genomic DNA. Translation: EAW96426.1.
CCDSiCCDS8688.1.
PIRiS04016. TCHUIA.
RefSeqiNP_000406.1. NM_000415.2.
NP_001316130.1. NM_001329201.1.
UniGeneiHs.46835.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KUWNMR-A53-62[»]
2G48X-ray2.60C/D34-70[»]
2KB8NMR-A34-70[»]
2L86NMR-A34-70[»]
3DG1X-ray1.66A61-66[»]
3FPOX-ray1.50A51-56[»]
3FR1X-ray1.85A47-52[»]
3FTHX-ray1.84A/B47-53[»]
3FTKX-ray1.50A64-70[»]
3FTLX-ray1.60A/B64-70[»]
3FTRX-ray1.61A61-66[»]
3G7VX-ray1.86A/B/C/D34-69[»]
3G7WX-ray1.75A34-55[»]
3HGZX-ray2.91D/E34-70[»]
ProteinModelPortaliP10997.
SMRiP10997.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29913N.
MINTiMINT-8074874.
STRINGi9606.ENSP00000240652.

Chemistry databases

ChEMBLiCHEMBL1914266.

PTM databases

iPTMnetiP10997.
PhosphoSitePlusiP10997.

Polymorphism and mutation databases

BioMutaiIAPP.
DMDMi124006.

Proteomic databases

PaxDbiP10997.
PeptideAtlasiP10997.
PRIDEiP10997.

Protocols and materials databases

DNASUi3375.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000240652; ENSP00000240652; ENSG00000121351.
ENST00000539393; ENSP00000437357; ENSG00000121351.
GeneIDi3375.
KEGGihsa:3375.
UCSCiuc001rev.4. human.

Organism-specific databases

CTDi3375.
DisGeNETi3375.
GeneCardsiIAPP.
HGNCiHGNC:5329. IAPP.
HPAiCAB000352.
HPA053194.
MIMi147940. gene.
neXtProtiNX_P10997.
OpenTargetsiENSG00000121351.
PharmGKBiPA29579.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J0NB. Eukaryota.
ENOG410Z7V7. LUCA.
GeneTreeiENSGT00510000048671.
HOGENOMiHOG000038203.
HOVERGENiHBG096065.
InParanoidiP10997.
KOiK08039.
OMAiSHQMEKR.
OrthoDBiEOG091G15QG.
PhylomeDBiP10997.
TreeFamiTF330783.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000121351-MONOMER.
ReactomeiR-HSA-210745. Regulation of gene expression in beta cells.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-419812. Calcitonin-like ligand receptors.
R-HSA-977225. Amyloid fiber formation.

Miscellaneous databases

EvolutionaryTraceiP10997.
GeneWikiiAmylin.
GenomeRNAii3375.
PMAP-CutDBP10997.
PROiP10997.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000121351.
CleanExiHS_IAPP.
ExpressionAtlasiP10997. baseline and differential.
GenevisibleiP10997. HS.

Family and domain databases

InterProiIPR021117. Calcitonin-like.
IPR021116. Calcitonin/adrenomedullin.
IPR018360. Calcitonin_CS.
IPR001693. Calcitonin_peptide-like.
IPR000443. Pro-islet_amyloid_polypep.
[Graphical view]
PANTHERiPTHR10505. PTHR10505. 1 hit.
PfamiPF00214. Calc_CGRP_IAPP. 1 hit.
[Graphical view]
PRINTSiPR00818. ISLETAMYLOID.
SMARTiSM00113. CALCITONIN. 1 hit.
[Graphical view]
PROSITEiPS00258. CALCITONIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIAPP_HUMAN
AccessioniPrimary (citable) accession number: P10997
Secondary accession number(s): Q0ZD87, Q14598
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 166 of the entry and version 1 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

Miscellaneous

IAPP is the peptide subunit of amyloid found in pancreatic islets of type 2 diabetic patients and in insulinomas.

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.