[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1073/pnas.86.15.5738; PubMed=2668946 [NCBI, ExPASy, EBI, Israel, Japan] Nishi M., Chan S.J., Nagamatsu S., Bell G.I., Steiner D.F.; "Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone."; Proc. Natl. Acad. Sci. U.S.A. 86:5738-5742(1989).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1073/pnas.86.9.3127; PubMed=2654937 [NCBI, ExPASy, EBI, Israel, Japan] Leffert J.D., Newgard C.B., Okamoto H., Milburn J.L., Luskey K.L.; "Rat amylin: cloning and tissue-specific expression in pancreatic islets."; Proc. Natl. Acad. Sci. U.S.A. 86:3127-3130(1989).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=WAP; TISSUE=Liver; 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).
[4]	PROTEIN SEQUENCE OF 38-74. DOI=10.1016/0006-291X(89)91733-6; PubMed=2679555 [NCBI, ExPASy, EBI, Israel, Japan] Asai J., Nakazato M., Kangawa K., Matsukura S., Matsuo H.; "Isolation and sequence determination of rat islet amyloid polypeptide."; Biochem. Biophys. Res. Commun. 164:400-405(1989).
[5]	PROTEIN SEQUENCE OF 38-74. DOI=10.1016/0006-291X(90)90400-H; PubMed=2357234 [NCBI, ExPASy, EBI, Israel, Japan] Asai J., Nakazato M., Miyazato M., Kangawa K., Matsuo H., Matsukura S.; "Regional distribution and molecular forms of rat islet amyloid polypeptide."; Biochem. Biophys. Res. Commun. 169:788-795(1990).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 38-74. 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).

Comments

FUNCTION: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Abundant in the islets of Langerhans but is not present in the brain or seven other tissues examined.
SIMILARITY: Belongs to the calcitonin family.

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

M25390; AAA41359.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04544; AAA40730.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52820; CAA37003.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52821; CAA37003.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00202679; -.

S13566; TCRTIA.

NP_036718.1; -.

3D structure databases

ModBase

P12969.

Organism-specific databases

RGD

2854; Iapp.

Gene expression databases

ArrayExpress

P12969; -.

GermOnline

ENSRNOG00000012417; Rattus norvegicus.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-SubCell).
GO:0030141;	Cellular component: secretory granule (traceable author statement from RGD).
GO:0005179;	Molecular function: hormone activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006006;	Biological process: glucose metabolic process (traceable author statement from RGD).
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.

Genome annotation databases

Ensembl

ENSRNOG00000012417; Rattus norvegicus. [Contig view]

GeneID

24476; -.

KEGG

rno:24476; -.

Phylogenomic databases

HOVERGEN

P12969; -.

OMA

P12969; NTYGKRN.

Other

603429; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amidation; Amyloid; Cleavage on pair of basic residues; Direct protein sequencing; Disulfide bond; Hormone; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`Potential.`
`PROPEP`	`24 35`	`12`		`PRO_0000004121`
`PEPTIDE`	`38 74`	`37`	`Islet amyloid polypeptide.`	`PRO_0000004122`
`PROPEP`	`78 93`	`16`		`PRO_0000004123`
`MOD_RES`	`74 74`		`Tyrosine amide.`
`DISULFID`	`39 44`		`By similarity.`

Sequence information

Length: 93 AA [This is the length of the unprocessed precursor]

Molecular weight: 10015 Da [This is the MW of the unprocessed precursor]

CRC64: 5A76C92E624DA962 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRCISRLPAV LLILSVALGH LRATPVGSGT NPQVDKRKCN TATCATQRLA NFLVRSSNNL 

        70         80         90 
GPVLPPTNVG SNTYGKRNVA EDPNRESLDF LLL

P12969 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools