ID A0A3P8NXQ7_ASTCA Unreviewed; 131 AA.
AC A0A3P8NXQ7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Islet amyloid polypeptide {ECO:0000313|Ensembl:ENSACLP00000009520.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000009520.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000009520.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000009520.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Causes a rapid but short-lived drop in the level of calcium
CC and phosphate in blood by promoting the incorporation of those ions in
CC the bones. {ECO:0000256|ARBA:ARBA00003306}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the calcitonin family.
CC {ECO:0000256|ARBA:ARBA00009222}.
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DR AlphaFoldDB; A0A3P8NXQ7; -.
DR STRING; 8154.ENSACLP00000009520; -.
DR Ensembl; ENSACLT00000009742.1; ENSACLP00000009520.1; ENSACLG00000006495.1.
DR GeneTree; ENSGT00510000048671; -.
DR OMA; MYHLKVP; -.
DR OrthoDB; 3910643at2759; -.
DR Proteomes; UP000265100; Chromosome 17.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR Gene3D; 6.10.250.2190; -; 1.
DR InterPro; IPR021117; Calcitonin-like.
DR InterPro; IPR021116; Calcitonin/adrenomedullin.
DR InterPro; IPR018360; Calcitonin_CS.
DR InterPro; IPR001693; Calcitonin_peptide-like.
DR InterPro; IPR000443; IAPP.
DR PANTHER; PTHR10505; CALCITONIN-RELATED; 1.
DR PANTHER; PTHR10505:SF4; ISLET AMYLOID POLYPEPTIDE; 1.
DR Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR PRINTS; PR00818; ISLETAMYLOID.
DR SMART; SM00113; CALCITONIN; 1.
DR PROSITE; PS00258; CALCITONIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR621116-50};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..131
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018125144"
FT TRANSMEM 46..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..121
FT /note="Calcitonin peptide-like"
FT /evidence="ECO:0000259|SMART:SM00113"
FT DISULFID 82..87
FT /evidence="ECO:0000256|PIRSR:PIRSR621116-50"
SQ SEQUENCE 131 AA; 14423 MW; B9B3AA933E6181D7 CRC64;
MYHLRVPVLL LMLLVLLHCI TAAPSYRYFS PSSSSEQESD LPDSEAWLLP GLISNPFLSL
VGTRPRRGLT AMNSHHIEKR KCNTATCVTQ RLADFLVRSS NTIGTVYAPT NVGSATYGKR
GLLEPSGYVN L
//
