ID A0A5A9PSU0_9TELE Unreviewed; 125 AA.
AC A0A5A9PSU0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-NOV-2024, entry version 14.
DE SubName: Full=Calcitonin gene-related peptide {ECO:0000313|EMBL:KAA0724119.1};
GN ORFNames=E1301_Tti023256 {ECO:0000313|EMBL:KAA0724119.1};
OS Triplophysa tibetana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Nemacheilidae; Triplophysa.
OX NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0724119.1, ECO:0000313|Proteomes:UP000324632};
RN [1] {ECO:0000313|EMBL:KAA0724119.1, ECO:0000313|Proteomes:UP000324632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0724119.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA0724119.1};
RX PubMed=30977968;
RA Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA Wang W., Yang R.;
RT "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT to the harsh high-altitude environment of the Tibetan Plateau.";
RL Mol. Ecol. Resour. 19:1027-1036(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA0724119.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SOYY01000002; KAA0724119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A9PSU0; -.
DR Proteomes; UP000324632; Chromosome 2.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0031716; F:calcitonin receptor binding; IEA:TreeGrafter.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:TreeGrafter.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:TreeGrafter.
DR Gene3D; 6.10.250.2190; -; 1.
DR InterPro; IPR021117; Calcitonin-like.
DR InterPro; IPR021116; Calcitonin/adrenomedullin.
DR InterPro; IPR018360; Calcitonin_CS.
DR InterPro; IPR015476; Calcitonin_gene-rel_peptide.
DR InterPro; IPR001693; Calcitonin_peptide-like.
DR PANTHER; PTHR10505:SF16; CALCITONIN; 1.
DR PANTHER; PTHR10505; CALCITONIN-RELATED; 1.
DR Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR PRINTS; PR00817; CALCITONINB.
DR SMART; SM00113; CALCITONIN; 1.
DR PROSITE; PS00258; CALCITONIN; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR621116-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000324632};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..125
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023130405"
FT DOMAIN 78..120
FT /note="Calcitonin peptide-like"
FT /evidence="ECO:0000259|SMART:SM00113"
FT DISULFID 81..86
FT /evidence="ECO:0000256|PIRSR:PIRSR621116-50"
SQ SEQUENCE 125 AA; 13642 MW; 08FCB944E14FCF60 CRC64;
MFLLKISSVL VAYAVIVCQM SCSQAAPVRG AQDLLTDRLA LMDFETRRLL SAIVKSVVQM
TAEEPVDEDN GSSVTAHKRA CNTATCVTHR LADFLSRSGG VGNRNFIPTN VGSKAFGRRR
RNLQL
//
