ID B5XGR7_SALSA Unreviewed; 143 AA.
AC B5XGR7;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Calcitonin-1 {ECO:0000313|EMBL:ACI70037.1, ECO:0000313|RefSeq:NP_001135058.1};
DE SubName: Full=Calcitonin-1-like isoform X1 {ECO:0000313|RefSeq:XP_014031410.1};
GN Name=CALC1 {ECO:0000313|EMBL:ACI70037.1};
GN Synonyms=calc1 {ECO:0000313|RefSeq:NP_001135058.1}, LOC106587496
GN {ECO:0000313|RefSeq:XP_014031410.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI70037.1};
RN [1] {ECO:0000313|EMBL:ACI70037.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI70037.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI70037.1, ECO:0000313|RefSeq:NP_001135058.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI70037.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACI70037.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI70037.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007829|PDB:7TYN, ECO:0007829|PDB:7TYW}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.60 ANGSTROMS) OF 90-121, AND DISULFIDE
RP BONDS.
RX PubMed=35324283; DOI=10.1126/science.abm9609;
RA Cao J., Belousoff M.J., Liang Y.L., Johnson R.M., Josephs T.M.,
RA Fletcher M.M., Christopoulos A., Hay D.L., Danev R., Wootten D.,
RA Sexton P.M.;
RT "A structural basis for amylin receptor phenotype.";
RL Science 375:eabm9609-eabm9609(2022).
RN [5] {ECO:0000313|RefSeq:NP_001135058.1, ECO:0000313|RefSeq:XP_014031410.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014031410.1};
RG RefSeq;
RL Submitted (NOV-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 EMBL; BT050236; ACI70037.1; -; mRNA.
DR RefSeq; NP_001135058.1; NM_001141586.1.
DR RefSeq; XP_014031410.1; XM_014175935.1.
DR PDB; 7TYN; EM; 2.60 A; P=90-121.
DR PDB; 7TYW; EM; 3.00 A; P=90-121.
DR PDB; 7TYY; EM; 3.00 A; P=90-121.
DR EMDB; EMD-26188; -.
DR EMDB; EMD-26199; -.
DR STRING; 8030.ENSSSAP00000050160; -.
DR Allergome; 9878; Sal s Calcitonin.
DR PaxDb; 8030-ENSSSAP00000050160; -.
DR GeneID; 100196557; -.
DR KEGG; sasa:100196557; -.
DR KEGG; sasa:106587496; -.
DR CTD; 100196557; -.
DR OMA; MEETNEG; -.
DR OrthoDB; 4002581at2759; -.
DR Proteomes; UP000087266; Chromosome ssa26.
DR Bgee; ENSSSAG00000050076; Expressed in liver and 7 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR InterPro; IPR021118; Calcitonin.
DR InterPro; IPR021117; Calcitonin-like.
DR InterPro; IPR021116; Calcitonin/adrenomedullin.
DR InterPro; IPR018360; Calcitonin_CS.
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; PR00270; CALCITONINA.
DR SMART; SM00113; CALCITONIN; 1.
DR PROSITE; PS00258; CALCITONIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7TYN, ECO:0007829|PDB:7TYW};
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:UP000087266};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..143
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001135058.1"
FT /id="PRO_5009732247"
FT DOMAIN 88..125
FT /note="Calcitonin peptide-like"
FT /evidence="ECO:0000259|SMART:SM00113"
FT REGION 109..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 90..96
FT /evidence="ECO:0000256|PIRSR:PIRSR621116-50,
FT ECO:0007829|PDB:7TYN"
SQ SEQUENCE 143 AA; 15921 MW; A8E4484E3259AF6F CRC64;
MCFTAGTMVM MKLSALLIAY FLVICQMYSS HAAPTRTGLE SMTDQVTLTD YEARRLLNAI
VKEFVQMTSE ELEQQANEGN SLDRPMSKRC SNLSTCVLGK LSQELHKLQT YPRTNTGSGT
PGKKRSLPES NRYASYGDSY DGI
//
