ID A0A5N3XDI0_MUNRE Unreviewed; 142 AA.
AC A0A5N3XDI0;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 02-APR-2025, entry version 17.
DE RecName: Full=Calcitonin {ECO:0000256|ARBA:ARBA00015874};
GN ORFNames=FD755_017638 {ECO:0000313|EMBL:KAB0371229.1};
OS Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9886 {ECO:0000313|EMBL:KAB0371229.1, ECO:0000313|Proteomes:UP000326062};
RN [1] {ECO:0000313|EMBL:KAB0371229.1, ECO:0000313|Proteomes:UP000326062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCam_UCB_Mr {ECO:0000313|EMBL:KAB0371229.1};
RC TISSUE=Fibroblast cell line {ECO:0000313|EMBL:KAB0371229.1};
RA Mudd A.B., Bredeson J.V., Baum R., Hockemeyer D., Rokhsar D.S.;
RT "Discovery of a novel chromosome fission-fusion reversal in muntjac.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcitonin is a peptide hormone that causes a rapid but
CC short-lived drop in the level of calcium and phosphate in blood by
CC promoting the incorporation of those ions in the bones. Calcitonin
CC function is mediated by the calcitonin receptor/CALCR and the CALCR-
CC RAMP2 (AMYR2) receptor complex. {ECO:0000256|ARBA:ARBA00049621}.
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:KAB0371229.1}.
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DR EMBL; VCEB01000013; KAB0371229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N3XDI0; -.
DR Proteomes; UP000326062; Chromosome 13.
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:UniProtKB-KW.
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 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 3: Inferred from homology;
KW Amidation {ECO:0000256|ARBA:ARBA00022815};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR621116-50};
KW Hormone {ECO:0000256|ARBA:ARBA00022702};
KW Reference proteome {ECO:0000313|Proteomes:UP000326062};
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..142
FT /note="Calcitonin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5024313767"
FT DOMAIN 84..121
FT /note="Calcitonin peptide-like"
FT /evidence="ECO:0000259|SMART:SM00113"
FT REGION 62..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 86..92
FT /evidence="ECO:0000256|PIRSR:PIRSR621116-50"
SQ SEQUENCE 142 AA; 15567 MW; E2AE4A6332E91D2D CRC64;
MGFGKSSPFL AFSILVLCQA GSLQATPLRS ALETLPDPGT LSEKEGRLLL AALVKAYVQR
KTNELEQEEE QETEDSSLDG SRAKRCSNLS TCVLSAYWKD LNNYHRFSGM GFGPETPGKK
RDVANGLERD RSSHFGVPQD AN
//
