ID   CALC_HUMAN              Reviewed;         141 AA.
AC   P01258; B7ZL39; Q13935; Q13937; Q52LX7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 3.
DT   04-NOV-2026, entry version 223.
DE   RecName: Full=Calcitonin {ECO:0000303|PubMed:6546550};
DE   Contains:
DE     RecName: Full=Calcitonin {ECO:0000303|PubMed:6546550};
DE              Short=CT {ECO:0000303|PubMed:6546550};
DE   Contains:
DE     RecName: Full=Katacalcin {ECO:0000303|PubMed:6132180};
DE     AltName: Full=Calcitonin carboxyl-terminal peptide;
DE              Short=CCP;
DE     AltName: Full=PDN-21;
DE   Flags: Precursor;
GN   Name=CALCA {ECO:0000312|HGNC:HGNC:1437}; Synonyms=CALC1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=6546550; DOI=10.1016/0014-5793(84)80839-x;
RA   le Moullec J.-M., Jullienne A., Chenais J., Lasmoles F., Guliana J.M.,
RA   Milhaud G., Moukhtar M.S.;
RT   "The complete sequence of human preprocalcitonin.";
RL   FEBS Lett. 167:93-97(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3872459; DOI=10.1073/pnas.82.7.1994;
RA   Jonas V., Lin C.R., Kawashima E., Semon D., Swanson L.W., Mermod J.-J.,
RA   Evans R.M., Rosenfeld M.G.;
RT   "Alternative RNA processing events in human calcitonin/calcitonin gene-
RT   related peptide gene expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:1994-1998(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3034287;
RA   Craig R.K., Riley J.H., Edbrooke M.R., Broad P.M., Foord S.M.,
RA   Al-Kazwini S.J., Holman J.J., Marshall I.;
RT   "Expression and function of the human calcitonin/alpha-CGRP gene in health
RT   and disease.";
RL   Biochem. Soc. Symp. 52:91-105(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3485540; DOI=10.1016/0014-5793(86)81187-5;
RA   Riley J.H., Edbrooke M.R., Craig R.K.;
RT   "Ectopic synthesis of high-Mr calcitonin by the BEN lung carcinoma cell
RT   line reflects aberrant proteolytic processing.";
RL   FEBS Lett. 198:71-79(1986).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Thyroid carcinoma;
RX   PubMed=1761559; DOI=10.1016/s0021-9258(18)54275-7;
RA   Minvielle S., Giscard-Dartevelle S., Cohen R., Taboulet J., Labye F.,
RA   Jullienne A., Rivaille P., Milhaud G., Moukhtar M.S., Lasmoles F.;
RT   "A novel calcitonin carboxyl-terminal peptide produced in medullary thyroid
RT   carcinoma by alternative RNA processing of the calcitonin/calcitonin gene-
RT   related peptide gene.";
RL   J. Biol. Chem. 266:24627-24631(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-2; LYS-67; ARG-76;
RP   THR-123 AND PRO-138.
RG   NIEHS SNPs program;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 48-83 (ISOFORM 1).
RX   PubMed=6148938; DOI=10.1016/0006-291x(84)90278-x;
RA   Nelkin B.D., Rosenfeld K.I., de Bustros A., Leong S.S., Roos B.A.,
RA   Baylin S.B.;
RT   "Structure and expression of a gene encoding human calcitonin and
RT   calcitonin gene related peptide.";
RL   Biochem. Biophys. Res. Commun. 123:648-655(1984).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 50-141 (ISOFORM 1).
RX   PubMed=2408883; DOI=10.1002/j.1460-2075.1985.tb03688.x;
RA   Edbrooke M.R., Parker D., McVey J.H., Riley J.H., Sorenson G.D.,
RA   Pettengill O.S., Craig R.K.;
RT   "Expression of the human calcitonin/CGRP gene in lung and thyroid
RT   carcinoma.";
RL   EMBO J. 4:715-724(1985).
RN   [12]
RP   PROTEIN SEQUENCE OF 85-116, AND AMIDATION AT PRO-116.
RX   PubMed=5760861; DOI=10.1002/hlca.19680510811;
RA   Neher R., Riniker B., Rittel W., Zuber H.;
RT   "Human calcitonin. Structure of calcitonin M and D.";
RL   Helv. Chim. Acta 51:1900-1905(1968).
RN   [13]
RP   STRUCTURE BY NMR OF CALCITONIN.
RX   PubMed=2001366; DOI=10.1021/bi00223a010;
RA   Motta A., Temussi P.A., Wunsch E., Bovermann G.;
RT   "A 1H NMR study of human calcitonin in solution.";
RL   Biochemistry 30:2364-2371(1991).
RN   [14]
RP   FUNCTION (CALCITONIN).
RX   PubMed=7057295; DOI=10.1002/path.1711360104;
RA   Chambers T.J., Magnus C.J.;
RT   "Calcitonin alters behaviour of isolated osteoclasts.";
RL   J. Pathol. 136:27-39(1982).
RN   [15]
RP   FUNCTION, AND CHARACTERIZATION OF KATACALCIN.
RX   PubMed=6132180; DOI=10.1016/s0140-6736(83)91387-9;
RA   Hillyard C.J., Myers C., Abeyasekera G., Stevvensvenson J.C., Craig R.K.,
RA   MacIntyre I.;
RT   "Katacalcin: a new plasma calcium-lowering hormone.";
RL   Lancet 1:846-848(1983).
RN   [16]
RP   FUNCTION (KATACALCIN), AND SUBCELLULAR LOCATION (KATACALCIN).
RX   PubMed=3350911; DOI=10.1210/jcem-66-3-640;
RA   Hurley D.L., Katz H.H., Tiegs R.D., Calvo M.S., Barta J.R., Heath H. III;
RT   "Cosecretion of calcitonin gene products: studies with a C18 cartridge
RT   extraction method for human plasma PDN-21 (katacalcin).";
RL   J. Clin. Endocrinol. Metab. 66:640-644(1988).
RN   [17]
RP   FUNCTION (KATACALCIN).
RX   PubMed=12369791; DOI=10.1359/jbmr.2002.17.10.1872;
RA   Kaneider N.C., Egger P., Wiedermann F.J., Ritter M., Woell E.,
RA   Wiedermann C.J.;
RT   "Involvement of cyclic adenosine monophosphate-dependent protein kinase A
RT   and pertussis toxin-sensitive G proteins in the migratory response of human
RT   CD14+ mononuclear cells to katacalcin.";
RL   J. Bone Miner. Res. 17:1872-1882(2002).
RN   [18]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:R8.1-R8.16(2004).
RN   [19]
RP   FUNCTION (CALCITONIN).
RX   PubMed=17535751;
RA   Yamamoto Y., Yamamoto Y., Udagawa N., Okumura S., Mizoguchi T., Take I.,
RA   Yamauchi H., Yamauchi H., Noguchi T., Takahashi N.;
RT   "Effects of calcitonin on the function of human osteoclast-like cells
RT   formed from CD14-positive monocytes.";
RL   Cell. Mol. Biol. 52:25-31(2006).
RN   [20] {ECO:0007744|PDB:7TYH, ECO:0007744|PDB:7TYO}
RP   STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH CALCR; RAMP2 AND G
RP   PROTEINS, DISULFIDE BOND, AND FUNCTION.
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 375:0-0(2022).
CC   -!- FUNCTION: [Calcitonin]: Peptide hormone secreted by thyroid
CC       parafollicular (C) cells that acts as a high-affinity agonist of the
CC       calcitonin receptor/CALCR that primarily couples to Gs/adenylate
CC       cyclase signaling, resulting in activation of cAMP-dependent pathways,
CC       and can additionally mobilize intracellular calcium and activate ERK
CC       signaling (PubMed:35324283). Acutely lowers blood calcium levels
CC       predominantly by inhibiting osteoclast-mediated bone resorption
CC       (PubMed:7057295, PubMed:17535751). In osteoclasts, receptor activation
CC       rapidly induces loss of the ruffled border, cytoplasmic retraction, and
CC       suppression of cell motility and resorptive activity (PubMed:7057295,
CC       PubMed:17535751). Functions to restrain bone remodeling and turnover,
CC       protect the maternal skeleton during periods of calcium stress such as
CC       lactation, and limit induced hypercalcemia, while playing only a minor
CC       role in basal calcium homeostasis (By similarity).
CC       {ECO:0000250|UniProtKB:P70160, ECO:0000269|PubMed:17535751,
CC       ECO:0000269|PubMed:35324283}.
CC   -!- FUNCTION: [Katacalcin]: Peptide cleaved from the C-terminal region of
CC       the calcitonin precursor and co-secreted with calcitonin from thyroid
CC       parafollicular (C) cells in approximately equimolar amounts
CC       (PubMed:3350911). May stimulates the migration of CD14(+) peripheral
CC       blood monocytes through a cAMP/PKA protein-dependent pathway
CC       (PubMed:12369791). {ECO:0000269|PubMed:12369791,
CC       ECO:0000269|PubMed:3350911}.
CC   -!- FUNCTION: [Katacalcin]: Katacalcin is a potent plasma calcium-lowering
CC       peptide. {ECO:0000269|PubMed:6132180}.
CC   -!- INTERACTION:
CC       P01258; X5D778: ANKRD11; NbExp=3; IntAct=EBI-1018474, EBI-17183751;
CC       P01258; Q01814: ATP2B2; NbExp=2; IntAct=EBI-1018474, EBI-1174243;
CC       P01258; P23634: ATP2B4; NbExp=2; IntAct=EBI-1018474, EBI-1174388;
CC       P01258; P01258: CALCA; NbExp=3; IntAct=EBI-1018474, EBI-1018474;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P01258-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P01258-2; Sequence=VSP_000709;
CC       Name=3;
CC         IsoId=P06881-1; Sequence=External;
CC   -!- MISCELLANEOUS: The CALCA gene (HGNC:1437) encodes a small family of
CC       peptides including calcitonin (UniProtKB:P01258), its C-terminal
CC       flanking peptide katacalcin (UniProtKB:P01258) and the calcitonin gene-
CC       related peptide/CGRP1 (UniProtKB:P06881). {ECO:0000269|PubMed:3872459,
CC       ECO:0000269|PubMed:6148938}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305|PubMed:14759258}.
CC   -!- SIMILARITY: Belongs to the calcitonin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Calcitonin entry;
CC       URL="https://en.wikipedia.org/wiki/Calcitonin";
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DR   EMBL; X00356; CAA25103.1; -; mRNA.
DR   EMBL; M12666; AAA51913.1; -; Genomic_DNA.
DR   EMBL; M12664; AAA51913.1; JOINED; Genomic_DNA.
DR   EMBL; M12665; AAA51913.1; JOINED; Genomic_DNA.
DR   EMBL; M26095; AAA35501.1; -; mRNA.
DR   EMBL; X03662; CAA27299.1; -; mRNA.
DR   EMBL; M64486; AAA58403.1; -; mRNA.
DR   EMBL; DQ080435; AAY68212.1; -; Genomic_DNA.
DR   EMBL; AC090835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471064; EAW68468.1; -; Genomic_DNA.
DR   EMBL; BC069684; AAH69684.1; -; mRNA.
DR   EMBL; BC069704; AAH69704.1; -; mRNA.
DR   EMBL; BC069760; AAH69760.1; -; mRNA.
DR   EMBL; BC069778; AAH69778.1; -; mRNA.
DR   EMBL; BC093753; AAH93753.1; -; mRNA.
DR   EMBL; BC101599; AAI01600.1; -; mRNA.
DR   EMBL; BC143562; AAI43563.1; -; mRNA.
DR   EMBL; K03513; AAA52124.1; -; mRNA.
DR   EMBL; X02330; CAA26189.1; -; mRNA.
DR   CCDS; CCDS7819.1; -. [P01258-1]
DR   PIR; A41716; A41716.
DR   PIR; S07643; TCHU.
DR   RefSeq; NP_001029124.1; NM_001033952.3. [P01258-1]
DR   RefSeq; NP_001365878.1; NM_001378949.1. [P01258-1]
DR   RefSeq; NP_001732.1; NM_001741.3. [P01258-1]
DR   RefSeq; XP_054225903.1; XM_054369928.1. [P01258-1]
DR   RefSeq; XP_054225904.1; XM_054369929.1. [P01258-1]
DR   PDB; 2JXZ; NMR; -; A=85-116.
DR   PDB; 7TYH; EM; 3.30 A; P=85-116.
DR   PDB; 7TYO; EM; 2.70 A; P=85-116.
DR   AlphaFoldDB; P01258; -.
DR   BMRB; P01258; -.
DR   EMDB; EMD-26179; -.
DR   EMDB; EMD-26190; -.
DR   SMR; P01258; -.
DR   BioGRID; 107247; 18.
DR   FunCoup; P01258; 782.
DR   IntAct; P01258; 11.
DR   NDEx; IQUERY-CP-CALCA; 6 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000331746; -.
DR   GlyCosmos; P01258; 3 sites, 1 glycan.
DR   GlyGen; P01258; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P01258; -.
DR   MetOSite; P01258; -.
DR   PhosphoSitePlus; P01258; -.
DR   BioMuta; CALCA; -.
DR   DMDM; 322510018; -.
DR   MassIVE; P01258; -.
DR   PaxDb; 9606-ENSP00000331746; -.
DR   PeptideAtlas; P01258; -.
DR   ProteomicsDB; 51362; -. [P01258-1]
DR   ProteomicsDB; 51363; -. [P01258-2]
DR   TopDownProteomics; P01258-1; -. [P01258-1]
DR   ABCD; P01258; 3 sequenced antibodies.
DR   Antibodypedia; 3493; 2002 antibodies from 56 providers.
DR   DNASU; 796; -.
DR   Ensembl; ENST00000331587.9; ENSP00000331746.4; ENSG00000110680.14. [P01258-1]
DR   Ensembl; ENST00000396372.2; ENSP00000379657.2; ENSG00000110680.14. [P01258-1]
DR   Ensembl; ENST00000469608.5; ENSP00000420618.1; ENSG00000110680.14. [P01258-2]
DR   GeneID; 796; -.
DR   KEGG; hsa:796; -.
DR   MANE-Select; ENST00000331587.9; ENSP00000331746.4; NM_001741.3; NP_001732.1.
DR   UCSC; uc001mlv.2; human. [P01258-1]
DR   AGR; HGNC:1437; -.
DR   ClinPGx; PA26029; -.
DR   CTD; 796; -.
DR   DisGeNET; 796; -.
DR   GeneCards; CALCA; -.
DR   HGNC; HGNC:1437; CALCA.
DR   HPA; ENSG00000110680; Group enriched (parathyroid gland, thyroid gland).
DR   MalaCards; CALCA; -.
DR   MIM; 114130; gene.
DR   OpenTargets; ENSG00000110680; -.
DR   VEuPathDB; HostDB:ENSG00000110680; -.
DR   eggNOG; ENOG502RZI5; Eukaryota.
DR   GeneTree; ENSGT00940000162876; -.
DR   HOGENOM; CLU_122444_0_0_1; -.
DR   InParanoid; P01258; -.
DR   OrthoDB; 9929923at2759; -.
DR   PAN-GO; P01258; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; P01258; -.
DR   PathwayCommons; P01258; -.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-419812; Calcitonin-like ligand receptors.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   SignaLink; P01258; -.
DR   Agora; ENSG00000110680; -.
DR   BioGRID-ORCS; 796; 15 hits in 1146 CRISPR screens.
DR   ChiTaRS; CALCA; human.
DR   EvolutionaryTrace; P01258; -.
DR   GeneWiki; Calcitonin; -.
DR   GenomeRNAi; 796; -.
DR   Pharos; P01258; Tbio.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P01258; protein.
DR   Bgee; ENSG00000110680; Expressed in dorsal root ganglion and 124 other cell types or tissues.
DR   ExpressionAtlas; P01258; baseline and differential.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0031716; F:calcitonin receptor binding; IPI:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IDA:UniProt.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0150060; P:amylin receptor 2 signaling pathway; IDA:UniProt.
DR   GO; GO:0097646; P:calcitonin family receptor signaling pathway; IDA:UniProt.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IDA:UniProtKB.
DR   GO; GO:0002548; P:monocyte chemotaxis; IDA:BHF-UCL.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0045779; P:negative regulation of bone resorption; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045986; P:negative regulation of smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0042311; P:vasodilation; IEA:Ensembl.
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; Alternative splicing; Amidation;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hormone; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..82
FT                   /id="PRO_0000004050"
FT   PEPTIDE         85..116
FT                   /note="Calcitonin"
FT                   /evidence="ECO:0000269|PubMed:5760861"
FT                   /id="PRO_0000004051"
FT   PEPTIDE         121..141
FT                   /note="Katacalcin"
FT                   /id="PRO_0000004052"
FT   REGION          64..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01257"
FT   MOD_RES         116
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:5760861"
FT   DISULFID        85..91
FT                   /evidence="ECO:0000269|PubMed:35324283,
FT                   ECO:0000269|PubMed:5760861"
FT   VAR_SEQ         134..141
FT                   /note="VSMPQNAN -> NHCPEESL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1761559"
FT                   /id="VSP_000709"
FT   VARIANT         2
FT                   /note="G -> R (in dbSNP:rs34587547)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_025271"
FT   VARIANT         57
FT                   /note="D -> N (in dbSNP:rs5239)"
FT                   /id="VAR_014592"
FT   VARIANT         67
FT                   /note="E -> K (in dbSNP:rs34164367)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_025272"
FT   VARIANT         76
FT                   /note="S -> R (in dbSNP:rs5241)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_014593"
FT   VARIANT         123
FT                   /note="S -> T (in dbSNP:rs34414857)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_025273"
FT   VARIANT         138
FT                   /note="Q -> P (in dbSNP:rs13306224)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_025274"
FT   CONFLICT        92
FT                   /note="M -> I (in Ref. 2; AAA51913)"
FT                   /evidence="ECO:0000305"
FT   HELIX           92..101
FT                   /evidence="ECO:0007829|PDB:7TYO"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:7TYO"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:7TYH"
SQ   SEQUENCE   141 AA;  15467 MW;  99622305DD8B286F CRC64;
     MGFQKFSPFL ALSILVLLQA GSLHAAPFRS ALESSPADPA TLSEDEARLL LAALVQDYVQ
     MKASELEQEQ EREGSSLDSP RSKRCGNLST CMLGTYTQDF NKFHTFPQTA IGVGAPGKKR
     DMSSDLERDH RPHVSMPQNA N
//