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Database: UniProt
Entry: A0A3Q1HTW1_ANATE
LinkDB: A0A3Q1HTW1_ANATE
Original site: A0A3Q1HTW1_ANATE 
ID   A0A3Q1HTW1_ANATE        Unreviewed;       126 AA.
AC   A0A3Q1HTW1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Calcitonin/calcitonin-related polypeptide, alpha {ECO:0000313|Ensembl:ENSATEP00000010789.1};
GN   Name=CALCB {ECO:0000313|Ensembl:ENSATEP00000010789.1};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000010789.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000010789.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A3Q1HTW1; -.
DR   STRING; 64144.ENSATEP00000010789; -.
DR   Ensembl; ENSATET00000010973.2; ENSATEP00000010789.1; ENSATEG00000007554.2.
DR   GeneTree; ENSGT00940000156267; -.
DR   InParanoid; A0A3Q1HTW1; -.
DR   OMA; STCVTHR; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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:UP000265040};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..126
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018696451"
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   126 AA;  13867 MW;  33405999C9DC62EE CRC64;
     VIMLKLWTLL LACALIICKI SQAAPSRNSK EFMTDGATRS DDDVQKLLRA IKEFMQITSD
     EQDHQTAEGN RYGNATAQKR SCNTATCVTH RLADFLSRSG GLGHSNFVPT NVGAQAFGRR
     KRHGTV
//
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