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Database: UniProt
Entry: A0A3Q3MAP0_9TELE
LinkDB: A0A3Q3MAP0_9TELE
Original site: A0A3Q3MAP0_9TELE 
ID   A0A3Q3MAP0_9TELE        Unreviewed;       285 AA.
AC   A0A3Q3MAP0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Stanniocalcin {ECO:0000256|ARBA:ARBA00017831, ECO:0000256|RuleBase:RU369112};
DE            Short=STC {ECO:0000256|RuleBase:RU369112};
DE   AltName: Full=Corpuscles of Stannius protein {ECO:0000256|RuleBase:RU369112};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000018059.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000018059.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Has an anti-hypocalcemic action on calcium and phosphate
CC       homeostasis. {ECO:0000256|ARBA:ARBA00037055}.
CC   -!- FUNCTION: Its primary function is the prevention of hypercalcemia. Upon
CC       release into the circulation, it lowers calcium transport by the gills,
CC       thereby reducing its rate of influx from the environment into the
CC       extracellular compartment. STC also stimulates phosphate reabsorption
CC       by renal proximal tubules. The consequence of this action is increased
CC       levels of plasma phosphate, which combines with excess calcium and
CC       promotes its disposal into bone and scales.
CC       {ECO:0000256|ARBA:ARBA00003962, ECO:0000256|RuleBase:RU369112}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748,
CC       ECO:0000256|RuleBase:RU369112}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU369112}.
CC   -!- SIMILARITY: Belongs to the stanniocalcin family.
CC       {ECO:0000256|ARBA:ARBA00008693, ECO:0000256|RuleBase:RU369112}.
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DR   AlphaFoldDB; A0A3Q3MAP0; -.
DR   Ensembl; ENSMAMT00000018533.2; ENSMAMP00000018059.1; ENSMAMG00000012202.2.
DR   GeneTree; ENSGT00390000005989; -.
DR   InParanoid; A0A3Q3MAP0; -.
DR   OrthoDB; 4573585at2759; -.
DR   Proteomes; UP000261640; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   InterPro; IPR004978; Stanniocalcin.
DR   PANTHER; PTHR11245; STANNIOCALCIN; 1.
DR   PANTHER; PTHR11245:SF2; STANNIOCALCIN-2; 1.
DR   Pfam; PF03298; Stanniocalcin; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|RuleBase:RU369112};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW   Secreted {ECO:0000256|RuleBase:RU369112}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..285
FT                   /note="Stanniocalcin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018733671"
FT   REGION          212..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   285 AA;  31491 MW;  D16457376215BA98 CRC64;
     MLVKLAVALL VLSVLEQVVG SDNIDIHDSP PEKPVSQKGR LSLQNTAEIQ HCLVSAGDVG
     CGVFECFENN SCEIRGLQEI CMTFLHNAGK FDSQGKSFIK DALKCMAHGL RHKFSCISRK
     CVSIKEMVFQ LQRECYIKHN LCSAAKENVA VMVEMIHFQD LFPKGPYVEL VNILLSCGEE
     VKEALTRSVR LQCEQNWGAL CDSLSLCSSL APSPAGSAGE HHRHPSPSHP SPEHPRPPRQ
     GDKDKAGKAG FNPHPRNRSQ GLRRQSPEAR VVAEQENPEA PDIRR
//
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