ID   A0A3Q3A1K5_KRYMA        Unreviewed;       269 AA.
AC   A0A3Q3A1K5;
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};
GN   Name=STC2 {ECO:0000313|Ensembl:ENSKMAP00000010103.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000010103.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000010103.1}
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; A0A3Q3A1K5; -.
DR   STRING; 37003.ENSKMAP00000010103; -.
DR   Ensembl; ENSKMAT00000010265.1; ENSKMAP00000010103.1; ENSKMAG00000007593.1.
DR   GeneTree; ENSGT00390000005989; -.
DR   OMA; DWSTDNA; -.
DR   Proteomes; UP000264800; 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:UP000264800};
KW   Secreted {ECO:0000256|RuleBase:RU369112}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..269
FT                   /note="Stanniocalcin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018608418"
FT   REGION          214..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   269 AA;  29555 MW;  0D0C7A6623641632 CRC64;
     MPVTLSSGMF LLLLACHHIL AVDLHDVQEK QGVKKRLSLQ STTEIQSCLV SSGDVGCGTF
     QCFNNNSCEI HGLHHICLTL LHNAGRYDSQ GKSLVKDALR CMALGLRQRF SCVSRRCSAV
     KEMVFSLQRE CYSKHNLCLA LQDHIDTTGS LVQFHLMFPT GPYVELMNFL LKCGDEIRAW
     VGRRLQGQCK QHWGALCGSF ANICPLNQSD VLDDPTTPQP TVARPVTAVE PSLQPTGEAE
     LENKSPVRSI DSATDSGLAV SEHPFVSDS
//