ID A0A3Q3GB39_9LABR Unreviewed; 286 AA.
AC A0A3Q3GB39;
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:ENSLBEP00000030162.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000030162.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000030162.1}
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; A0A3Q3GB39; -.
DR STRING; 56723.ENSLBEP00000030162; -.
DR Ensembl; ENSLBET00000031567.1; ENSLBEP00000030162.1; ENSLBEG00000022787.1.
DR GeneTree; ENSGT00390000005989; -.
DR InParanoid; A0A3Q3GB39; -.
DR OrthoDB; 4573585at2759; -.
DR Proteomes; UP000261660; 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:UP000261660};
KW Secreted {ECO:0000256|RuleBase:RU369112}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..286
FT /note="Stanniocalcin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018678863"
FT REGION 215..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 31709 MW; 5C1B4BB116C3001C CRC64;
MLVKLAVALL VLSVLEQVVG SDNIDLHDSL PEKPATQKGR LSLQNTAEIQ HCLVSAGDVG
CGVFECFENN SCEIRGLQEI CMTFLHNAGK FDSQGKSFIK DALKCMAHGL RHKFSCISRK
CVSIKEMVFQ LQRECYIKHN LCSAAKENVA VMVEMIHFQD LFPKGPYVEL VNILLSCGEE
VKEALTRSVR LQCEQNWGAL CDSLSLCSSL APSPAGSPVV EHHRRPLPSH PEPEHPRLPR
QGEKEKPAKA GFNAHPRNRS QGPRRQSPEA GIVAEQEDPE ATDIRR
//
