STC_ANGAU
ID STC_ANGAU Reviewed; 250 AA.
AC P18301;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Stanniocalcin;
DE Short=STC;
DE AltName: Full=Corpuscles of Stannius protein;
DE Short=CS;
DE AltName: Full=Hypocalcin;
DE AltName: Full=Teleocalcin;
DE Flags: Precursor;
GN Name=stc;
OS Anguilla australis (Australian eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 33-57.
RX PubMed=3319739; DOI=10.1016/0303-7207(87)90149-3;
RA Butkus A., Roche P.J., Fernley R.T., Haralambidis J., Penschow J.D.,
RA Ryan G.B., Trahair J.F., Tregear G.W., Coghlan J.P.;
RT "Purification and cloning of a corpuscles of Stannius protein from Anguilla
RT australis.";
RL Mol. Cell. Endocrinol. 54:123-133(1987).
RN [2]
RP SEQUENCE REVISION.
RA Roche P.J.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- TISSUE SPECIFICITY: Corpuscles of Stannius.
CC -!- SIMILARITY: Belongs to the stanniocalcin family. {ECO:0000305}.
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DR EMBL; M36967; AAB91483.1; -; mRNA.
DR PIR; A54648; A54648.
DR AlphaFoldDB; P18301; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR InterPro; IPR004978; Stanniocalcin.
DR PANTHER; PTHR11245; PTHR11245; 1.
DR Pfam; PF03298; Stanniocalcin; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..32
FT /evidence="ECO:0000255"
FT /id="PRO_0000033308"
FT CHAIN 33..250
FT /note="Stanniocalcin"
FT /id="PRO_0000033309"
FT REGION 228..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 44..58
FT /evidence="ECO:0000250"
FT DISULFID 53..73
FT /evidence="ECO:0000250"
FT DISULFID 64..113
FT /evidence="ECO:0000250"
FT DISULFID 97..127
FT /evidence="ECO:0000250"
FT DISULFID 134..169
FT /evidence="ECO:0000250"
FT DISULFID 201
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 250 AA; 27174 MW; BB972BD951F75B3E CRC64;
MLRMSGLILT LVLVTAAYEQ DESEPLSPRT ARFSASSPSD VARCLNGALQ VGCSAFACLD
NSTCNTDGMH EICRSFLHGA AKFDTQGKTF VKESLKCIAN GITSKVFLTI RRCSSFQKMI
SEVQEECYSK LDLCSVAQSN PEAMGEVAQV PSQFPNRYYS TLLQSLLTCD EDTVEQVRAG
LVSRLEPEMG VLFQLLQTKA CPPSAAGGTG PVGAGGSWRW PMGPPMFKIQ PNLRSRDPTH
LFAKKRSTSS