ID A0A3Q2ZZ26_KRYMA Unreviewed; 281 AA.
AC A0A3Q2ZZ26;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 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:ENSKMAP00000008660.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000008660.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_017272642.1; XM_017417153.1.
DR AlphaFoldDB; A0A3Q2ZZ26; -.
DR STRING; 37003.ENSKMAP00000008660; -.
DR Ensembl; ENSKMAT00000008792.1; ENSKMAP00000008660.1; ENSKMAG00000006496.1.
DR GeneID; 108236486; -.
DR KEGG; kmr:108236486; -.
DR CTD; 6781; -.
DR GeneTree; ENSGT00390000005989; -.
DR OMA; CAERTMP; -.
DR OrthoDB; 4573585at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR InterPro; IPR004978; Stanniocalcin.
DR PANTHER; PTHR11245; STANNIOCALCIN; 1.
DR PANTHER; PTHR11245:SF1; STANNIOCALCIN-1; 1.
DR Pfam; PF03298; Stanniocalcin; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU369112};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hormone {ECO:0000256|ARBA:ARBA00022702};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU369112};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..281
FT /note="Stanniocalcin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018529800"
FT REGION 257..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 30833 MW; FC5BF1F60A27C777 CRC64;
MNPSQSRKCL CASSGCVSSC AERTMLWRTG LFLLMVLNAS AYELDQNESH SPRRARFSVN
SPSDVARCLN SALQVGCGAF ACLENSTCDT DGLHDICKSF LYSAAKFDTQ GKAFVKESLK
CIANGITSKA FSTIRRCSTF QRMITEVQEE CYSKLDICTV AQSNPDAIGE VAQLPSHFPN
RFYGKLLQSL MDCDEDTVDR IRTSMVSRLG PEMTMLIQLL QNKPCPSTAV AAVAAAIPTG
VEARGSWRWS TGPNMYKIQP NLRNRDPATH LGKKRSASDN S
//
