STC2_HUMAN
ID STC2_HUMAN Reviewed; 302 AA.
AC O76061;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Stanniocalcin-2;
DE Short=STC-2;
DE AltName: Full=Stanniocalcin-related protein;
DE Short=STC-related protein;
DE Short=STCRP;
DE Flags: Precursor;
GN Name=STC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9723890; DOI=10.1016/s0303-7207(98)00097-5;
RA Chang A.C.-M., Reddel R.R.;
RT "Identification of a second stanniocalcin cDNA in mouse and human:
RT stanniocalcin 2.";
RL Mol. Cell. Endocrinol. 141:95-99(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Osteosarcoma;
RX PubMed=9753616; DOI=10.1006/bbrc.1998.9300;
RA Ishiabshi K., Miyamoto K., Taketani Y., Morita K., Takeda E., Sasaki S.,
RA Imai M.;
RT "Molecular cloning of a second human stanniocalcin homologue (STC2).";
RL Biochem. Biophys. Res. Commun. 250:252-258(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10022771; DOI=10.1016/s0303-7207(98)00163-4;
RA DiMattia G.E., Varghese R., Wagner G.F.;
RT "Molecular cloning and characterization of stanniocalcin-related protein.";
RL Mol. Cell. Endocrinol. 146:137-140(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Mammary carcinoma;
RX PubMed=10450831; DOI=10.1055/s-2007-978764;
RA Moore E.E., Kuestner R.E., Conklin D.C., Whitmore T.E., Downey W.,
RA Buddle M.M., Adams R.L., Bell L.A., Thompson D.L., Wolf A., Chen L.,
RA Stamm M.R., Grant F.J., Lok S., Ren H., de Jongh K.S.;
RT "Stanniocalcin 2: characterization of the protein and its localization to
RT human pancreatic alpha cells.";
RL Horm. Metab. Res. 31:406-414(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION AT SER-250; SER-251 AND THR-254.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
CC -!- FUNCTION: Has an anti-hypocalcemic action on calcium and phosphate
CC homeostasis.
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues including muscle,
CC heart, pancreas, kidney, spleen, prostate, small intestine, colon and
CC peripheral blood leukocytes.
CC -!- SIMILARITY: Belongs to the stanniocalcin family. {ECO:0000305}.
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DR EMBL; AF055460; AAC27036.1; -; mRNA.
DR EMBL; AB012664; BAA33489.1; -; mRNA.
DR EMBL; AF098462; AAC97948.1; -; mRNA.
DR EMBL; AF031036; AAD01922.1; -; mRNA.
DR EMBL; BT019591; AAV38398.1; -; mRNA.
DR EMBL; BC000658; AAH00658.1; -; mRNA.
DR EMBL; BC006352; AAH06352.1; -; mRNA.
DR EMBL; BC013958; AAH13958.1; -; mRNA.
DR CCDS; CCDS4388.1; -.
DR PIR; JE0357; JE0357.
DR RefSeq; NP_003705.1; NM_003714.2.
DR AlphaFoldDB; O76061; -.
DR BioGRID; 114172; 48.
DR IntAct; O76061; 16.
DR STRING; 9606.ENSP00000265087; -.
DR GlyConnect; 1769; 5 N-Linked glycans (1 site).
DR GlyGen; O76061; 3 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; O76061; -.
DR PhosphoSitePlus; O76061; -.
DR BioMuta; STC2; -.
DR EPD; O76061; -.
DR jPOST; O76061; -.
DR MassIVE; O76061; -.
DR PaxDb; O76061; -.
DR PeptideAtlas; O76061; -.
DR PRIDE; O76061; -.
DR ProteomicsDB; 50367; -.
DR Antibodypedia; 28957; 417 antibodies from 34 providers.
DR DNASU; 8614; -.
DR Ensembl; ENST00000265087.9; ENSP00000265087.4; ENSG00000113739.11.
DR GeneID; 8614; -.
DR KEGG; hsa:8614; -.
DR MANE-Select; ENST00000265087.9; ENSP00000265087.4; NM_003714.3; NP_003705.1.
DR CTD; 8614; -.
DR DisGeNET; 8614; -.
DR GeneCards; STC2; -.
DR HGNC; HGNC:11374; STC2.
DR HPA; ENSG00000113739; Tissue enriched (breast).
DR MIM; 603665; gene.
DR neXtProt; NX_O76061; -.
DR OpenTargets; ENSG00000113739; -.
DR PharmGKB; PA36191; -.
DR VEuPathDB; HostDB:ENSG00000113739; -.
DR eggNOG; ENOG502QU7E; Eukaryota.
DR GeneTree; ENSGT00390000005989; -.
DR HOGENOM; CLU_064102_0_0_1; -.
DR InParanoid; O76061; -.
DR OMA; SNEWEDE; -.
DR OrthoDB; 1195745at2759; -.
DR PhylomeDB; O76061; -.
DR TreeFam; TF324693; -.
DR PathwayCommons; O76061; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; O76061; -.
DR SIGNOR; O76061; -.
DR BioGRID-ORCS; 8614; 10 hits in 1083 CRISPR screens.
DR ChiTaRS; STC2; human.
DR GeneWiki; STC2; -.
DR GenomeRNAi; 8614; -.
DR Pharos; O76061; Tbio.
DR PRO; PR:O76061; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O76061; protein.
DR Bgee; ENSG00000113739; Expressed in stromal cell of endometrium and 120 other tissues.
DR ExpressionAtlas; O76061; baseline and differential.
DR Genevisible; O76061; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0046885; P:regulation of hormone biosynthetic process; IDA:UniProtKB.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR InterPro; IPR004978; Stanniocalcin.
DR PANTHER; PTHR11245; PTHR11245; 1.
DR Pfam; PF03298; Stanniocalcin; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hormone; Phosphoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..302
FT /note="Stanniocalcin-2"
FT /id="PRO_0000033303"
FT REGION 23..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 250
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 251
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 254
FT /note="Phosphothreonine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 302 AA; 33249 MW; 9B90D8911524FA22 CRC64;
MCAERLGQFM TLALVLATFD PARGTDATNP PEGPQDRSSQ QKGRLSLQNT AEIQHCLVNA
GDVGCGVFEC FENNSCEIRG LHGICMTFLH NAGKFDAQGK SFIKDALKCK AHALRHRFGC
ISRKCPAIRE MVSQLQRECY LKHDLCAAAQ ENTRVIVEMI HFKDLLLHEP YVDLVNLLLT
CGEEVKEAIT HSVQVQCEQN WGSLCSILSF CTSAIQKPPT APPERQPQVD RTKLSRAHHG
EAGHHLPEPS SRETGRGAKG ERGSKSHPNA HARGRVGGLG AQGPSGSSEW EDEQSEYSDI
RR
