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   13-FEB-2019, entry version 145.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Sasaki S., 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
RT   protein.";
RL   Mol. Cell. Endocrinol. 146:137-140(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=Mammary carcinoma;
RX   PubMed=10450831;
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
RT   to 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
RT   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
RT   project: 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
RT   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
CC       muscle, heart, pancreas, kidney, spleen, prostate, small
CC       intestine, colon and 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   UniGene; Hs.233160; -.
DR   ProteinModelPortal; O76061; -.
DR   BioGrid; 114172; 21.
DR   IntAct; O76061; 13.
DR   STRING; 9606.ENSP00000265087; -.
DR   GlyConnect; 1769; -.
DR   iPTMnet; O76061; -.
DR   PhosphoSitePlus; O76061; -.
DR   BioMuta; STC2; -.
DR   EPD; O76061; -.
DR   jPOST; O76061; -.
DR   PaxDb; O76061; -.
DR   PeptideAtlas; O76061; -.
DR   PRIDE; O76061; -.
DR   ProteomicsDB; 50367; -.
DR   DNASU; 8614; -.
DR   Ensembl; ENST00000265087; ENSP00000265087; ENSG00000113739.
DR   GeneID; 8614; -.
DR   KEGG; hsa:8614; -.
DR   CTD; 8614; -.
DR   DisGeNET; 8614; -.
DR   EuPathDB; HostDB:ENSG00000113739.10; -.
DR   GeneCards; STC2; -.
DR   HGNC; HGNC:11374; STC2.
DR   HPA; HPA045372; -.
DR   MIM; 603665; gene.
DR   neXtProt; NX_O76061; -.
DR   OpenTargets; ENSG00000113739; -.
DR   PharmGKB; PA36191; -.
DR   eggNOG; ENOG410IIGP; Eukaryota.
DR   eggNOG; ENOG410XT17; LUCA.
DR   GeneTree; ENSGT00390000005989; -.
DR   HOGENOM; HOG000220830; -.
DR   HOVERGEN; HBG001048; -.
DR   InParanoid; O76061; -.
DR   OMA; FCTSAIQ; -.
DR   OrthoDB; 1195745at2759; -.
DR   PhylomeDB; O76061; -.
DR   TreeFam; TF324693; -.
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   ChiTaRS; STC2; human.
DR   GeneWiki; STC2; -.
DR   GenomeRNAi; 8614; -.
DR   PRO; PR:O76061; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000113739; Expressed in 124 organ(s), highest expression level in epithelium of mammary gland.
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; IEA:Ensembl.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
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:0043687; P:post-translational protein modification; TAS:Reactome.
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   Complete proteome; Disulfide bond; Glycoprotein; Hormone;
KW   Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    302       Stanniocalcin-2.
FT                                /FTId=PRO_0000033303.
FT   MOD_RES     250    250       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   MOD_RES     251    251       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   MOD_RES     254    254       Phosphothreonine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   CARBOHYD     73     73       N-linked (GlcNAc...) asparagine.
FT                                {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
//