ID STC1_HUMAN Reviewed; 247 AA.
AC P52823; B4DN22; Q71UE5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=Stanniocalcin-1;
DE Short=STC-1;
DE Flags: Precursor;
GN Name=STC1; Synonyms=STC;
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] (ISOFORM 1).
RC TISSUE=Fibrosarcoma, and Lung carcinoma;
RX PubMed=7489828; DOI=10.1016/0303-7207(95)03601-3;
RA Chang A.C.-M., Janosi J., Hulsbeek M., de Jong D., Jeffrey K.J.,
RA Noble J.R., Reddel R.R.;
RT "A novel human cDNA highly homologous to the fish hormone stanniocalcin.";
RL Mol. Cell. Endocrinol. 112:241-247(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal lung;
RX PubMed=8700837; DOI=10.1073/pnas.93.5.1792;
RA Olsen H.S., Cepeda M.A., Zhang Q.-Q., Rosen C.A., Vozzolo B.L.,
RA Wagner G.F.;
RT "Human stanniocalcin: a possible hormonal regulator of mineral
RT metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1792-1796(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jeffrey K.J., Reddel R.R.;
RT "Characterization of the human stanniocalcin 1 gene.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, Kidney, and Stomach;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157.
RX PubMed=9794484; DOI=10.1210/endo.139.11.6313;
RA Varghese R., Wong C.K., Deol H., Wagner G.F., DiMattia G.E.;
RT "Comparative analysis of mammalian stanniocalcin genes.";
RL Endocrinology 139:4714-4725(1998).
RN [8]
RP PROTEIN SEQUENCE OF 18-32.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
CC -!- FUNCTION: Stimulates renal phosphate reabsorption, and could therefore
CC prevent hypercalcemia.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- INTERACTION:
CC P52823; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12268818, EBI-16439278;
CC P52823; P52823: STC1; NbExp=2; IntAct=EBI-12268818, EBI-12268818;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P52823-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52823-2; Sequence=VSP_057169;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, with the highest levels
CC in ovary, prostate, heart, kidney and thyroid. In the kidney,
CC expression is confined to the nephron, specifically in the distal
CC convoluted tubule and in the collecting tubule. Not detected in the
CC brain, liver, spleen, peripheral blood leukocytes and adrenal medulla.
CC -!- SIMILARITY: Belongs to the stanniocalcin family. {ECO:0000305}.
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DR EMBL; U25997; AAC09472.1; -; mRNA.
DR EMBL; U46768; AAA88903.1; -; mRNA.
DR EMBL; AF242179; AAL79522.1; -; Genomic_DNA.
DR EMBL; AK297734; BAG60084.1; -; mRNA.
DR EMBL; AC012119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029044; AAH29044.1; -; mRNA.
DR EMBL; AF098463; AAC97949.1; -; Genomic_DNA.
DR CCDS; CCDS6043.1; -. [P52823-1]
DR RefSeq; NP_003146.1; NM_003155.2. [P52823-1]
DR AlphaFoldDB; P52823; -.
DR SMR; P52823; -.
DR BioGRID; 112658; 2.
DR IntAct; P52823; 2.
DR STRING; 9606.ENSP00000290271; -.
DR BindingDB; P52823; -.
DR ChEMBL; CHEMBL4879441; -.
DR GlyCosmos; P52823; 1 site, No reported glycans.
DR GlyGen; P52823; 4 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P52823; -.
DR PhosphoSitePlus; P52823; -.
DR BioMuta; STC1; -.
DR DMDM; 1706175; -.
DR EPD; P52823; -.
DR jPOST; P52823; -.
DR MassIVE; P52823; -.
DR MaxQB; P52823; -.
DR PaxDb; 9606-ENSP00000290271; -.
DR PeptideAtlas; P52823; -.
DR ProteomicsDB; 4664; -.
DR ProteomicsDB; 56541; -. [P52823-1]
DR Antibodypedia; 9801; 462 antibodies from 37 providers.
DR DNASU; 6781; -.
DR Ensembl; ENST00000290271.7; ENSP00000290271.2; ENSG00000159167.12. [P52823-1]
DR Ensembl; ENST00000524323.1; ENSP00000427932.1; ENSG00000159167.12. [P52823-2]
DR GeneID; 6781; -.
DR KEGG; hsa:6781; -.
DR MANE-Select; ENST00000290271.7; ENSP00000290271.2; NM_003155.3; NP_003146.1.
DR UCSC; uc003xdw.2; human. [P52823-1]
DR AGR; HGNC:11373; -.
DR CTD; 6781; -.
DR DisGeNET; 6781; -.
DR GeneCards; STC1; -.
DR HGNC; HGNC:11373; STC1.
DR HPA; ENSG00000159167; Low tissue specificity.
DR MIM; 601185; gene.
DR neXtProt; NX_P52823; -.
DR OpenTargets; ENSG00000159167; -.
DR PharmGKB; PA36190; -.
DR VEuPathDB; HostDB:ENSG00000159167; -.
DR eggNOG; ENOG502QU7E; Eukaryota.
DR GeneTree; ENSGT00390000005989; -.
DR HOGENOM; CLU_064102_1_1_1; -.
DR InParanoid; P52823; -.
DR OMA; CAERTMP; -.
DR OrthoDB; 4573585at2759; -.
DR PhylomeDB; P52823; -.
DR TreeFam; TF324693; -.
DR PathwayCommons; P52823; -.
DR SignaLink; P52823; -.
DR BioGRID-ORCS; 6781; 11 hits in 1151 CRISPR screens.
DR ChiTaRS; STC1; human.
DR GeneWiki; STC1; -.
DR GenomeRNAi; 6781; -.
DR Pharos; P52823; Tchem.
DR PRO; PR:P52823; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P52823; Protein.
DR Bgee; ENSG00000159167; Expressed in pericardium and 157 other cell types or tissues.
DR ExpressionAtlas; P52823; baseline and differential.
DR Genevisible; P52823; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060348; P:bone development; IDA:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0035988; P:chondrocyte proliferation; IDA:UniProtKB.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IDA:UniProtKB.
DR GO; GO:0003421; P:growth plate cartilage axis specification; IDA:UniProtKB.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IDA:UniProtKB.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:1903403; P:negative regulation of renal phosphate excretion; IDA:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IDA:UniProtKB.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IDA:UniProtKB.
DR GO; GO:0044070; P:regulation of monoatomic anion transport; IDA:UniProtKB.
DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR InterPro; IPR004978; Stanniocalcin.
DR PANTHER; PTHR11245; STANNIOCALCIN; 1.
DR PANTHER; PTHR11245:SF1; STANNIOCALCIN-1; 1.
DR Pfam; PF03298; Stanniocalcin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:15340161"
FT PROPEP 18..33
FT /evidence="ECO:0000255"
FT /id="PRO_0000033297"
FT CHAIN 34..247
FT /note="Stanniocalcin-1"
FT /id="PRO_0000033298"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..59
FT /evidence="ECO:0000250"
FT DISULFID 54..74
FT /evidence="ECO:0000250"
FT DISULFID 65..114
FT /evidence="ECO:0000250"
FT DISULFID 98..128
FT /evidence="ECO:0000250"
FT DISULFID 135..170
FT /evidence="ECO:0000250"
FT DISULFID 202
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057169"
SQ SEQUENCE 247 AA; 27621 MW; 1E4A8BD861B49AED CRC64;
MLQNSAVLLV LVISASATHE AEQNDSVSPR KSRVAAQNSA EVVRCLNSAL QVGCGAFACL
ENSTCDTDGM YDICKSFLYS AAKFDTQGKA FVKESLKCIA NGVTSKVFLA IRRCSTFQRM
IAEVQEECYS KLNVCSIAKR NPEAITEVVQ LPNHFSNRYY NRLVRSLLEC DEDTVSTIRD
SLMEKIGPNM ASLFHILQTD HCAQTHPRAD FNRRRTNEPQ KLKVLLRNLR GEEDSPSHIK
RTSHESA
//
