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Metalloreductase STEAP3 (EC 1.16.1.-) (Dudulin-2) (Six-transmembrane epithelial antigen of prostate 3) (Tumor suppressor-activated pathway protein 6) (hTSAP6) (pHyde) (hpHyde)

 STEA3_HUMAN             Reviewed;         488 AA.
Q658P3; A8K6E3; Q4VBR2; Q4ZG36; Q53SQ8; Q7Z389; Q86SF6; Q8NEW6;
Q8TDP3; Q8TF03; Q9NVB5;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
25-OCT-2017, entry version 130.
RecName: Full=Metalloreductase STEAP3;
EC=1.16.1.-;
AltName: Full=Dudulin-2;
AltName: Full=Six-transmembrane epithelial antigen of prostate 3;
AltName: Full=Tumor suppressor-activated pathway protein 6;
Short=hTSAP6;
AltName: Full=pHyde;
Short=hpHyde;
Name=STEAP3; Synonyms=TSAP6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION,
AND INTERACTION WITH BNIP3L AND MYT1.
PubMed=12606722; DOI=10.1073/pnas.0530298100;
Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C.,
Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L.,
Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R.,
Telerman A.;
"The p53-inducible TSAP6 gene product regulates apoptosis and the cell
cycle and interacts with Nix and the Myt1 kinase.";
Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=15897894; DOI=10.1038/sj.onc.1208677;
Korkmaz C.G., Korkmaz K.S., Kurys P., Elbi C., Wang L., Klokk T.I.,
Hammarstrom C., Troen G., Svindland A., Hager G.L., Saatcioglu F.;
"Molecular cloning and characterization of STAMP2, an androgen-
regulated six transmembrane protein that is overexpressed in prostate
cancer.";
Oncogene 24:4934-4945(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
PubMed=10969787;
Steiner M.S., Zhang X., Wang Y., Lu Y.;
"Growth inhibition of prostate cancer by an adenovirus expressing a
novel tumor suppressor gene, pHyde.";
Cancer Res. 60:4419-4425(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Serru V., Manivet P., Lenoir C., Eschwege P., Lamblin D.,
Vaubourdolle M., Kellermann O., Loric S.;
"Dudulin 2, a new tumor antigen expressed in various human tumors.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Lu Y., Beheshti B., Squire J.A., Yang X.J.;
"Characterization of a novel apoptosis-inducing gene, hpHyde, that
inhibits prostate cancer cell growth.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon endothelium, and Endometrial adenocarcinoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
LACK OF TUMOR SUPPRESSOR FUNCTION.
PubMed=12866033; DOI=10.1002/ijc.11278;
Porkka K.P., Nupponen N.N., Tammela T.L., Vessella R.L., Visakorpi T.;
"Human pHyde is not a classical tumor suppressor gene in prostate
cancer.";
Int. J. Cancer 106:729-735(2003).
[12]
FUNCTION, AND INTERACTION WITH TCTP.
PubMed=15319436; DOI=10.1074/jbc.M404850200;
Amzallag N., Passer B.J., Allanic D., Segura E., Thery C., Goud B.,
Amson R., Telerman A.;
"TSAP6 facilitates the secretion of translationally controlled tumor
protein/histamine-releasing factor via a nonclassical pathway.";
J. Biol. Chem. 279:46104-46112(2004).
[13]
TISSUE SPECIFICITY.
PubMed=15885357; DOI=10.1016/j.jhep.2005.01.027;
Coulouarn C., Derambure C., Lefebvre G., Daveau R., Hiron M.,
Scotte M., Francois A., Daveau M., Salier J.-P.;
"Global gene repression in hepatocellular carcinoma and fetal liver,
and suppression of dudulin-2 mRNA as a possible marker for the
cirrhosis-to-tumor transition.";
J. Hepatol. 42:860-869(2005).
[14]
TISSUE SPECIFICITY.
PubMed=16227996; DOI=10.1038/ng1658;
Ohgami R.S., Campagna D.R., Greer E.L., Antiochos B., McDonald A.,
Chen J., Sharp J.J., Fujiwara Y., Barker J.E., Fleming M.D.;
"Identification of a ferrireductase required for efficient
transferrin-dependent iron uptake in erythroid cells.";
Nat. Genet. 37:1264-1269(2005).
[15]
FUNCTION.
PubMed=16651434; DOI=10.1158/0008-5472.CAN-05-4579;
Yu X., Harris S.L., Levine A.J.;
"The regulation of exosome secretion: a novel function of the p53
protein.";
Cancer Res. 66:4795-4801(2006).
[16]
INVOLVEMENT IN AHMIO2.
PubMed=22031863; DOI=10.1182/blood-2011-01-329011;
Grandchamp B., Hetet G., Kannengiesser C., Oudin C., Beaumont C.,
Rodrigues-Ferreira S., Amson R., Telerman A., Nielsen P., Kohne E.,
Balser C., Heimpel H.;
"A novel type of congenital hypochromic anemia associated with a
nonsense mutation in the STEAP3/TSAP6 gene.";
Blood 118:6660-6666(2011).
[17]
CLEAVAGE BY RHBDD1, INTERACTION WITH RHBDD1, GLYCOSYLATION AT ASN-256
AND ASN-344, AND MUTAGENESIS OF ASN-256; LEU-325 AND ASN-344.
PubMed=22624035; DOI=10.1371/journal.pone.0037452;
Wan C., Fu J., Wang Y., Miao S., Song W., Wang L.;
"Exosome-related multi-pass transmembrane protein TSAP6 is a target of
rhomboid protease RHBDD1-induced proteolysis.";
PLoS ONE 7:E37452-E37452(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-17; SER-20 AND
THR-474, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-215 ALONE AND IN COMPLEX
WITH NADPH, COFACTOR, AND SUBUNIT.
PubMed=18495927; DOI=10.1073/pnas.0801318105;
Sendamarai A.K., Ohgami R.S., Fleming M.D., Lawrence C.M.;
"Structure of the membrane proximal oxidoreductase domain of human
Steap3, the dominant ferrireductase of the erythroid transferrin
cycle.";
Proc. Natl. Acad. Sci. U.S.A. 105:7410-7415(2008).
-!- FUNCTION: Endosomal ferrireductase required for efficient
transferrin-dependent iron uptake in erythroid cells. Participates
in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Can
also reduce of Cu(2+) to Cu(1+), suggesting that it participates
in copper homeostasis. Uses NADP(+) as acceptor. May play a role
downstream of p53/TP53 to interface apoptosis and cell cycle
progression. Indirectly involved in exosome secretion by
facilitating the secretion of proteins such as TCTP.
{ECO:0000269|PubMed:15319436, ECO:0000269|PubMed:16651434}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
-!- COFACTOR:
Name=NADP(+); Xref=ChEBI:CHEBI:58349;
Evidence={ECO:0000269|PubMed:18495927};
-!- SUBUNIT: Homodimer. Interacts with BNIP3L, MYT1, RHBDL4/RHBDD1 and
TCTP. {ECO:0000269|PubMed:12606722, ECO:0000269|PubMed:15319436,
ECO:0000269|PubMed:18495927, ECO:0000269|PubMed:22624035}.
-!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Note=Localizes to vesicular-like
structures at the plasma membrane and around the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q658P3-1; Sequence=Displayed;
Name=2;
IsoId=Q658P3-2; Sequence=VSP_024829;
Name=3;
IsoId=Q658P3-3; Sequence=VSP_024830;
Name=4; Synonyms=pHyde II;
IsoId=Q658P3-4; Sequence=VSP_024830, VSP_024831;
-!- TISSUE SPECIFICITY: Expressed in adult bone marrow, placenta,
liver, skeletal muscle and pancreas. Down-regulated in
hepatocellular carcinoma. {ECO:0000269|PubMed:12606722,
ECO:0000269|PubMed:15885357, ECO:0000269|PubMed:16227996}.
-!- INDUCTION: By p53/TP53. {ECO:0000269|PubMed:12606722}.
-!- PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-
induced cleavage occurs at multiple sites in a glycosylation-
independent manner. {ECO:0000269|PubMed:22624035}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:22624035}.
-!- DISEASE: Anemia, hypochromic microcytic, with iron overload 2
(AHMIO2) [MIM:615234]: A hematologic disease characterized by
abnormal hemoglobin content in the erythrocytes which are reduced
in size, severe anemia, erythropoietic hyperplasia of bone marrow,
massive hepatic iron deposition, and hepatosplenomegaly.
{ECO:0000269|PubMed:22031863}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the STEAP family. {ECO:0000305}.
-!- CAUTION: Was initially thought to have tumor suppressor function
in prostate cancer. However, it was shown that it is probably not
the case (PubMed:12866033). {ECO:0000305|PubMed:12866033}.
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EMBL; AY214461; AAO38238.1; -; mRNA.
EMBL; AF423424; AAQ04065.1; -; mRNA.
EMBL; AF238864; AAL78206.1; -; mRNA.
EMBL; AF262322; AAM08128.1; -; mRNA.
EMBL; AY029585; AAK50538.1; -; mRNA.
EMBL; AY082673; AAM45136.1; -; mRNA.
EMBL; AK001691; BAA91839.1; -; mRNA.
EMBL; AK291608; BAF84297.1; -; mRNA.
EMBL; AL833624; CAH56204.1; -; mRNA.
EMBL; BX538047; CAD97986.1; -; mRNA.
EMBL; AC016673; AAX88963.1; -; Genomic_DNA.
EMBL; AC016736; AAY14872.1; -; Genomic_DNA.
EMBL; CH471103; EAW95209.1; -; Genomic_DNA.
EMBL; BC042150; AAH42150.1; -; mRNA.
EMBL; BC095421; AAH95421.2; -; mRNA.
CCDS; CCDS2125.1; -. [Q658P3-1]
CCDS; CCDS42738.1; -. [Q658P3-2]
RefSeq; NP_001008410.1; NM_001008410.1. [Q658P3-1]
RefSeq; NP_060704.2; NM_018234.2. [Q658P3-1]
RefSeq; NP_619543.2; NM_138637.2.
RefSeq; NP_878919.2; NM_182915.2. [Q658P3-2]
RefSeq; XP_006712677.1; XM_006712614.3. [Q658P3-1]
RefSeq; XP_006712678.1; XM_006712615.1. [Q658P3-1]
RefSeq; XP_011509705.1; XM_011511403.1. [Q658P3-1]
UniGene; Hs.647822; -.
PDB; 2VNS; X-ray; 2.00 A; A/B=1-215.
PDB; 2VQ3; X-ray; 2.00 A; A/B=1-215.
PDBsum; 2VNS; -.
PDBsum; 2VQ3; -.
ProteinModelPortal; Q658P3; -.
SMR; Q658P3; -.
BioGrid; 120533; 39.
IntAct; Q658P3; 5.
STRING; 9606.ENSP00000376822; -.
TCDB; 5.B.6.1.1; the transmembrane epithelial antigen protien-3 ferric reductase (steap) family.
iPTMnet; Q658P3; -.
PhosphoSitePlus; Q658P3; -.
SwissPalm; Q658P3; -.
BioMuta; STEAP3; -.
DMDM; 146325737; -.
EPD; Q658P3; -.
MaxQB; Q658P3; -.
PaxDb; Q658P3; -.
PeptideAtlas; Q658P3; -.
PRIDE; Q658P3; -.
DNASU; 55240; -.
Ensembl; ENST00000393106; ENSP00000376818; ENSG00000115107. [Q658P3-1]
Ensembl; ENST00000393107; ENSP00000376819; ENSG00000115107. [Q658P3-1]
Ensembl; ENST00000393110; ENSP00000376822; ENSG00000115107. [Q658P3-2]
GeneID; 55240; -.
KEGG; hsa:55240; -.
UCSC; uc002tlp.4; human. [Q658P3-1]
CTD; 55240; -.
DisGeNET; 55240; -.
EuPathDB; HostDB:ENSG00000115107.19; -.
GeneCards; STEAP3; -.
HGNC; HGNC:24592; STEAP3.
HPA; HPA050510; -.
MalaCards; STEAP3; -.
MIM; 609671; gene.
MIM; 615234; phenotype.
neXtProt; NX_Q658P3; -.
OpenTargets; ENSG00000115107; -.
Orphanet; 300298; Severe congenital hypochromic anemia with ringed sideroblasts.
PharmGKB; PA142670863; -.
eggNOG; ENOG410IF4F; Eukaryota.
eggNOG; COG2085; LUCA.
GeneTree; ENSGT00390000008042; -.
HOVERGEN; HBG054379; -.
InParanoid; Q658P3; -.
KO; K10142; -.
OMA; TLQSGPR; -.
OrthoDB; EOG091G0F9X; -.
PhylomeDB; Q658P3; -.
TreeFam; TF332031; -.
Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
ChiTaRS; STEAP3; human.
EvolutionaryTrace; Q658P3; -.
GeneWiki; STEAP3; -.
GenomeRNAi; 55240; -.
PRO; PR:Q658P3; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115107; -.
ExpressionAtlas; Q658P3; baseline and differential.
Genevisible; Q658P3; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005771; C:multivesicular body; IDA:MGI.
GO; GO:0008823; F:cupric reductase activity; IBA:GO_Central.
GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016723; F:oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0015677; P:copper ion import; IBA:GO_Central.
GO; GO:0098706; P:ferric iron import across plasma membrane; IBA:GO_Central.
GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
GO; GO:0009306; P:protein secretion; IDA:MGI.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0033572; P:transferrin transport; TAS:Reactome.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR028939; P5C_Rdtase_cat_N.
Pfam; PF03807; F420_oxidored; 1.
Pfam; PF01794; Ferric_reduct; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cell cycle;
Complete proteome; Copper; Endosome; FAD; Flavoprotein; Glycoprotein;
Heme; Ion transport; Iron; Iron transport; Membrane; Metal-binding;
NADP; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 488 Metalloreductase STEAP3.
/FTId=PRO_0000285171.
TOPO_DOM 1 207 Cytoplasmic. {ECO:0000255}.
TRANSMEM 208 228 Helical. {ECO:0000255}.
TOPO_DOM 229 258 Vesicular. {ECO:0000255}.
TRANSMEM 259 279 Helical. {ECO:0000255}.
TOPO_DOM 280 304 Cytoplasmic. {ECO:0000255}.
TRANSMEM 305 325 Helical. {ECO:0000255}.
TOPO_DOM 326 358 Vesicular. {ECO:0000255}.
TRANSMEM 359 379 Helical. {ECO:0000255}.
TOPO_DOM 380 390 Cytoplasmic. {ECO:0000255}.
TRANSMEM 391 411 Helical. {ECO:0000255}.
TOPO_DOM 412 433 Vesicular. {ECO:0000255}.
TRANSMEM 434 454 Helical. {ECO:0000255}.
TOPO_DOM 455 488 Cytoplasmic. {ECO:0000255}.
DOMAIN 259 407 Ferric oxidoreductase.
METAL 316 316 Iron (heme axial ligand). {ECO:0000305}.
METAL 409 409 Iron (heme axial ligand). {ECO:0000305}.
BINDING 36 36 NADP. {ECO:0000269|PubMed:18495927}.
BINDING 38 38 NADP; via amide nitrogen.
{ECO:0000269|PubMed:18495927}.
BINDING 39 39 NADP; via amide nitrogen.
{ECO:0000269|PubMed:18495927}.
BINDING 58 58 NADP. {ECO:0000269|PubMed:18495927}.
BINDING 59 59 NADP. {ECO:0000269|PubMed:18495927}.
BINDING 91 91 NADP; via carbonyl oxygen.
{ECO:0000269|PubMed:18495927}.
BINDING 116 116 NADP; via amide nitrogen.
{ECO:0000269|PubMed:18495927}.
BINDING 151 151 NADP; via amide nitrogen.
{ECO:0000269|PubMed:18495927}.
SITE 325 326 Cleavage; by RHBDL4/RHBDD1.
{ECO:0000305}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 474 474 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:22624035}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:22624035}.
VAR_SEQ 1 1 M -> MSHQPAVATKM (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_024829.
VAR_SEQ 351 351 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:10969787,
ECO:0000303|Ref.5}.
/FTId=VSP_024830.
VAR_SEQ 396 488 SSLGFVALVLSTLHTLTYGWTRAFEESRYKFYLPPTFTLTL
LVPCVVILAKALFLLPCISRRLARIRRGWERESTIKFTLPT
DHALAEKTSHV -> CVATSSAGNTGSGTRRPESQSQDPHL
PAPHHQTSFLGPRSFCCSLVPVSTPYGHQEDLSWTR (in
isoform 4).
{ECO:0000303|PubMed:10969787}.
/FTId=VSP_024831.
VARIANT 184 184 A -> T (in dbSNP:rs17013371).
/FTId=VAR_031975.
MUTAGEN 256 256 N->I: Inhibits glycosylation and does not
inhibit RHBDL4/RHBDD1-induced cleavage;
when associated with A-344.
{ECO:0000269|PubMed:22624035}.
MUTAGEN 325 325 L->F: Strongly inhibits RHBDL4/RHBDD1-
induced cleavage.
{ECO:0000269|PubMed:22624035}.
MUTAGEN 344 344 N->I: Inhibits glycosylation and does not
inhibit RHBDL4/RHBDD1-induced cleavage;
when associated with A-256.
{ECO:0000269|PubMed:22624035}.
CONFLICT 32 32 G -> S (in Ref. 3; AAL78206/AAM08128 and
6; AAM45136). {ECO:0000305}.
CONFLICT 68 68 F -> Y (in Ref. 4; AAK50538 and 7;
BAA91839). {ECO:0000305}.
CONFLICT 163 163 R -> G (in Ref. 3; AAL78206/AAM08128).
{ECO:0000305}.
CONFLICT 478 478 D -> G (in Ref. 8; CAD97986).
{ECO:0000305}.
STRAND 31 34 {ECO:0000244|PDB:2VNS}.
HELIX 38 49 {ECO:0000244|PDB:2VNS}.
STRAND 54 60 {ECO:0000244|PDB:2VNS}.
HELIX 61 67 {ECO:0000244|PDB:2VNS}.
STRAND 72 76 {ECO:0000244|PDB:2VNS}.
HELIX 77 80 {ECO:0000244|PDB:2VNS}.
STRAND 85 89 {ECO:0000244|PDB:2VNS}.
HELIX 93 95 {ECO:0000244|PDB:2VNS}.
HELIX 97 102 {ECO:0000244|PDB:2VNS}.
HELIX 103 106 {ECO:0000244|PDB:2VNS}.
STRAND 110 113 {ECO:0000244|PDB:2VNS}.
HELIX 119 124 {ECO:0000244|PDB:2VNS}.
HELIX 129 136 {ECO:0000244|PDB:2VNS}.
STRAND 140 145 {ECO:0000244|PDB:2VNS}.
HELIX 151 155 {ECO:0000244|PDB:2VNS}.
STRAND 164 170 {ECO:0000244|PDB:2VNS}.
HELIX 172 184 {ECO:0000244|PDB:2VNS}.
STRAND 188 191 {ECO:0000244|PDB:2VNS}.
HELIX 195 197 {ECO:0000244|PDB:2VNS}.
HELIX 198 203 {ECO:0000244|PDB:2VNS}.
SEQUENCE 488 AA; 54601 MW; C89EB0D0430F9BFB CRC64;
MPEEMDKPLI SLHLVDSDSS LAKVPDEAPK VGILGSGDFA RSLATRLVGS GFKVVVGSRN
PKRTARLFPS AAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLSDQLAGKI LVDVSNPTEQ
EHLQHRESNA EYLASLFPTC TVVKAFNVIS AWTLQAGPRD GNRQVPICGD QPEAKRAVSE
MALAMGFMPV DMGSLASAWE VEAMPLRLLP AWKVPTLLAL GLFVCFYAYN FVRDVLQPYV
QESQNKFFKL PVSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ
HRKQIGLLSF FCAALHALYS FCLPLRRAHR YDLVNLAVKQ VLANKSHLWV EEEVWRMEIY
LSLGVLALGT LSLLAVTSLP SIANSLNWRE FSFVQSSLGF VALVLSTLHT LTYGWTRAFE
ESRYKFYLPP TFTLTLLVPC VVILAKALFL LPCISRRLAR IRRGWEREST IKFTLPTDHA
LAEKTSHV


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