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Q8CI59

- STEA3_MOUSE

UniProt

Q8CI59 - STEA3_MOUSE

Protein

Metalloreductase STEAP3

Gene

Steap3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe3+ to Fe2+. Also mediates reduction of Cu2+ to Cu1+, 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.2 Publications

    Cofactori

    FAD.1 Publication
    NADP.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361NADPBy similarity
    Binding sitei38 – 381NADP; via amide nitrogenBy similarity
    Binding sitei39 – 391NADP; via amide nitrogenBy similarity
    Binding sitei58 – 581NADPBy similarity
    Binding sitei59 – 591NADPBy similarity
    Binding sitei91 – 911NADP; via carbonyl oxygenBy similarity
    Binding sitei116 – 1161NADP; via amide nitrogenBy similarity
    Binding sitei151 – 1511NADP; via amide nitrogenBy similarity
    Metal bindingi316 – 3161Iron (heme axial ligand)Curated
    Sitei325 – 3262Cleavage; by RHBDL4/RHBDD1By similarity
    Metal bindingi409 – 4091Iron (heme axial ligand)Curated

    GO - Molecular functioni

    1. cupric reductase activity Source: MGI
    2. ferric-chelate reductase (NADPH) activity Source: MGI
    3. ferric-chelate reductase activity Source: MGI
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell cycle Source: UniProtKB-KW
    3. copper ion import Source: MGI
    4. exosomal secretion Source: MGI
    5. ferric iron import into cell Source: MGI
    6. iron ion homeostasis Source: UniProtKB-KW
    7. iron ion transport Source: MGI
    8. oxidation-reduction process Source: MGI
    9. positive regulation of apoptotic process Source: Ensembl
    10. positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
    11. protein secretion Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Apoptosis, Cell cycle, Ion transport, Iron transport, Transport

    Keywords - Ligandi

    Copper, FAD, Flavoprotein, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    ReactomeiREACT_198515. Transferrin endocytosis and recycling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metalloreductase STEAP3 (EC:1.16.1.-)
    Alternative name(s):
    Dudulin-2
    Protein nm1054
    Six-transmembrane epithelial antigen of prostate 3
    Tumor suppressor-activated pathway protein 6
    Gene namesi
    Name:Steap3
    Synonyms:Tsap6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1915678. Steap3.

    Subcellular locationi

    Endosome membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. endosome Source: MGI
    2. endosome membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. multivesicular body Source: MGI
    5. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice display iron deficiency anemia, due to a defect in iron release through the transferrin cycle.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi316 – 3161H → L: Loss of function. 1 Publication
    Mutagenesisi409 – 4091H → L: Loss of function. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 488488Metalloreductase STEAP3PRO_0000285172Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171Phosphoserine1 Publication
    Modified residuei20 – 201Phosphoserine2 Publications
    Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage occurs at multiple sites in a glycosylation-independent manner By similarity.By similarity
    Glycosylated.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ8CI59.
    PRIDEiQ8CI59.

    PTM databases

    PhosphoSiteiQ8CI59.

    Expressioni

    Tissue specificityi

    Highly expressed in fetal liver (the site of midgestational hematopoiesis).2 Publications

    Gene expression databases

    ArrayExpressiQ8CI59.
    BgeeiQ8CI59.
    CleanExiMM_STEAP3.
    GenevestigatoriQ8CI59.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with BNIP3L, MYT1, RHBDL4/RHBDD1 and TCTP By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CI59.
    SMRiQ8CI59. Positions 29-209.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 207207CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini229 – 25830VesicularSequence AnalysisAdd
    BLAST
    Topological domaini280 – 30425CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini326 – 35833VesicularSequence AnalysisAdd
    BLAST
    Topological domaini380 – 39011CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini412 – 43322VesicularSequence AnalysisAdd
    BLAST
    Topological domaini455 – 48834CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei208 – 22821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei259 – 27921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei305 – 32521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei359 – 37921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei391 – 41121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei434 – 45421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini259 – 407149Ferric oxidoreductaseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the STEAP family.Curated
    Contains 1 ferric oxidoreductase domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2085.
    GeneTreeiENSGT00390000008042.
    HOGENOMiHOG000234491.
    HOVERGENiHBG054379.
    InParanoidiQ8CI59.
    KOiK10142.
    PhylomeDBiQ8CI59.
    TreeFamiTF332031.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR013130. Fe3_Rdtase_TM_dom.
    IPR016040. NAD(P)-bd_dom.
    IPR028939. ProC_N.
    [Graphical view]
    PfamiPF03807. F420_oxidored. 1 hit.
    PF01794. Ferric_reduct. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8CI59-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSGEMDKPLI SRRLVDSDGS LAEVPKEAPK VGILGSGDFA RSLATRLVGS    50
    GFSVVVGSRN PKRTAGLFPS LAQVTFQEEA VSSPEVIFVA VFREHYSSLC 100
    SLADQLAGKI LVDVSNPTEK EHLQHRQSNA EYLASLFPAC TVVKAFNVIS 150
    AWALQAGPRD GNRQVLICSD QPEAKRTISE MARAMGFTPL DMGSLASARE 200
    VEAIPLRLLP SWKVPTLLAL GLFVCFYTYN FIRDVLQPYI RKDENKFYKM 250
    PLSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ 300
    HRKQIGLLSF FFAMLHALYS FCLPLRRSHR YDLVNLAVKQ VLANKSRLWV 350
    EEEVWRMEIY LSLGVLALGM LSLLAVTSLP SIANSLNWKE FSFVQSTLGF 400
    VALILSTMHT LTYGWTRAFE ENHYKFYLPP TFTLTLLLPC VIILAKGLFL 450
    LPCLSRRLTK IRRGWEKDGA VKFMLPGDHT QGEKTSHV 488
    Length:488
    Mass (Da):54,749
    Last modified:March 1, 2003 - v1
    Checksum:i9A08D99C90CF83F4
    GO
    Isoform 2 (identifier: Q8CI59-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAAEAHRQQGSCPTIPSEGCGKSPEKKGSAADSRPGTAM

    Show »
    Length:526
    Mass (Da):58,530
    Checksum:i6306CD717E25200A
    GO

    Sequence cautioni

    The sequence AAK50539.1 differs from that shown. Reason: Frameshift at positions 171, 173 and 479.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti81 – 811V → M in BAC37383. (PubMed:16141072)Curated
    Sequence conflicti157 – 1571G → V in AAK50539. 1 PublicationCurated
    Sequence conflicti169 – 1724SDQP → GNQQ in AAK50539. 1 PublicationCurated
    Sequence conflicti176 – 1794RTIS → QRVM in AAK50539. 1 PublicationCurated
    Sequence conflicti212 – 2121W → G in AAK50539. 1 PublicationCurated
    Sequence conflicti350 – 3501V → A in BAC37383. (PubMed:16141072)Curated
    Sequence conflicti350 – 3501V → A in BAE39201. (PubMed:16141072)Curated
    Sequence conflicti455 – 4551S → N in BAC37383. (PubMed:16141072)Curated
    Sequence conflicti455 – 4551S → N in BAE39201. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAAEAHRQQGSCPTIPSEGC GKSPEKKGSAADSRPGTAM in isoform 2. 1 PublicationVSP_024832

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY214462 mRNA. Translation: AAO38239.1.
    AY029586 mRNA. Translation: AAK50539.1. Frameshift.
    AK078769 mRNA. Translation: BAC37383.1.
    AK167028 mRNA. Translation: BAE39201.1.
    AK171237 mRNA. Translation: BAE42333.1.
    BC037435 mRNA. Translation: AAH37435.1.
    CCDSiCCDS48343.1. [Q8CI59-1]
    RefSeqiNP_001078878.1. NM_001085409.1.
    NP_573449.2. NM_133186.3.
    UniGeneiMm.181033.

    Genome annotation databases

    EnsembliENSMUST00000112639; ENSMUSP00000108258; ENSMUSG00000026389.
    ENSMUST00000112640; ENSMUSP00000108259; ENSMUSG00000026389.
    ENSMUST00000112641; ENSMUSP00000108260; ENSMUSG00000026389.
    GeneIDi68428.
    KEGGimmu:68428.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY214462 mRNA. Translation: AAO38239.1 .
    AY029586 mRNA. Translation: AAK50539.1 . Frameshift.
    AK078769 mRNA. Translation: BAC37383.1 .
    AK167028 mRNA. Translation: BAE39201.1 .
    AK171237 mRNA. Translation: BAE42333.1 .
    BC037435 mRNA. Translation: AAH37435.1 .
    CCDSi CCDS48343.1. [Q8CI59-1 ]
    RefSeqi NP_001078878.1. NM_001085409.1.
    NP_573449.2. NM_133186.3.
    UniGenei Mm.181033.

    3D structure databases

    ProteinModelPortali Q8CI59.
    SMRi Q8CI59. Positions 29-209.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8CI59.

    Proteomic databases

    PaxDbi Q8CI59.
    PRIDEi Q8CI59.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000112639 ; ENSMUSP00000108258 ; ENSMUSG00000026389 .
    ENSMUST00000112640 ; ENSMUSP00000108259 ; ENSMUSG00000026389 .
    ENSMUST00000112641 ; ENSMUSP00000108260 ; ENSMUSG00000026389 .
    GeneIDi 68428.
    KEGGi mmu:68428.

    Organism-specific databases

    CTDi 55240.
    MGIi MGI:1915678. Steap3.

    Phylogenomic databases

    eggNOGi COG2085.
    GeneTreei ENSGT00390000008042.
    HOGENOMi HOG000234491.
    HOVERGENi HBG054379.
    InParanoidi Q8CI59.
    KOi K10142.
    PhylomeDBi Q8CI59.
    TreeFami TF332031.

    Enzyme and pathway databases

    Reactomei REACT_198515. Transferrin endocytosis and recycling.

    Miscellaneous databases

    NextBioi 327158.
    PROi Q8CI59.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CI59.
    Bgeei Q8CI59.
    CleanExi MM_STEAP3.
    Genevestigatori Q8CI59.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR013130. Fe3_Rdtase_TM_dom.
    IPR016040. NAD(P)-bd_dom.
    IPR028939. ProC_N.
    [Graphical view ]
    Pfami PF03807. F420_oxidored. 1 hit.
    PF01794. Ferric_reduct. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    2. Serru V., Lamblin D., Lenoir C., Manivet P., Vaubourdolle M., Kellermann O., Loric S.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J and NOD.
      Tissue: Testis.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: Czech II.
      Tissue: Mammary tumor.
    5. "Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells."
      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.
      Nat. Genet. 37:1264-1269(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, HEME-BINDING, COFACTOR, TISSUE SPECIFICITY, MUTAGENESIS OF HIS-316 AND HIS-409.
    6. Cited for: FUNCTION.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSTEA3_MOUSE
    AccessioniPrimary (citable) accession number: Q8CI59
    Secondary accession number(s): Q3TKE4
    , Q80ZF3, Q8C5F0, Q924Z1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3