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Q8CI59

- STEA3_MOUSE

UniProt

Q8CI59 - STEA3_MOUSE

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Protein

Metalloreductase STEAP3

Gene
Steap3, Tsap6
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Inferred.1 Publication
NADP By similarity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361NADP By similarity
Binding sitei38 – 381NADP; via amide nitrogen By similarity
Binding sitei39 – 391NADP; via amide nitrogen By similarity
Binding sitei58 – 581NADP By similarity
Binding sitei59 – 591NADP By similarity
Binding sitei91 – 911NADP; via carbonyl oxygen By similarity
Binding sitei116 – 1161NADP; via amide nitrogen By similarity
Binding sitei151 – 1511NADP; via amide nitrogen By similarity
Metal bindingi316 – 3161Iron (heme axial ligand) Inferred
Sitei325 – 3262Cleavage; by RHBDL4/RHBDD1 By similarity
Metal bindingi409 – 4091Iron (heme axial ligand) Inferred

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
Complete GO annotation...

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; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 207207Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei208 – 22821Helical; Reviewed predictionAdd
BLAST
Topological domaini229 – 25830Vesicular Reviewed predictionAdd
BLAST
Transmembranei259 – 27921Helical; Reviewed predictionAdd
BLAST
Topological domaini280 – 30425Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei305 – 32521Helical; Reviewed predictionAdd
BLAST
Topological domaini326 – 35833Vesicular Reviewed predictionAdd
BLAST
Transmembranei359 – 37921Helical; Reviewed predictionAdd
BLAST
Topological domaini380 – 39011Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei391 – 41121Helical; Reviewed predictionAdd
BLAST
Topological domaini412 – 43322Vesicular Reviewed predictionAdd
BLAST
Transmembranei434 – 45421Helical; Reviewed predictionAdd
BLAST
Topological domaini455 – 48834Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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...) Reviewed prediction

Post-translational modificationi

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

Structurei

3D structure databases

ProteinModelPortaliQ8CI59.
SMRiQ8CI59. Positions 29-209.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the STEAP family.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAAEAHRQQGSCPTIPSEGC GKSPEKKGSAADSRPGTAM in isoform 2. VSP_024832

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 92 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

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