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Protein

Metalloreductase STEAP2

Gene

Steap2

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

Functioni

Metalloreductase that has the ability to reduce both Fe3+ to Fe2+ and Cu2+ to Cu1+. Uses NAD+ as acceptor.1 Publication

Cofactori

FADBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi315 – 3151Iron (heme axial ligand)By similarity
Metal bindingi408 – 4081Iron (heme axial ligand)By similarity

GO - Molecular functioni

  • cupric reductase activity Source: MGI
  • ferric-chelate reductase (NADPH) activity Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • transporter activity Source: UniProtKB

GO - Biological processi

  • copper ion import Source: MGI
  • endocytosis Source: UniProtKB
  • ferric iron import into cell Source: MGI
  • Golgi to plasma membrane transport Source: UniProtKB
  • iron ion homeostasis Source: UniProtKB-KW
  • oxidation-reduction process Source: MGI
  • regulated exocytosis Source: UniProtKB
  • response to hormone Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Ion transport, Iron transport, Transport

Keywords - Ligandi

Copper, FAD, Flavoprotein, Heme, Iron, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloreductase STEAP2 (EC:1.16.1.-)
Alternative name(s):
Six-transmembrane epithelial antigen of prostate 2
Gene namesi
Name:Steap2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1921301. Steap2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei207 – 22721HelicalSequence analysisAdd
BLAST
Transmembranei258 – 27821HelicalSequence analysisAdd
BLAST
Transmembranei304 – 32421HelicalSequence analysisAdd
BLAST
Transmembranei358 – 37821HelicalSequence analysisAdd
BLAST
Transmembranei392 – 41221HelicalSequence analysisAdd
BLAST
Transmembranei431 – 45121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489Metalloreductase STEAP2PRO_0000191698Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31PhosphoserineBy similarity
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei482 – 4821PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BWB6.
PaxDbiQ8BWB6.
PRIDEiQ8BWB6.

PTM databases

iPTMnetiQ8BWB6.
PhosphoSiteiQ8BWB6.

Expressioni

Gene expression databases

BgeeiQ8BWB6.
ExpressionAtlasiQ8BWB6. baseline and differential.
GenevisibleiQ8BWB6. MM.

Interactioni

Protein-protein interaction databases

BioGridi216452. 1 interaction.
STRINGi10090.ENSMUSP00000015797.

Structurei

3D structure databases

ProteinModelPortaliQ8BWB6.
SMRiQ8BWB6. Positions 32-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini258 – 406149Ferric oxidoreductaseAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IF4F. Eukaryota.
COG2085. LUCA.
GeneTreeiENSGT00390000008042.
HOGENOMiHOG000234491.
HOVERGENiHBG054379.
InParanoidiQ8BWB6.
KOiK14738.
OMAiLLITTFH.
PhylomeDBiQ8BWB6.
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]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BWB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESISMMGSP KSLETFLPNG INGIKDARQV TVGVIGSGDF AKSLTIRLIR
60 70 80 90 100
CGYHVVIGSR NPKFASEFFP HVVDVTHHED ALTKTNIIFV AIHREHYTSL
110 120 130 140 150
WDLRHLLVGK ILIDVSNNMR VNQYPESNAE YLASLFPDSL IVKGFNVISA
160 170 180 190 200
WALQLGPKDA SRQVYICSNN IQARQQVIEL ARQLNFIPVD LGSLSSAKEI
210 220 230 240 250
ENLPLRLFTL WRGPVVVAIS LATFFFLYSF VRDVIHPYAR NQQSDFYKIP
260 270 280 290 300
IEIVNKTLPI VAITLLSLVY LAGLLAAAYQ LYYGTKYRRF PPWLDTWLQC
310 320 330 340 350
RKQLGLLSFF FAVVHVAYSL CLPMRRSERY LFLNMAYQQV HANIENAWNE
360 370 380 390 400
EEVWRIEMYI SFGIMSLGLL SLLAVTSIPS VSNALNWREF SFIQSTLGYV
410 420 430 440 450
ALLITTFHVL IYGWKRAFAE EYYRFYTPPN FVLALVLPSI VILGKMILLL
460 470 480
PCISRKLKRI KKGWEKSQFL DEGMGGAVPH LSPERVTVM
Length:489
Mass (Da):55,760
Last modified:March 1, 2003 - v1
Checksum:i98CD63D59DDDF24C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052981 mRNA. Translation: BAC35230.1.
AK162343 mRNA. Translation: BAE36864.1.
CCDSiCCDS39007.1.
RefSeqiNP_001096626.1. NM_001103156.2.
NP_001096627.1. NM_001103157.2.
NP_001272398.1. NM_001285469.1.
NP_001272399.1. NM_001285470.1.
NP_083010.2. NM_028734.5.
XP_011238977.1. XM_011240675.1.
UniGeneiMm.274956.

Genome annotation databases

EnsembliENSMUST00000015797; ENSMUSP00000015797; ENSMUSG00000015653.
ENSMUST00000115424; ENSMUSP00000111084; ENSMUSG00000015653.
ENSMUST00000115425; ENSMUSP00000111085; ENSMUSG00000015653.
ENSMUST00000115426; ENSMUSP00000111086; ENSMUSG00000015653.
ENSMUST00000164219; ENSMUSP00000132501; ENSMUSG00000015653.
GeneIDi74051.
KEGGimmu:74051.
UCSCiuc008wiw.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052981 mRNA. Translation: BAC35230.1.
AK162343 mRNA. Translation: BAE36864.1.
CCDSiCCDS39007.1.
RefSeqiNP_001096626.1. NM_001103156.2.
NP_001096627.1. NM_001103157.2.
NP_001272398.1. NM_001285469.1.
NP_001272399.1. NM_001285470.1.
NP_083010.2. NM_028734.5.
XP_011238977.1. XM_011240675.1.
UniGeneiMm.274956.

3D structure databases

ProteinModelPortaliQ8BWB6.
SMRiQ8BWB6. Positions 32-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216452. 1 interaction.
STRINGi10090.ENSMUSP00000015797.

PTM databases

iPTMnetiQ8BWB6.
PhosphoSiteiQ8BWB6.

Proteomic databases

MaxQBiQ8BWB6.
PaxDbiQ8BWB6.
PRIDEiQ8BWB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015797; ENSMUSP00000015797; ENSMUSG00000015653.
ENSMUST00000115424; ENSMUSP00000111084; ENSMUSG00000015653.
ENSMUST00000115425; ENSMUSP00000111085; ENSMUSG00000015653.
ENSMUST00000115426; ENSMUSP00000111086; ENSMUSG00000015653.
ENSMUST00000164219; ENSMUSP00000132501; ENSMUSG00000015653.
GeneIDi74051.
KEGGimmu:74051.
UCSCiuc008wiw.3. mouse.

Organism-specific databases

CTDi261729.
MGIiMGI:1921301. Steap2.

Phylogenomic databases

eggNOGiENOG410IF4F. Eukaryota.
COG2085. LUCA.
GeneTreeiENSGT00390000008042.
HOGENOMiHOG000234491.
HOVERGENiHBG054379.
InParanoidiQ8BWB6.
KOiK14738.
OMAiLLITTFH.
PhylomeDBiQ8BWB6.
TreeFamiTF332031.

Miscellaneous databases

ChiTaRSiSteap2. mouse.
PROiQ8BWB6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BWB6.
ExpressionAtlasiQ8BWB6. baseline and differential.
GenevisibleiQ8BWB6. MM.

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]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Epididymis and Head.
  2. Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiSTEA2_MOUSE
AccessioniPrimary (citable) accession number: Q8BWB6
Secondary accession number(s): Q3TS12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.