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Protein

Metalloreductase STEAP3

Gene

Steap3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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. Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP (By similarity). May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression.By similarity

Cofactori

Protein has several cofactor binding sites:

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)By similarity
Metal bindingi409 – 4091Iron (heme axial ligand)By similarity

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell cycle Source: UniProtKB-KW
  • ion transport Source: UniProtKB-KW
  • iron ion homeostasis Source: UniProtKB-KW
  • positive regulation of apoptotic process Source: RGD
  • 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, Heme, Iron, Metal-binding, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloreductase STEAP3 (EC:1.16.1.-)
Alternative name(s):
Six-transmembrane epithelial antigen of prostate 3
pHyde
Gene namesi
Name:Steap3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi708552. Steap3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 207207CytoplasmicSequence analysisAdd
BLAST
Transmembranei208 – 22821HelicalSequence analysisAdd
BLAST
Topological domaini229 – 25830VesicularSequence analysisAdd
BLAST
Transmembranei259 – 27921HelicalSequence analysisAdd
BLAST
Topological domaini280 – 30425CytoplasmicSequence analysisAdd
BLAST
Transmembranei305 – 32521HelicalSequence analysisAdd
BLAST
Topological domaini326 – 35833VesicularSequence analysisAdd
BLAST
Transmembranei359 – 37921HelicalSequence analysisAdd
BLAST
Topological domaini380 – 39011CytoplasmicSequence analysisAdd
BLAST
Transmembranei391 – 41121HelicalSequence analysisAdd
BLAST
Topological domaini412 – 43322VesicularSequence analysisAdd
BLAST
Transmembranei434 – 45421HelicalSequence analysisAdd
BLAST
Topological domaini455 – 48834CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Metalloreductase STEAP3PRO_0000285173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei20 – 201PhosphoserineCombined sources
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei325 – 3262Cleavage; by RHBDL4/RHBDD1By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ5RKL5.
PRIDEiQ5RKL5.

PTM databases

iPTMnetiQ5RKL5.

Expressioni

Gene expression databases

GenevisibleiQ5RKL5. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064137.

Structurei

3D structure databases

ProteinModelPortaliQ5RKL5.
SMRiQ5RKL5. Positions 29-209.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiENOG410IF4F. Eukaryota.
COG2085. LUCA.
HOVERGENiHBG054379.
InParanoidiQ5RKL5.
KOiK10142.
OMAiGWKVPAL.
OrthoDBiEOG7Z0JWH.
PhylomeDBiQ5RKL5.

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.

Q5RKL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGEMDKPLI SRRLVDSDGS LAEVPKEAPK VGILGSGDFA RSLATRLVGS
60 70 80 90 100
GFSVVVGSRN PKRTAGLFPS LAQVTFQEEA VSSPEVIFVA VFREHYSSLC
110 120 130 140 150
SLADQLAGKI LVDVSNPTEK ERLQHRQSNA EYLASLFPAC TVVKAFNVIS
160 170 180 190 200
AWALQAGPRD GNRQVLICGD QLEAKHTVSE MARAMGFTPL DMGSLASARE
210 220 230 240 250
VEAIPLRLLP SWKVPTLLAL GLFVCFYAYN FIRDVLQPYI RKDENKFYKM
260 270 280 290 300
PLSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ
310 320 330 340 350
HRKQIGLLSF FFAMLHALYS FCLPLRRSHR YDLVNLAVKQ VLANKSRLWV
360 370 380 390 400
EEEVWRMEIY LSLGVLALGM LSLLAVTSIP SIANSLNWKE FSFVQSTLGF
410 420 430 440 450
VALMLSTMHT LTYGWTRAFE ENHYKFYLPP TFTLTLLLPC VIILAKGLFL
460 470 480
LPCLSHRLTK IRRGWERDGA VKFMLPAGHT QGEKTSHV
Length:488
Mass (Da):54,674
Last modified:December 21, 2004 - v1
Checksum:i686E91B7DF2B88B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531S → F in AAL78207 (PubMed:10969787).Curated
Sequence conflicti53 – 531S → F in AAK00361 (PubMed:10969787).Curated
Sequence conflicti223 – 2264FVCF → STQS in AAL78207 (PubMed:10969787).Curated
Sequence conflicti223 – 2264FVCF → STQS in AAK00361 (PubMed:10969787).Curated
Sequence conflicti259 – 2591L → I in AAL78207 (PubMed:10969787).Curated
Sequence conflicti259 – 2591L → I in AAK00361 (PubMed:10969787).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF335281 mRNA. Translation: AAK00361.1.
AF238865 mRNA. Translation: AAL78207.1.
BC085696 mRNA. Translation: AAH85696.1.
RefSeqiNP_579848.1. NM_133314.1.
UniGeneiRn.16304.

Genome annotation databases

GeneIDi170824.
KEGGirno:170824.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF335281 mRNA. Translation: AAK00361.1.
AF238865 mRNA. Translation: AAL78207.1.
BC085696 mRNA. Translation: AAH85696.1.
RefSeqiNP_579848.1. NM_133314.1.
UniGeneiRn.16304.

3D structure databases

ProteinModelPortaliQ5RKL5.
SMRiQ5RKL5. Positions 29-209.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064137.

PTM databases

iPTMnetiQ5RKL5.

Proteomic databases

PaxDbiQ5RKL5.
PRIDEiQ5RKL5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi170824.
KEGGirno:170824.

Organism-specific databases

CTDi55240.
RGDi708552. Steap3.

Phylogenomic databases

eggNOGiENOG410IF4F. Eukaryota.
COG2085. LUCA.
HOVERGENiHBG054379.
InParanoidiQ5RKL5.
KOiK10142.
OMAiGWKVPAL.
OrthoDBiEOG7Z0JWH.
PhylomeDBiQ5RKL5.

Miscellaneous databases

PROiQ5RKL5.

Gene expression databases

GenevisibleiQ5RKL5. RN.

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. "Growth inhibition of prostate cancer by an adenovirus expressing a novel tumor suppressor gene, pHyde."
    Steiner M.S., Zhang X., Wang Y., Lu Y.
    Cancer Res. 60:4419-4425(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Prostatic carcinoma.
  2. "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].
    Tissue: Heart.
  3. "Apoptosis induction in prostate cancer cells by a novel gene product, pHyde, involves caspase-3."
    Zhang X., Steiner M.S., Rinaldy A., Lu Y.
    Oncogene 20:5982-5990(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [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_RAT
AccessioniPrimary (citable) accession number: Q5RKL5
Secondary accession number(s): Q99P41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: December 21, 2004
Last modified: June 8, 2016
This is version 85 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. 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.