Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01116
Entry Name
UniProt Accession
Theoretical PI
8.86
Molecular Weight
54600.64
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Metalloreductase STEAP3
Protein Synonyms/Alias
1.16.1.-; Dudulin-2; Six-transmembrane epithelial antigen of prostate 3; Tumor suppressor-activated pathway protein 6; hTSAP6; pHyde; hpHyde;
Gene Name
STEAP3
Gene Synonyms/Alias
TSAP6;
Created Date
01-MAY-2007
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
453
Canonical
KALFLLPCISRRLAR
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Topological domain: 1 207 Cytoplasmic.
Transmembrane: 208 228 Helical.
Topological domain: 229 258 Vesicular.
Transmembrane: 259 279 Helical.
Topological domain: 280 304 Cytoplasmic.
Transmembrane: 305 325 Helical.
Topological domain: 326 358 Vesicular.
Transmembrane: 359 379 Helical.
Topological domain: 380 390 Cytoplasmic.
Transmembrane: 391 411 Helical.
Topological domain: 412 433 Vesicular.
Transmembrane: 434 454 Helical.
Topological domain: 455 488 Cytoplasmic.
Domain: 259 407 Ferric oxidoreductase.
Metal binding site: 316 316 Iron (heme axial ligand).
Metal binding site: 409 409 Iron (heme axial ligand).
Binding site: 36 36 NADP.
Binding site: 38 38 NADP; via amide nitrogen.
Binding site: 39 39 NADP; via amide nitrogen.
Binding site: 58 58 NADP.
Binding site: 59 59 NADP.
Binding site: 91 91 NADP; via carbonyl oxygen.
Binding site: 116 116 NADP; via amide nitrogen.
Binding site: 151 151 NADP; via amide nitrogen.
Functional site: 325 326 Cleavage; by RHBDL4/RHBDD1.
Modified residue: 17 17 Phosphoserine.
Modified residue: 20 20 Phosphoserine.
Protein Length
488 AA.
Protein Sequence
(Canonical)
MPEEMDKPLI SLHLVDSDSS LAKVPDEAPK VGILGSGDFA RSLATRLVGS GFKVVVGSRN  60
PKRTARLFPS AAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLSDQLAGKI LVDVSNPTEQ  120
EHLQHRESNA EYLASLFPTC TVVKAFNVIS AWTLQAGPRD GNRQVPICGD QPEAKRAVSE  180
MALAMGFMPV DMGSLASAWE VEAMPLRLLP AWKVPTLLAL GLFVCFYAYN FVRDVLQPYV  240
QESQNKFFKL PVSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ  300
HRKQIGLLSF FCAALHALYS FCLPLRRAHR YDLVNLAVKQ VLANKSHLWV EEEVWRMEIY  360
LSLGVLALGT LSLLAVTSLP SIANSLNWRE FSFVQSSLGF VALVLSTLHT LTYGWTRAFE  420
ESRYKFYLPP TFTLTLLVPC VVILAKALFL LPCISRRLAR IRRGWEREST IKFTLPTDHA  480
LAEKTSHV                                                           488
FASTA
(Canonical)
>LipidDB-9606-01116|Q658P3
MPEEMDKPLISLHLVDSDSSLAKVPDEAPKVGILGSGDFARSLATRLVGSGFKVVVGSRN
PKRTARLFPSAAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLSDQLAGKILVDVSNPTEQ
EHLQHRESNAEYLASLFPTCTVVKAFNVISAWTLQAGPRDGNRQVPICGDQPEAKRAVSE
MALAMGFMPVDMGSLASAWEVEAMPLRLLPAWKVPTLLALGLFVCFYAYNFVRDVLQPYV
QESQNKFFKLPVSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQ
HRKQIGLLSFFCAALHALYSFCLPLRRAHRYDLVNLAVKQVLANKSHLWVEEEVWRMEIY
LSLGVLALGTLSLLAVTSLPSIANSLNWREFSFVQSSLGFVALVLSTLHTLTYGWTRAFE
ESRYKFYLPPTFTLTLLVPCVVILAKALFLLPCISRRLARIRRGWERESTIKFTLPTDHA
LAEKTSHV
Gene Ontology
GO:0010008; C:endosome membrane; TAS:Reactome
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005771; C:multivesicular body; IDA:MGI
GO:0005886; C:plasma membrane; IEA:Ensembl
GO:0008823; F:cupric reductase activity; IEA:Ensembl
GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:Ensembl
GO:0000293; F:ferric-chelate reductase activity; IEA:Ensembl
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW
GO:0007049; P:cell cycle; IEA:UniProtKB-KW
GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome
GO:0015677; P:copper ion import; IEA:Ensembl
GO:1990182; P:exosomal secretion; IEA:Ensembl
GO:0097461; P:ferric iron import into cell; IEA:Ensembl
GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl
GO:1902167; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl
GO:0009306; P:protein secretion; IMP:UniProtKB
GO:0033572; P:transferrin transport; TAS:Reactome
GO:0055085; P:transmembrane transport; TAS:Reactome
Interpro
InterPro; IPR013130; Fe3_Rdtase_TM_dom
InterPro; IPR016040; NAD(P)-bd_dom
InterPro; IPR028939; ProC_N
Pfam
Pfam; PF03807; F420_oxidored;
Pfam; PF01794; Ferric_reduct;
SMART
PROSITE
PRINTS