STEAP3
entrez
55240
canonical
uniprot
Q658P3
canonical
ensembl
ENSG00000115107
resolver
ensp
ENSP00000376818
resolver
ensp
ENSP00000376819
resolver
ensp
ENSP00000376822
resolver
ensp
ENSP00000386510
resolver
ensp
ENSP00000539463
resolver
enst
ENST00000409811
resolver
genesymbol
STEAP3
resolver
genesymbol_syn
TSAP6
resolver
hgnc
HGNC:24592
resolver
uniprot
A8K6E3
resolver
uniprot
B8ZZX6
resolver
uniprot
Q4VBR2
resolver
uniprot
Q4ZG36
resolver
uniprot
Q53SQ8
resolver
uniprot
Q7Z389
resolver
uniprot
Q86SF6
resolver
uniprot
Q8NEW6
resolver
uniprot
Q8TDP3
resolver
uniprot
Q8TF03
resolver
uniprot
Q9NVB5
resolver
uniprot_entry
B8ZZX6_HUMAN
resolver
uniprot_entry
STEA3_HUMAN
resolver
uniprot_sec
A8K6E3
resolver
uniprot_sec
Q4VBR2
resolver
uniprot_sec
Q4ZG36
resolver
uniprot_sec
Q53SQ8
resolver
uniprot_sec
Q7Z389
resolver
uniprot_sec
Q86SF6
resolver
uniprot_sec
Q8NEW6
resolver
uniprot_sec
Q8TDP3
resolver
uniprot_sec
Q8TF03
resolver
uniprot_sec
Q9NVB5
resolver
amino_acid_sequence
MPEEMDKPLISLHLVDSDSSLAKVPDEAPKVGILGSGDFARSLATRLVGSGFKVVVGSRNPKRTARLFPSAAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLSDQLAGKILVDVSNPTEQEHLQHRESNAEYLASLFPTCTVVKAFNVISAWTLQAGPRDGNRQVPICGDQPEAKRAVSEMALAMGFMPVDMGSLASAWEVEAMPLRLLPAWKVPTLLALGLFVCFYAYNFVRDVLQPYVQESQNKFFKLPVSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFCAALHALYSFCLPLRRAHRYDLVNLAVKQVLANKSHLWVEEEVWRMEIYLSLGVLALGTLSLLAVTSLPSIANSLNWREFSFVQSSLGFVALVLSTLHTLTYGWTRAFEESRYKFYLPPTFTLTLLVPCVVILAKALFLLPCISRRLARIRRGWERESTIKFTLPTDHALAEKTSHV
uniprot
proteins
disease_involvement
DISEASE: Anemia, hypochromic microcytic, with iron overload 2 (AHMIO2) [MIM:615234]: A hematologic disease characterized by abnormal hemoglobin content in the erythrocytes which are reduced in size, severe anemia, erythropoietic hyperplasia of bone marrow, massive hepatic iron deposition, and hepatosplenomegaly. {ECO:0000269|PubMed:22031863}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.16.1.-
uniprot
proteins
function
FUNCTION: Integral membrane protein that functions as a NADPH-dependent ferric-chelate reductase, using NADPH from one side of the membrane to reduce a Fe(3+) chelate that is bound on the other side of the membrane (PubMed:26205815). Mediates sequential transmembrane electron transfer from NADPH to FAD and onto heme, and finally to the Fe(3+) chelate (By similarity). Can also reduce Cu(2+) to Cu(1+) (By similarity). Mediates efficient transferrin-dependent iron uptake in erythroid cells (By similarity). May play a role downstream of p53/TP53 to interface apoptosis and cell cycle progression (By similarity). Indirectly involved in exosome secretion by facilitating the secretion of proteins such as TCTP (PubMed:15319436, PubMed:16651434). {ECO:0000250|UniProtKB:Q5RKL5, ECO:0000250|UniProtKB:Q687X5, ECO:0000250|UniProtKB:Q8CI59, ECO:0000269|PubMed:15319436, ECO:0000269|PubMed:16651434, ECO:0000269|PubMed:26205815}.
uniprot
proteins
mass_dalton
54601
uniprot
proteins
mutagenesis
MUTAGEN 229; /note="Y->A: 2.5-fold increase in Km for Fe(+3)."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 229; /note="Y->F: 3-fold increase in Km for Fe(+3). 5-fold increase in Km for Fe(+3); when associated with F-319."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 256; /note="N->I: Inhibits glycosylation and does not inhibit RHBDL4/RHBDD1-induced cleavage; when associated with A-344."; /evidence="ECO:0000269|PubMed:22624035"; MUTAGEN 281; /note="Q->A: Loss of ferric-chelate reductase activity."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 287; /note="K->A: Loss of ferric-chelate reductase activity."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 295; /note="L->A: Loss of ferric-chelate reductase activity."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 298; /note="W->A: 2.5-fold increase in Km for FAD."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 302; /note="R->A: 3-fold increase in Km for FAD."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 302; /note="R->E: Loss of ferric-chelate reductase activity."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 303; /note="K->A: 3-fold increase in Km for FAD."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 303; /note="K->E: 5-fold increase in Km for FAD."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 316; /note="H->L: Loss of ferric-chelate reductase activity and heme b-binding."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 319; /note="Y->A: 2-fold increase in Km for Fe(+3)."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 319; /note="Y->F: 3-fold increase in Km for Fe(+3). 5-fold increase in Km for Fe(+3); when associated with F-229."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 325; /note="L->F: Strongly inhibits RHBDL4/RHBDD1-induced cleavage."; /evidence="ECO:0000269|PubMed:22624035"; MUTAGEN 344; /note="N->I: Inhibits glycosylation and does not inhibit RHBDL4/RHBDD1-induced cleavage; when associated with A-256."; /evidence="ECO:0000269|PubMed:22624035"; MUTAGEN 388; /note="W->A: 3-fold increase in Km for FAD."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 390; /note="E->A: 5-fold increase in Km for FAD."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 395; /note="Q->A: 20-fold increase in Km for FAD."; /evidence="ECO:0000269|PubMed:26205815"; MUTAGEN 409; /note="H->L: Loss of ferric-chelate reductase activity and heme b-binding."; /evidence="ECO:0000269|PubMed:26205815
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage occurs at multiple sites in a glycosylation-independent manner. {ECO:0000269|PubMed:22624035}.; PTM: Glycosylated. {ECO:0000269|PubMed:22624035}.
uniprot
proteins
protein_family
STEAP family
uniprot
proteins
pubmed
10969787
uniprot
proteins
pubmed
12606722
uniprot
proteins
pubmed
12866033
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15319436
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15885357
uniprot
proteins
pubmed
15897894
uniprot
proteins
pubmed
16227996
uniprot
proteins
pubmed
16651434
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18495927
uniprot
proteins
pubmed
22031863
uniprot
proteins
pubmed
22624035
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26205815
uniprot
proteins
sequence_length
488
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q8CI59}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to vesicular-like structures at the plasma membrane and around the nucleus. {ECO:0000269|PubMed:15319436}.
uniprot
proteins
transmembrane_region
TRANSMEM 208..228; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 259..279; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 305..325; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 359..379; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 391..411; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 434..454; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins