Q658P3 (STEA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Metalloreductase STEAP3
EC=1.16.1.-

Alternative name(s):
Dudulin-2
Six-transmembrane epithelial antigen of prostate 3
Tumor suppressor-activated pathway protein 6
Short name=hTSAP6
pHyde
Short name=hpHyde

Gene names

Name:	STEAP3
Synonyms:	TSAP6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endosomal ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Participates in erythroid iron homeostasis by reducing Fe3+ to Fe2+. Can also reduce 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. Ref.11 Ref.12 Ref.15
Cofactor	FAD By similarity. Ref.17 NADP. Ref.17
Subunit structure	Homodimer. Interacts with BNIP3L, MYT1, RHBDL4/RHBDD1 and TCTP. Ref.1 Ref.12 Ref.16 Ref.17
Subcellular location	Endosome membrane; Multi-pass membrane protein By similarity. Note: Localizes to vesicular-like structures at the plasma membrane and around the nucleus.
Tissue specificity	Expressed in adult bone marrow, placenta, liver, skeletal muscle and pancreas. Down-regulated in hepatocellular carcinoma. Ref.1 Ref.13 Ref.14
Induction	By p53/TP53. Ref.1
Post-translational modification	Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage occurs at multiple sites in a glycosylation-independent manner. Ref.16 Glycosylated. Ref.16
Sequence similarities	Belongs to the STEAP family. Contains 1 ferric oxidoreductase domain.
Caution	Was initially thought to have tumor suppressor function in prostate cancer. However, it was shown that it is probably not the case (Ref.11).

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Ion transport Iron transport Transport
Cellular component	Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Copper FAD Flavoprotein Iron Metal-binding NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cellular iron ion homeostasis Traceable author statement. Source: Reactome induction of apoptosis Inferred from electronic annotation. Source: Compara protein secretion Inferred from mutant phenotype Ref.16. Source: UniProtKB transferrin transport Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome
Cellular_component	endosome membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW multivesicular body Inferred from direct assay Ref.12. Source: MGI plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	ferric-chelate reductase activity Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q658P3-1)

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.

Isoform 2 (identifier: Q658P3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSHQPAVATKM

Isoform 3 (identifier: Q658P3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     351-351: Missing.

Isoform 4 (identifier: Q658P3-4)

Also known as: pHyde II;

The sequence of this isoform differs from the canonical sequence as follows:
     351-351: Missing.
     396-488: SSLGFVALVL...HALAEKTSHV → CVATSSAGNT...GHQEDLSWTR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 488

488

Metalloreductase STEAP3

PRO_0000285171

Regions

Topological domain

1 – 207

207

Cytoplasmic Potential

Transmembrane

208 – 228

21

Helical; Potential

Topological domain

229 – 258

30

Vesicular Potential

Transmembrane

259 – 279

21

Helical; Potential

Topological domain

280 – 304

25

Cytoplasmic Potential

Transmembrane

305 – 325

21

Helical; Potential

Topological domain

326 – 358

33

Vesicular Potential

Transmembrane

359 – 379

21

Helical; Potential

Topological domain

380 – 390

11

Cytoplasmic Potential

Transmembrane

391 – 411

21

Helical; Potential

Topological domain

412 – 433

22

Vesicular Potential

Transmembrane

434 – 454

21

Helical; Potential

Topological domain

455 – 488

34

Cytoplasmic Potential

Domain

259 – 407

149

Ferric oxidoreductase

Sites

Metal binding

316

1

Iron (heme axial ligand) Probable

Metal binding

409

1

Iron (heme axial ligand) Probable

Binding site

36

1

NADP

Binding site

38

1

NADP; via amide nitrogen

Binding site

39

1

NADP; via amide nitrogen

Binding site

58

1

NADP

Binding site

59

1

NADP

Binding site

91

1

NADP; via carbonyl oxygen

Binding site

116

1

NADP; via amide nitrogen

Binding site

151

1

NADP; via amide nitrogen

Site

325 – 326

2

Cleavage; by RHBDL4/RHBDD1 Probable

Amino acid modifications

Modified residue

17

1

Phosphoserine By similarity

Modified residue

20

1

Phosphoserine By similarity

Glycosylation

256

1

N-linked (GlcNAc...) Probable

Glycosylation

344

1

N-linked (GlcNAc...) Probable

Natural variations

Alternative sequence

1

1

M → MSHQPAVATKM in isoform 2.

VSP_024829

Alternative sequence

351

1

Missing in isoform 3 and isoform 4.

VSP_024830

Alternative sequence

396 – 488

93

SSLGF…KTSHV → CVATSSAGNTGSGTRRPESQ SQDPHLPAPHHQTSFLGPRS FCCSLVPVSTPYGHQEDLSW TR in isoform 4.

VSP_024831

Natural variant

184

1

A → T.
Corresponds to variant rs17013371 [ dbSNP | Ensembl ].

VAR_031975

Experimental info

Mutagenesis

256

1

N → I: Inhibits glycosylation and does not inhibit RHBDL4/RHBDD1-induced cleavage; when associated with A-344. Ref.16

Mutagenesis

325

1

L → F: Strongly inhibits RHBDL4/RHBDD1-induced cleavage. Ref.16

Mutagenesis

344

1

N → I: Inhibits glycosylation and does not inhibit RHBDL4/RHBDD1-induced cleavage; when associated with A-256. Ref.16

Sequence conflict

32

1

G → S in AAL78206. Ref.3

Sequence conflict

32

1

G → S in AAM08128. Ref.3

Sequence conflict

32

1

G → S in AAM45136. Ref.6

Sequence conflict

68

1

F → Y in AAK50538. Ref.4

Sequence conflict

68

1

F → Y in BAA91839. Ref.7

Sequence conflict

163

1

R → G in AAL78206. Ref.3

Sequence conflict

163

1

R → G in AAM08128. Ref.3

Sequence conflict

478

1

D → G in CAD97986. Ref.8

Secondary structure

1

.

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.

.

.

.

.

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.

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.

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488

Helix Strand Turn

Details...

Beta strand

31 – 34

4

Helix

38 – 49

12

Beta strand

54 – 60

7

Helix

61 – 67

7

Beta strand

72 – 76

5

Helix

77 – 80

4

Beta strand

85 – 89

5

Helix

93 – 95

3

Helix

97 – 102

6

Helix

103 – 106

4

Beta strand

110 – 113

4

Helix

119 – 124

6

Helix

129 – 136

8

Beta strand

140 – 145

6

Helix

151 – 155

5

Beta strand

164 – 170

7

Helix

172 – 184

13

Beta strand

188 – 191

4

Helix

195 – 197

3

Helix

198 – 203

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: C89EB0D0430F9BFB	FASTA	488	54,601
	10 20 30 40 50 60 MPEEMDKPLI SLHLVDSDSS LAKVPDEAPK VGILGSGDFA RSLATRLVGS GFKVVVGSRN 70 80 90 100 110 120 PKRTARLFPS AAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLSDQLAGKI LVDVSNPTEQ 130 140 150 160 170 180 EHLQHRESNA EYLASLFPTC TVVKAFNVIS AWTLQAGPRD GNRQVPICGD QPEAKRAVSE 190 200 210 220 230 240 MALAMGFMPV DMGSLASAWE VEAMPLRLLP AWKVPTLLAL GLFVCFYAYN FVRDVLQPYV 250 260 270 280 290 300 QESQNKFFKL PVSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ 310 320 330 340 350 360 HRKQIGLLSF FCAALHALYS FCLPLRRAHR YDLVNLAVKQ VLANKSHLWV EEEVWRMEIY 370 380 390 400 410 420 LSLGVLALGT LSLLAVTSLP SIANSLNWRE FSFVQSSLGF VALVLSTLHT LTYGWTRAFE 430 440 450 460 470 480 ESRYKFYLPP TFTLTLLVPC VVILAKALFL LPCISRRLAR IRRGWEREST IKFTLPTDHA LAEKTSHV
	Isoform 2 [UniParc]. Checksum: 69DD201AA00C2D6B	FASTA	498	55,652
	10 20 30 40 50 60 MSHQPAVATK MPEEMDKPLI SLHLVDSDSS LAKVPDEAPK VGILGSGDFA RSLATRLVGS 70 80 90 100 110 120 GFKVVVGSRN PKRTARLFPS AAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLSDQLAGKI 130 140 150 160 170 180 LVDVSNPTEQ EHLQHRESNA EYLASLFPTC TVVKAFNVIS AWTLQAGPRD GNRQVPICGD 190 200 210 220 230 240 QPEAKRAVSE MALAMGFMPV DMGSLASAWE VEAMPLRLLP AWKVPTLLAL GLFVCFYAYN 250 260 270 280 290 300 FVRDVLQPYV QESQNKFFKL PVSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR 310 320 330 340 350 360 FPDWLDHWLQ HRKQIGLLSF FCAALHALYS FCLPLRRAHR YDLVNLAVKQ VLANKSHLWV 370 380 390 400 410 420 EEEVWRMEIY LSLGVLALGT LSLLAVTSLP SIANSLNWRE FSFVQSSLGF VALVLSTLHT 430 440 450 460 470 480 LTYGWTRAFE ESRYKFYLPP TFTLTLLVPC VVILAKALFL LPCISRRLAR IRRGWEREST 490 IKFTLPTDHA LAEKTSHV
	Isoform 3 [UniParc]. Checksum: 4A279EE7C8964412	FASTA	487	54,472
	10 20 30 40 50 60 MPEEMDKPLI SLHLVDSDSS LAKVPDEAPK VGILGSGDFA RSLATRLVGS GFKVVVGSRN 70 80 90 100 110 120 PKRTARLFPS AAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLSDQLAGKI LVDVSNPTEQ 130 140 150 160 170 180 EHLQHRESNA EYLASLFPTC TVVKAFNVIS AWTLQAGPRD GNRQVPICGD QPEAKRAVSE 190 200 210 220 230 240 MALAMGFMPV DMGSLASAWE VEAMPLRLLP AWKVPTLLAL GLFVCFYAYN FVRDVLQPYV 250 260 270 280 290 300 QESQNKFFKL PVSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ 310 320 330 340 350 360 HRKQIGLLSF FCAALHALYS FCLPLRRAHR YDLVNLAVKQ VLANKSHLWV EEVWRMEIYL 370 380 390 400 410 420 SLGVLALGTL SLLAVTSLPS IANSLNWREF SFVQSSLGFV ALVLSTLHTL TYGWTRAFEE 430 440 450 460 470 480 SRYKFYLPPT FTLTLLVPCV VILAKALFLL PCISRRLARI RRGWERESTI KFTLPTDHAL AEKTSHV
	Isoform 4 (pHyde II) [UniParc]. Checksum: 2ECEEB9C1515A9B7	FASTA	456	50,499
	10 20 30 40 50 60 MPEEMDKPLI SLHLVDSDSS LAKVPDEAPK VGILGSGDFA RSLATRLVGS GFKVVVGSRN 70 80 90 100 110 120 PKRTARLFPS AAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLSDQLAGKI LVDVSNPTEQ 130 140 150 160 170 180 EHLQHRESNA EYLASLFPTC TVVKAFNVIS AWTLQAGPRD GNRQVPICGD QPEAKRAVSE 190 200 210 220 230 240 MALAMGFMPV DMGSLASAWE VEAMPLRLLP AWKVPTLLAL GLFVCFYAYN FVRDVLQPYV 250 260 270 280 290 300 QESQNKFFKL PVSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ 310 320 330 340 350 360 HRKQIGLLSF FCAALHALYS FCLPLRRAHR YDLVNLAVKQ VLANKSHLWV EEVWRMEIYL 370 380 390 400 410 420 SLGVLALGTL SLLAVTSLPS IANSLNWREF SFVQCVATSS AGNTGSGTRR PESQSQDPHL 430 440 450 PAPHHQTSFL GPRSFCCSLV PVSTPYGHQE DLSWTR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The p53-inducible TSAP6 gene product regulates apoptosis and the cell cycle and interacts with Nix and the Myt1 kinase." Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C., Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L., Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R., Telerman A. Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH BNIP3L AND MYT1.
[2]	"Molecular cloning and characterization of STAMP2, an androgen-regulated six transmembrane protein that is overexpressed in prostate cancer." Korkmaz C.G., Korkmaz K.S., Kurys P., Elbi C., Wang L., Klokk T.I., Hammarstrom C., Troen G., Svindland A., Hager G.L., Saatcioglu F. Oncogene 24:4934-4945(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"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] (ISOFORMS 3 AND 4).
[4]	"Dudulin 2, a new tumor antigen expressed in various human tumors." Serru V., Manivet P., Lenoir C., Eschwege P., Lamblin D., Vaubourdolle M., Kellermann O., Loric S. Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Characterization of a novel apoptosis-inducing gene, hpHyde, that inhibits prostate cancer cell growth." Lu Y., Beheshti B., Squire J.A., Yang X.J. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Placenta.
[7]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Colon endothelium and Endometrial adenocarcinoma.
[8]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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). Tissue: Kidney.
[11]	"Human pHyde is not a classical tumor suppressor gene in prostate cancer." Porkka K.P., Nupponen N.N., Tammela T.L., Vessella R.L., Visakorpi T. Int. J. Cancer 106:729-735(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LACK OF TUMOR SUPPRESSOR FUNCTION.
[12]	"TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway." Amzallag N., Passer B.J., Allanic D., Segura E., Thery C., Goud B., Amson R., Telerman A. J. Biol. Chem. 279:46104-46112(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TCTP.
[13]	"Global gene repression in hepatocellular carcinoma and fetal liver, and suppression of dudulin-2 mRNA as a possible marker for the cirrhosis-to-tumor transition." Coulouarn C., Derambure C., Lefebvre G., Daveau R., Hiron M., Scotte M., Francois A., Daveau M., Salier J.-P. J. Hepatol. 42:860-869(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[14]	"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: TISSUE SPECIFICITY.
[15]	"The regulation of exosome secretion: a novel function of the p53 protein." Yu X., Harris S.L., Levine A.J. Cancer Res. 66:4795-4801(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis." Wan C., Fu J., Wang Y., Miao S., Song W., Wang L. PLoS ONE 7:E37452-E37452(2012) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY RHBDD1, INTERACTION WITH RHBDD1, GLYCOSYLATION AT ASN-256 AND ASN-344, MUTAGENESIS OF ASN-256; LEU-325 AND ASN-344.
[17]	"Structure of the membrane proximal oxidoreductase domain of human Steap3, the dominant ferrireductase of the erythroid transferrin cycle." Sendamarai A.K., Ohgami R.S., Fleming M.D., Lawrence C.M. Proc. Natl. Acad. Sci. U.S.A. 105:7410-7415(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-215 ALONE AND IN COMPLEX WITH NADPH, COFACTOR, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY214461 mRNA. Translation: AAO38238.1.
AF423424 mRNA. Translation: AAQ04065.1.
AF238864 mRNA. Translation: AAL78206.1.
AF262322 mRNA. Translation: AAM08128.1.
AY029585 mRNA. Translation: AAK50538.1.
AY082673 mRNA. Translation: AAM45136.1.
AK001691 mRNA. Translation: BAA91839.1.
AK291608 mRNA. Translation: BAF84297.1.
AL833624 mRNA. Translation: CAH56204.1.
BX538047 mRNA. Translation: CAD97986.1.
AC016673 Genomic DNA. Translation: AAX88963.1.
AC016736 Genomic DNA. Translation: AAY14872.1.
CH471103 Genomic DNA. Translation: EAW95209.1.
BC042150 mRNA. Translation: AAH42150.1.
BC095421 mRNA. Translation: AAH95421.2.

IPI

IPI00019350.
IPI00411628.
IPI00845307.
IPI00845327.

RefSeq

NP_001008410.1. NM_001008410.1.
NP_060704.2. NM_018234.2.
NP_878919.2. NM_182915.2.

UniGene

Hs.647822.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VNS	X-ray	2.00	A/B	1-215	[»]
2VQ3	X-ray	2.00	A/B	1-215	[»]

ProteinModelPortal

Q658P3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q658P3. 2 interactions.

Protein family/group databases

TCDB

9.B.66.1.1. animal nonclassical protein secretion (NPS) family.

PTM databases

PhosphoSite

Q658P3.

Polymorphism databases

DMDM

146325737.

Proteomic databases

PaxDb

Q658P3.

PRIDE

Q658P3.

Protocols and materials databases

DNASU

55240.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354888; ENSP00000346961; ENSG00000115107.
ENST00000393106; ENSP00000376818; ENSG00000115107.
ENST00000393107; ENSP00000376819; ENSG00000115107.
ENST00000393108; ENSP00000376820; ENSG00000115107.
ENST00000393110; ENSP00000376822; ENSG00000115107.
ENST00000425223; ENSP00000396214; ENSG00000115107.

GeneID

55240.

KEGG

hsa:55240.

UCSC

uc002tlp.3. human.
uc002tlq.3. human.

Organism-specific databases

CTD

55240.

GeneCards

GC02P119981.

HGNC

HGNC:24592. STEAP3.

HPA

HPA050510.

MIM

609671. gene.

neXtProt

NX_Q658P3.

PharmGKB

PA142670863.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2085.

HOVERGEN

HBG054379.

InParanoid

Q658P3.

KO

K10142.

OMA

QSGPRDG.

OrthoDB

EOG412M5Q.

PhylomeDB

Q658P3.

Enzyme and pathway databases

Reactome

REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

Q658P3.

Bgee

Q658P3.

Genevestigator

Q658P3.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR013130. Fe3_Rdtase_TM_dom.
IPR016040. NAD(P)-bd_dom.
IPR004455. NADP_OxRdtase_F420.
[Graphical view]

Pfam

PF03807. F420_oxidored. 1 hit.
PF01794. Ferric_reduct. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

STEAP3. human.

EvolutionaryTrace

Q658P3.

GenomeRNAi

55240.

NextBio

59270.

SOURCE

Search...

Entry information

Entry name

STEA3_HUMAN

Accession

Primary (citable) accession number: Q658P3
Secondary accession number(s): A8K6E3 , Q4VBR2, Q4ZG36, Q53SQ8, Q7Z389, Q86SF6, Q8NEW6, Q8TDP3, Q8TF03, Q9NVB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.