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Metalloreductase STEAP2 (EC 1.16.1.-) (Prostate cancer-associated protein 1) (Protein up-regulated in metastatic prostate cancer) (PUMPCn) (Six-transmembrane epithelial antigen of prostate 2) (SixTransMembrane protein of prostate 1)

 STEA2_HUMAN             Reviewed;         490 AA.
Q8NFT2; A4D1F1; G5E9C6; Q6UXN6; Q6YPB1; Q8IUE7;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
25-OCT-2017, entry version 127.
RecName: Full=Metalloreductase STEAP2;
EC=1.16.1.-;
AltName: Full=Prostate cancer-associated protein 1;
AltName: Full=Protein up-regulated in metastatic prostate cancer;
Short=PUMPCn;
AltName: Full=Six-transmembrane epithelial antigen of prostate 2;
AltName: Full=SixTransMembrane protein of prostate 1;
Name=STEAP2; Synonyms=PCANAP1, STAMP1; ORFNames=UNQ6507/PRO23203;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
VARIANTS CYS-17 AND ILE-475.
TISSUE=Prostate;
PubMed=12095985; DOI=10.1074/jbc.M202414200;
Korkmaz K.S., Elbi C.C., Korkmaz C.G., Loda M., Hager G.L.,
Saatcioglu F.;
"Molecular cloning and characterization of STAMP1, a highly prostate
specific six-trans-membrane protein that is overexpressed in prostate
cancer.";
J. Biol. Chem. 277:36689-36696(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND VARIANTS CYS-17; GLN-456 AND ILE-475.
TISSUE=Prostate;
PubMed=12429817;
Porkka K.P., Helenius M.A., Visakorpi T.;
"Cloning and characterization of a novel six-transmembrane protein
STEAP2, expressed in normal and malignant prostate.";
Lab. Invest. 82:1573-1582(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT CYS-17.
Zhang Z., Eberhard D.A., Polakis P., Grimaldi C., Frantz G.D.,
Hillan K.J., Wood W.I.;
"Bioinformatics identification and clinical validation of tumor
antigens by analysis of EST and tissue microarray data.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
CYS-17.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-475.
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-475.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
TISSUE SPECIFICITY.
PubMed=16609065; DOI=10.1182/blood-2006-02-003681;
Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.;
"The Steap proteins are metalloreductases.";
Blood 108:1388-1394(2006).
[9]
VARIANT [LARGE SCALE ANALYSIS] CYS-17, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
-!- FUNCTION: Metalloreductase that has the ability to reduce both
Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor (By
similarity). {ECO:0000250}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Cell membrane
{ECO:0000269|PubMed:12429817}; Multi-pass membrane protein
{ECO:0000269|PubMed:12429817}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8NFT2-1; Sequence=Displayed;
Name=2;
IsoId=Q8NFT2-2; Sequence=VSP_030999;
Name=3;
IsoId=Q8NFT2-3; Sequence=VSP_045590;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at high levels in prostate and at
significantly lower levels in heart, brain, kidney, pancreas, and
ovary. {ECO:0000269|PubMed:12095985, ECO:0000269|PubMed:12429817,
ECO:0000269|PubMed:16609065}.
-!- SIMILARITY: Belongs to the STEAP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/STEAP2ID42435ch7q21.html";
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EMBL; AY008444; AAG32148.1; -; mRNA.
EMBL; AY008445; AAG32149.1; -; mRNA.
EMBL; AF455138; AAN04080.1; -; mRNA.
EMBL; AF526382; AAQ08976.1; -; mRNA.
EMBL; AY358267; AAQ88634.1; -; mRNA.
EMBL; AC002064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236949; EAL24165.1; -; Genomic_DNA.
EMBL; CH471091; EAW76890.1; -; Genomic_DNA.
EMBL; CH471091; EAW76894.1; -; Genomic_DNA.
CCDS; CCDS43612.1; -. [Q8NFT2-2]
CCDS; CCDS5615.1; -. [Q8NFT2-1]
CCDS; CCDS59064.1; -. [Q8NFT2-3]
RefSeq; NP_001035755.1; NM_001040665.1. [Q8NFT2-1]
RefSeq; NP_001035756.1; NM_001040666.1. [Q8NFT2-2]
RefSeq; NP_001231873.1; NM_001244944.1. [Q8NFT2-1]
RefSeq; NP_001231875.1; NM_001244946.1. [Q8NFT2-3]
RefSeq; NP_694544.2; NM_152999.3. [Q8NFT2-1]
RefSeq; XP_006715984.1; XM_006715921.3. [Q8NFT2-1]
RefSeq; XP_016867442.1; XM_017011953.1. [Q8NFT2-1]
RefSeq; XP_016867443.1; XM_017011954.1. [Q8NFT2-1]
UniGene; Hs.489051; -.
ProteinModelPortal; Q8NFT2; -.
SMR; Q8NFT2; -.
BioGrid; 129285; 4.
CORUM; Q8NFT2; -.
STRING; 9606.ENSP00000287908; -.
TCDB; 5.B.6.1.2; the transmembrane epithelial antigen protien-3 ferric reductase (steap) family.
iPTMnet; Q8NFT2; -.
PhosphoSitePlus; Q8NFT2; -.
BioMuta; STEAP2; -.
DMDM; 296452950; -.
MaxQB; Q8NFT2; -.
PaxDb; Q8NFT2; -.
PeptideAtlas; Q8NFT2; -.
PRIDE; Q8NFT2; -.
DNASU; 261729; -.
Ensembl; ENST00000287908; ENSP00000287908; ENSG00000157214. [Q8NFT2-1]
Ensembl; ENST00000394621; ENSP00000378119; ENSG00000157214. [Q8NFT2-1]
Ensembl; ENST00000394622; ENSP00000378120; ENSG00000157214. [Q8NFT2-1]
Ensembl; ENST00000394626; ENSP00000378123; ENSG00000157214. [Q8NFT2-2]
Ensembl; ENST00000394629; ENSP00000378125; ENSG00000157214. [Q8NFT2-2]
Ensembl; ENST00000394632; ENSP00000378128; ENSG00000157214. [Q8NFT2-3]
GeneID; 261729; -.
KEGG; hsa:261729; -.
UCSC; uc003ujz.4; human. [Q8NFT2-1]
CTD; 261729; -.
DisGeNET; 261729; -.
EuPathDB; HostDB:ENSG00000157214.13; -.
GeneCards; STEAP2; -.
HGNC; HGNC:17885; STEAP2.
HPA; HPA029115; -.
HPA; HPA055603; -.
MIM; 605094; gene.
neXtProt; NX_Q8NFT2; -.
OpenTargets; ENSG00000157214; -.
PharmGKB; PA38473; -.
eggNOG; ENOG410IF4F; Eukaryota.
eggNOG; COG2085; LUCA.
GeneTree; ENSGT00390000008042; -.
HOGENOM; HOG000234491; -.
HOVERGEN; HBG054379; -.
InParanoid; Q8NFT2; -.
KO; K14738; -.
OMA; THHEDAV; -.
OrthoDB; EOG091G0F9X; -.
PhylomeDB; Q8NFT2; -.
TreeFam; TF332031; -.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
ChiTaRS; STEAP2; human.
GeneWiki; STEAP2; -.
GenomeRNAi; 261729; -.
PRO; PR:Q8NFT2; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000157214; -.
CleanEx; HS_STEAP2; -.
ExpressionAtlas; Q8NFT2; baseline and differential.
Genevisible; Q8NFT2; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:UniProtKB.
GO; GO:0008823; F:cupric reductase activity; IBA:GO_Central.
GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005215; F:transporter activity; IDA:UniProtKB.
GO; GO:0015677; P:copper ion import; IBA:GO_Central.
GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
GO; GO:0098706; P:ferric iron import across plasma membrane; IBA:GO_Central.
GO; GO:0006893; P:Golgi to plasma membrane transport; IDA:UniProtKB.
GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
GO; GO:0045055; P:regulated exocytosis; IDA:UniProtKB.
GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR028939; P5C_Rdtase_cat_N.
Pfam; PF03807; F420_oxidored; 1.
Pfam; PF01794; Ferric_reduct; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Copper;
Electron transport; Endosome; FAD; Flavoprotein; Heme; Ion transport;
Iron; Iron transport; Membrane; Metal-binding; NAD; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 490 Metalloreductase STEAP2.
/FTId=PRO_0000191697.
TRANSMEM 208 228 Helical. {ECO:0000255}.
TRANSMEM 259 279 Helical. {ECO:0000255}.
TRANSMEM 305 325 Helical. {ECO:0000255}.
TRANSMEM 359 379 Helical. {ECO:0000255}.
TRANSMEM 393 413 Helical. {ECO:0000255}.
TRANSMEM 432 452 Helical. {ECO:0000255}.
DOMAIN 259 407 Ferric oxidoreductase.
METAL 316 316 Iron (heme axial ligand). {ECO:0000250}.
METAL 409 409 Iron (heme axial ligand). {ECO:0000250}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BWB6}.
VAR_SEQ 396 490 STLGYVALLISTFHVLIYGWKRAFEEEYYRFYTPPNFVLAL
VLPSIVILGKIILFLPCISRKLKRIKKGWEKSQFLEEGMGG
TIPHVSPERVTVM -> IFCSFADTQTELELEFVFLLTLLL
(in isoform 3).
{ECO:0000303|PubMed:12095985}.
/FTId=VSP_045590.
VAR_SEQ 445 490 GKIILFLPCISRKLKRIKKGWEKSQFLEEGMGGTIPHVSPE
RVTVM -> DLLQLCRYPD (in isoform 2).
{ECO:0000303|PubMed:12975309,
ECO:0000303|Ref.3}.
/FTId=VSP_030999.
VARIANT 17 17 F -> C (in dbSNP:rs194520).
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:12095985,
ECO:0000269|PubMed:12429817,
ECO:0000269|PubMed:12975309,
ECO:0000269|Ref.3}.
/FTId=VAR_060387.
VARIANT 40 40 D -> Y (in dbSNP:rs17863046).
/FTId=VAR_060388.
VARIANT 214 214 G -> E (in dbSNP:rs13228098).
/FTId=VAR_057727.
VARIANT 456 456 R -> Q (in dbSNP:rs194524).
{ECO:0000269|PubMed:12429817}.
/FTId=VAR_057728.
VARIANT 475 475 M -> I (in dbSNP:rs194525).
{ECO:0000269|PubMed:12095985,
ECO:0000269|PubMed:12429817,
ECO:0000269|PubMed:12690205,
ECO:0000269|Ref.7}.
/FTId=VAR_060389.
CONFLICT 17 17 F -> V (in Ref. 2; AAN04080).
{ECO:0000305}.
CONFLICT 211 211 L -> F (in Ref. 1; AAG32148/AAG32149).
{ECO:0000305}.
SEQUENCE 490 AA; 56056 MW; DB12E252DE3F4CAF CRC64;
MESISMMGSP KSLSETFLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS
RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM
RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE
LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA
RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ
CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY
ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE
EEYYRFYTPP NFVLALVLPS IVILGKIILF LPCISRKLKR IKKGWEKSQF LEEGMGGTIP
HVSPERVTVM


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