STEA1_HUMAN
ID STEA1_HUMAN Reviewed; 339 AA.
AC Q9UHE8; A4D1E0; O95034;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Metalloreductase STEAP1;
DE EC=1.16.1.-;
DE AltName: Full=Six-transmembrane epithelial antigen of prostate 1;
GN Name=STEAP1; Synonyms=PRSS24, STEAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10588738; DOI=10.1073/pnas.96.25.14523;
RA Hubert R.S., Vivanco I., Chen E., Rastegar S., Leong K., Mitchell S.C.,
RA Madraswala R., Zhou Y., Kuo J., Raitano A.B., Jakobovits A., Saffran D.C.,
RA Afar D.E.H.;
RT "STEAP: a prostate-specific cell-surface antigen highly expressed in human
RT prostate tumors.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14523-14528(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-47.
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16609065; DOI=10.1182/blood-2006-02-003681;
RA Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.;
RT "The Steap proteins are metalloreductases.";
RL Blood 108:1388-1394(2006).
CC -!- FUNCTION: Metalloreductase that has the ability to reduce both Fe(3+)
CC to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor.
CC {ECO:0000250|UniProtKB:Q9CWR7}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9CWR7};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9CWR7}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC prostate tumors. {ECO:0000269|PubMed:16609065}.
CC -!- SIMILARITY: Belongs to the STEAP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/STEAP1ID44482ch7q21.html";
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DR EMBL; AF186249; AAF17479.1; -; mRNA.
DR EMBL; AC005053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004969; AAD15620.2; -; Genomic_DNA.
DR EMBL; CH236949; EAL24167.1; -; Genomic_DNA.
DR EMBL; BC011802; AAH11802.1; -; mRNA.
DR CCDS; CCDS5614.1; -.
DR RefSeq; NP_036581.1; NM_012449.2.
DR PDB; 6Y9B; EM; 2.97 A; A/B/C=2-339.
DR PDBsum; 6Y9B; -.
DR AlphaFoldDB; Q9UHE8; -.
DR SMR; Q9UHE8; -.
DR BioGRID; 117921; 12.
DR IntAct; Q9UHE8; 3.
DR STRING; 9606.ENSP00000297205; -.
DR ChEMBL; CHEMBL3712956; -.
DR TCDB; 5.B.6.1.4; the transmembrane epithelial antigen protein-3 ferric reductase (steap) family.
DR iPTMnet; Q9UHE8; -.
DR PhosphoSitePlus; Q9UHE8; -.
DR SwissPalm; Q9UHE8; -.
DR BioMuta; STEAP1; -.
DR DMDM; 12643440; -.
DR EPD; Q9UHE8; -.
DR jPOST; Q9UHE8; -.
DR MassIVE; Q9UHE8; -.
DR MaxQB; Q9UHE8; -.
DR PaxDb; Q9UHE8; -.
DR PeptideAtlas; Q9UHE8; -.
DR PRIDE; Q9UHE8; -.
DR ProteomicsDB; 84335; -.
DR ABCD; Q9UHE8; 1 sequenced antibody.
DR Antibodypedia; 4048; 417 antibodies from 35 providers.
DR DNASU; 26872; -.
DR Ensembl; ENST00000297205.7; ENSP00000297205.2; ENSG00000164647.9.
DR GeneID; 26872; -.
DR KEGG; hsa:26872; -.
DR MANE-Select; ENST00000297205.7; ENSP00000297205.2; NM_012449.3; NP_036581.1.
DR UCSC; uc003ujx.3; human.
DR CTD; 26872; -.
DR DisGeNET; 26872; -.
DR GeneCards; STEAP1; -.
DR HGNC; HGNC:11378; STEAP1.
DR HPA; ENSG00000164647; Tissue enhanced (prostate).
DR MIM; 604415; gene.
DR neXtProt; NX_Q9UHE8; -.
DR OpenTargets; ENSG00000164647; -.
DR PharmGKB; PA36193; -.
DR VEuPathDB; HostDB:ENSG00000164647; -.
DR eggNOG; ENOG502QWI9; Eukaryota.
DR GeneTree; ENSGT00390000008042; -.
DR HOGENOM; CLU_034618_0_0_1; -.
DR InParanoid; Q9UHE8; -.
DR OMA; KWHLPMK; -.
DR OrthoDB; 638341at2759; -.
DR PhylomeDB; Q9UHE8; -.
DR TreeFam; TF332031; -.
DR PathwayCommons; Q9UHE8; -.
DR SignaLink; Q9UHE8; -.
DR BioGRID-ORCS; 26872; 18 hits in 999 CRISPR screens.
DR ChiTaRS; STEAP1; human.
DR GeneWiki; STEAP1; -.
DR GenomeRNAi; 26872; -.
DR Pharos; Q9UHE8; Tbio.
DR PRO; PR:Q9UHE8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UHE8; protein.
DR Bgee; ENSG00000164647; Expressed in pericardium and 153 other tissues.
DR ExpressionAtlas; Q9UHE8; baseline and differential.
DR Genevisible; Q9UHE8; HS.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR Pfam; PF01794; Ferric_reduct; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Electron transport; Endosome; FAD; Flavoprotein;
KW Heme; Ion transport; Iron; Iron transport; Membrane; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..339
FT /note="Metalloreductase STEAP1"
FT /id="PRO_0000191694"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 118..265
FT /note="Ferric oxidoreductase"
FT BINDING 140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 175
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 268
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT VARIANT 47
FT /note="H -> Q (in dbSNP:rs4015375)"
FT /evidence="ECO:0000269|PubMed:12690205"
FT /id="VAR_053696"
FT VARIANT 169
FT /note="F -> L (in dbSNP:rs2888782)"
FT /id="VAR_053697"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 72..93
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 114..143
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 161..180
FT /evidence="ECO:0007829|PDB:6Y9B"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 186..201
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 210..235
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 247..272
FT /evidence="ECO:0007829|PDB:6Y9B"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6Y9B"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:6Y9B"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:6Y9B"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:6Y9B"
SQ SEQUENCE 339 AA; 39851 MW; 55443A170C870387 CRC64;
MESRKDITNQ EELWKMKPRR NLEEDDYLHK DTGETSMLKR PVLLHLHQTA HADEFDCPSE
LQHTQELFPQ WHLPIKIAAI IASLTFLYTL LREVIHPLAT SHQQYFYKIP ILVINKVLPM
VSITLLALVY LPGVIAAIVQ LHNGTKYKKF PHWLDKWMLT RKQFGLLSFF FAVLHAIYSL
SYPMRRSYRY KLLNWAYQQV QQNKEDAWIE HDVWRMEIYV SLGIVGLAIL ALLAVTSIPS
VSDSLTWREF HYIQSKLGIV SLLLGTIHAL IFAWNKWIDI KQFVWYTPPT FMIAVFLPIV
VLIFKSILFL PCLRKKILKI RHGWEDVTKI NKTEICSQL
