STEA1_MOUSE
ID STEA1_MOUSE Reviewed; 339 AA.
AC Q9CWR7; Q6P8X4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Metalloreductase STEAP1;
DE EC=1.16.1.-;
DE AltName: Full=Six-transmembrane epithelial antigen of prostate 1;
GN Name=Steap1; Synonyms=Steap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
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:0000269|PubMed:16609065}.
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:0000269|PubMed:16609065};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16609065}.
CC -!- SIMILARITY: Belongs to the STEAP family. {ECO:0000305}.
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DR EMBL; AK010437; BAB26938.1; -; mRNA.
DR EMBL; BC061023; AAH61023.1; -; mRNA.
DR CCDS; CCDS19077.1; -.
DR RefSeq; NP_081675.2; NM_027399.3.
DR AlphaFoldDB; Q9CWR7; -.
DR SMR; Q9CWR7; -.
DR BioGRID; 213999; 1.
DR STRING; 10090.ENSMUSP00000015796; -.
DR iPTMnet; Q9CWR7; -.
DR PhosphoSitePlus; Q9CWR7; -.
DR MaxQB; Q9CWR7; -.
DR PaxDb; Q9CWR7; -.
DR PRIDE; Q9CWR7; -.
DR ProteomicsDB; 258663; -.
DR DNASU; 70358; -.
DR Ensembl; ENSMUST00000015796; ENSMUSP00000015796; ENSMUSG00000015652.
DR GeneID; 70358; -.
DR KEGG; mmu:70358; -.
DR UCSC; uc008wjb.2; mouse.
DR CTD; 26872; -.
DR MGI; MGI:1917608; Steap1.
DR VEuPathDB; HostDB:ENSMUSG00000015652; -.
DR eggNOG; ENOG502QWI9; Eukaryota.
DR GeneTree; ENSGT00390000008042; -.
DR HOGENOM; CLU_034618_0_0_1; -.
DR InParanoid; Q9CWR7; -.
DR OMA; KWHLPMK; -.
DR OrthoDB; 638341at2759; -.
DR PhylomeDB; Q9CWR7; -.
DR TreeFam; TF332031; -.
DR BioGRID-ORCS; 70358; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Steap1; mouse.
DR PRO; PR:Q9CWR7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CWR7; protein.
DR Bgee; ENSMUSG00000015652; Expressed in choroid plexus epithelium and 143 other tissues.
DR ExpressionAtlas; Q9CWR7; baseline and differential.
DR Genevisible; Q9CWR7; MM.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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 Copper; Electron transport; Endosome; FAD; Flavoprotein; Heme;
KW Ion transport; Iron; Iron transport; Membrane; Metal-binding; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..339
FT /note="Metalloreductase STEAP1"
FT /id="PRO_0000191695"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
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 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 118..265
FT /note="Ferric oxidoreductase"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT CONFLICT 161
FT /note="R -> K (in Ref. 1; BAB26938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 39292 MW; BF63B35AEE4356A0 CRC64;
MEISDDVTNP EQLWKMKPKG NLEDDSYSTK DSGETSMLKR PGLSHLQHAV HVDAFDCPSE
LQHTQEFFPN WRLPVKVAAI ISSLTFLYTL LREIIYPLVT SREQYFYKIP ILVINKVLPM
VAITLLALVY LPGELAAVVQ LRNGTKYKKF PPWLDRWMLA RKQFGLLSFF FAVLHAVYSL
SYPMRRSYRY KLLNWAYKQV QQNKEDAWVE HDVWRMEIYV SLGIVGLAIL ALLAVTSIPS
VSDSLTWREF HYIQSKLGIV SLLLGTVHAL VFAWNKWVDV SQFVWYMPPT FMIAVFLPTL
VLICKIALCL PCLRKKILKI RCGWEDVSKI NRTEMASRL
