STEA2_MOUSE
ID STEA2_MOUSE Reviewed; 489 AA.
AC Q8BWB6; Q3TS12;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Metalloreductase STEAP2;
DE EC=1.16.1.-;
DE AltName: Full=Six-transmembrane epithelial antigen of prostate 2;
GN Name=Steap2;
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; TISSUE=Epididymis, and Head;
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 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. 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; AK052981; BAC35230.1; -; mRNA.
DR EMBL; AK162343; BAE36864.1; -; mRNA.
DR CCDS; CCDS39007.1; -.
DR RefSeq; NP_001096626.1; NM_001103156.2.
DR RefSeq; NP_001096627.1; NM_001103157.2.
DR RefSeq; NP_001272398.1; NM_001285469.1.
DR RefSeq; NP_001272399.1; NM_001285470.1.
DR RefSeq; NP_083010.2; NM_028734.5.
DR RefSeq; XP_011238977.1; XM_011240675.2.
DR AlphaFoldDB; Q8BWB6; -.
DR SMR; Q8BWB6; -.
DR BioGRID; 216452; 1.
DR STRING; 10090.ENSMUSP00000111084; -.
DR iPTMnet; Q8BWB6; -.
DR PhosphoSitePlus; Q8BWB6; -.
DR MaxQB; Q8BWB6; -.
DR PaxDb; Q8BWB6; -.
DR PRIDE; Q8BWB6; -.
DR ProteomicsDB; 257488; -.
DR Antibodypedia; 29828; 214 antibodies from 30 providers.
DR Ensembl; ENSMUST00000015797; ENSMUSP00000015797; ENSMUSG00000015653.
DR Ensembl; ENSMUST00000115424; ENSMUSP00000111084; ENSMUSG00000015653.
DR Ensembl; ENSMUST00000115425; ENSMUSP00000111085; ENSMUSG00000015653.
DR Ensembl; ENSMUST00000115426; ENSMUSP00000111086; ENSMUSG00000015653.
DR Ensembl; ENSMUST00000164219; ENSMUSP00000132501; ENSMUSG00000015653.
DR GeneID; 74051; -.
DR KEGG; mmu:74051; -.
DR UCSC; uc008wiw.3; mouse.
DR CTD; 261729; -.
DR MGI; MGI:1921301; Steap2.
DR VEuPathDB; HostDB:ENSMUSG00000015653; -.
DR eggNOG; ENOG502QVSJ; Eukaryota.
DR GeneTree; ENSGT00390000008042; -.
DR InParanoid; Q8BWB6; -.
DR OMA; AKTNIIF; -.
DR OrthoDB; 638341at2759; -.
DR PhylomeDB; Q8BWB6; -.
DR TreeFam; TF332031; -.
DR Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR BioGRID-ORCS; 74051; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Steap2; mouse.
DR PRO; PR:Q8BWB6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BWB6; protein.
DR Bgee; ENSMUSG00000015653; Expressed in choroid plexus epithelium and 204 other tissues.
DR ExpressionAtlas; Q8BWB6; baseline and differential.
DR Genevisible; Q8BWB6; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
DR GO; GO:0008823; F:cupric reductase activity; IDA:MGI.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015677; P:copper ion import; IDA:MGI.
DR GO; GO:0098705; P:copper ion import across plasma membrane; IDA:MGI.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
DR GO; GO:0098706; P:iron ion import across cell outer membrane; IDA:MGI.
DR GO; GO:0098711; P:iron ion import across plasma membrane; IDA:MGI.
DR GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB.
DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Copper; Electron transport; Endosome; FAD; Flavoprotein;
KW Heme; Ion transport; Iron; Iron transport; Membrane; Metal-binding; NAD;
KW NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..489
FT /note="Metalloreductase STEAP2"
FT /id="PRO_0000191698"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 258..406
FT /note="Ferric oxidoreductase"
FT BINDING 37..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 59..60
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 92..99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 117
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 150
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 315
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 377
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 394
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 408
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 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 489 AA; 55760 MW; 98CD63D59DDDF24C CRC64;
MESISMMGSP KSLETFLPNG INGIKDARQV TVGVIGSGDF AKSLTIRLIR CGYHVVIGSR
NPKFASEFFP HVVDVTHHED ALTKTNIIFV AIHREHYTSL WDLRHLLVGK ILIDVSNNMR
VNQYPESNAE YLASLFPDSL IVKGFNVISA WALQLGPKDA SRQVYICSNN IQARQQVIEL
ARQLNFIPVD LGSLSSAKEI ENLPLRLFTL WRGPVVVAIS LATFFFLYSF VRDVIHPYAR
NQQSDFYKIP IEIVNKTLPI VAITLLSLVY LAGLLAAAYQ LYYGTKYRRF PPWLDTWLQC
RKQLGLLSFF FAVVHVAYSL CLPMRRSERY LFLNMAYQQV HANIENAWNE EEVWRIEMYI
SFGIMSLGLL SLLAVTSIPS VSNALNWREF SFIQSTLGYV ALLITTFHVL IYGWKRAFAE
EYYRFYTPPN FVLALVLPSI VILGKMILLL PCISRKLKRI KKGWEKSQFL DEGMGGAVPH
LSPERVTVM
