ID   D4A6H3_RAT              Unreviewed;       489 AA.
AC   D4A6H3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=STEAP2 metalloreductase {ECO:0000313|Ensembl:ENSRNOP00000007977.5};
GN   Name=Steap2 {ECO:0000313|Ensembl:ENSRNOP00000007977.5,
GN   ECO:0000313|RGD:1307050};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000007977.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000007977.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007977.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000007977.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000007977.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Cu(+) + H(+) + NADP(+) = 2 Cu(2+) + NADPH;
CC         Xref=Rhea:RHEA:71771, ChEBI:CHEBI:15378, ChEBI:CHEBI:29036,
CC         ChEBI:CHEBI:49552, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|ARBA:ARBA00036664};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71773;
CC         Evidence={ECO:0000256|ARBA:ARBA00036664};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(2+) + H(+) + NADP(+) = 2 Fe(3+) + NADPH;
CC         Xref=Rhea:RHEA:71767, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|ARBA:ARBA00035766};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71769;
CC         Evidence={ECO:0000256|ARBA:ARBA00035766};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004337}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the STEAP family.
CC       {ECO:0000256|ARBA:ARBA00007729}.
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DR   RefSeq; NP_001101316.1; NM_001107846.1.
DR   RefSeq; XP_006236094.1; XM_006236032.3.
DR   RefSeq; XP_006236096.1; XM_006236034.3.
DR   RefSeq; XP_006236097.1; XM_006236035.2.
DR   RefSeq; XP_006236098.1; XM_006236036.3.
DR   RefSeq; XP_008760925.1; XM_008762703.2.
DR   AlphaFoldDB; D4A6H3; -.
DR   SMR; D4A6H3; -.
DR   STRING; 10116.ENSRNOP00000007977; -.
DR   PhosphoSitePlus; D4A6H3; -.
DR   PaxDb; 10116-ENSRNOP00000007977; -.
DR   Ensembl; ENSRNOT00000007977.6; ENSRNOP00000007977.5; ENSRNOG00000006076.6.
DR   GeneID; 312052; -.
DR   KEGG; rno:312052; -.
DR   UCSC; RGD:1307050; rat.
DR   AGR; RGD:1307050; -.
DR   CTD; 261729; -.
DR   RGD; 1307050; Steap2.
DR   eggNOG; ENOG502QVSJ; Eukaryota.
DR   GeneTree; ENSGT00390000008042; -.
DR   HOGENOM; CLU_034618_1_1_1; -.
DR   OMA; HPYVKNQ; -.
DR   OrthoDB; 5361at2759; -.
DR   TreeFam; TF332031; -.
DR   Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000006076; Expressed in adult mammalian kidney and 17 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005769; C:early endosome; ISO:RGD.
DR   GO; GO:0005768; C:endosome; ISO:RGD.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:RGD.
DR   GO; GO:0008823; F:cupric reductase activity; ISO:RGD.
DR   GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; ISO:RGD.
DR   GO; GO:0015677; P:copper ion import; ISO:RGD.
DR   GO; GO:0098705; P:copper ion import across plasma membrane; ISO:RGD.
DR   GO; GO:0006897; P:endocytosis; ISO:RGD.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:RGD.
DR   GO; GO:0098711; P:iron ion import across plasma membrane; ISO:RGD.
DR   GO; GO:0045055; P:regulated exocytosis; ISO:RGD.
DR   GO; GO:0009725; P:response to hormone; ISO:RGD.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   PANTHER; PTHR14239; DUDULIN-RELATED; 1.
DR   PANTHER; PTHR14239:SF6; METALLOREDUCTASE STEAP2; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022496};
KW   Iron {ECO:0000256|ARBA:ARBA00022496};
KW   Iron transport {ECO:0000256|ARBA:ARBA00022496};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022496}.
FT   DOMAIN          31..118
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          260..404
FT                   /note="Ferric oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01794"
SQ   SEQUENCE   489 AA;  55792 MW;  604FC17BCD76BBD2 CRC64;
     MESISMMGSP KTLETFLPNG INGIKDARKV TVGVIGSGDF AKSLTIRLIR CGYHVVIGSR
     NPKFASEFFP HVVDVTHHED ALTKTNIIFV AIHREHYTSL WDLRHLLVGK VLIDVSNNMR
     VNQYPESNAE YLASLFPDSL IVKGFNVISA WALQLGPKDA SRQVYICSNN IQARQQVIEL
     ARQLNFIPVD LGSLSSAKEI ENLPLRLFTL WRGPVVVAIS LATFFFIYSF VRDVIHPYAR
     NQQSDFYKIP IEIVNKTLPI VAITLLSLVY LAGLLAAAYQ LYYGTKYRRF PPWLDTWLQC
     RKQLGLLSFF FAVVHVAYSL CLPMRRSERY LFLNMAYQQV HANIENAWNE EEVWRIEMYI
     SFGIMSLGLL SLLAVTSIPS VSNALNWREF SFIQSTLGYV ALLITTFHVL IYGWKRAFAE
     EYYRFYTPPN FVLALVLPSI VLLGKMMLLL PCIGRKLKRI KKGWEKSQFL EEGMGGTVPH
     LSPERVTVM
//