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Database: UniProt
Entry: I3MKH8_ICTTR
LinkDB: I3MKH8_ICTTR
Original site: I3MKH8_ICTTR 
ID   I3MKH8_ICTTR            Unreviewed;       403 AA.
AC   I3MKH8;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=STEAP2 metalloreductase {ECO:0000313|Ensembl:ENSSTOP00000011799.3};
GN   Name=STEAP2 {ECO:0000313|Ensembl:ENSSTOP00000011799.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000011799.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000011799.3}
RP   IDENTIFICATION.
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=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   EMBL; AGTP01078541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3MKH8; -.
DR   Ensembl; ENSSTOT00000013163.3; ENSSTOP00000011799.3; ENSSTOG00000013165.3.
DR   GeneTree; ENSGT00390000008042; -.
DR   HOGENOM; CLU_034618_1_1_1; -.
DR   TreeFam; TF332031; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
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   3: Inferred from homology;
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, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022496}.
FT   TRANSMEM        211..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..119
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          261..402
FT                   /note="Ferric oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01794"
SQ   SEQUENCE   403 AA;  46036 MW;  389B44920D9A710B CRC64;
     MESISMMGSP KSLSETFLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS
     RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM
     RINQYPESNA EYLASLFPDS LIVKGFNVIS AWALQLGPKD ASRQVYICSN NIQARQQVIE
     LARQLNFIPV DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLSTFFFLYS FVRDVIHPYA
     RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ
     CRKQLGLLSY FFTVVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY
     ISFGIMSLGL LSLLAVTSIP SVSSALNWRE FSFIQWPGAA LFY
//
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