ID A0A2K6BA74_MACNE Unreviewed; 490 AA.
AC A0A2K6BA74;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=STEAP2 metalloreductase {ECO:0000313|Ensembl:ENSMNEP00000008327.1};
GN Name=STEAP2 {ECO:0000313|Ensembl:ENSMNEP00000008327.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000008327.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000008327.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011729019.1; XM_011730717.1.
DR RefSeq; XP_011729020.1; XM_011730718.1.
DR RefSeq; XP_011729021.1; XM_011730719.1.
DR AlphaFoldDB; A0A2K6BA74; -.
DR STRING; 9545.ENSMNEP00000008327; -.
DR Ensembl; ENSMNET00000032494.1; ENSMNEP00000008327.1; ENSMNEG00000028663.1.
DR GeneID; 105475467; -.
DR KEGG; mni:105475467; -.
DR CTD; 261729; -.
DR GeneTree; ENSGT00390000008042; -.
DR OrthoDB; 5361at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000028663; Expressed in pituitary gland and 11 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IEA:Ensembl.
DR GO; GO:0008823; F:cupric reductase activity; IEA:Ensembl.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:Ensembl.
DR GO; GO:0015677; P:copper ion import; IEA:Ensembl.
DR GO; GO:0098705; P:copper ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:Ensembl.
DR GO; GO:0098711; P:iron ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0045055; P:regulated exocytosis; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
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:UP000233120};
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 TRANSMEM 391..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..454
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..404
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
SQ SEQUENCE 490 AA; 56007 MW; 225E3F95026DF49C CRC64;
MESISMMGSP KSLSETFLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS
RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM
RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE
LARQLNFIPV DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA
RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ
CRKQLGLLSF FFTVVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY
ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE
EEYYRFYTPP NFVLALVLPS VVILGKIILF LPCISRKLKR IKKGWEKSQF LEEGIGGTIP
HVSPERVTVM
//
