ID A0A452FDC7_CAPHI Unreviewed; 521 AA.
AC A0A452FDC7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=STEAP3 metalloreductase {ECO:0000313|Ensembl:ENSCHIP00000022374.1};
GN Name=STEAP3 {ECO:0000313|Ensembl:ENSCHIP00000022374.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000022374.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000022374.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000022374.1}
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 EMBL; LWLT01000002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005676308.1; XM_005676251.3.
DR AlphaFoldDB; A0A452FDC7; -.
DR SMR; A0A452FDC7; -.
DR STRING; 9925.ENSCHIP00000022374; -.
DR Ensembl; ENSCHIT00000030234.1; ENSCHIP00000022374.1; ENSCHIG00000020375.1.
DR GeneID; 102181998; -.
DR KEGG; chx:102181998; -.
DR CTD; 55240; -.
DR GeneTree; ENSGT00390000008042; -.
DR OrthoDB; 5361at2759; -.
DR Proteomes; UP000291000; Chromosome 2.
DR Bgee; ENSCHIG00000020375; Expressed in liver and 16 other cell types or tissues.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; 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:SF8; METALLOREDUCTASE STEAP3; 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:UP000291000};
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 247..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..150
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 294..438
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 57968 MW; EA73E3B51F3F0AD4 CRC64;
MKSGQLASRA PAPGCSKSLD MEDSPLHPQS ATRTSGKMDK PLISHHLVDS DGSLAEAPSE
VPKVGILGSG DFARSLATRL VGSGFSVVVG SRNPKRMAGL FPSAAQLTFQ EEAVGSPEVI
FVAMFREHYS TLCGLSDQLS GKILVDVSNP TEQEHLQHHE SNAEYLASLF PTCAVVKAFN
VISAWTLQSG PRDGNRQVPI CSDQPEAKRT VLEMVRAMGF TPVDMGSLAS AREVEAMPLR
LFLGWKVPAL LALGLFIFFY AYNFVRDVLE PYVQEGKNKF YKLPVLVVNT TLPCVAYVLL
SLVYLPGVLA AALQLRRGTK YQRFPDWLDH WLQHRKQMGL LSFFCAALHA VYSLCLPLRR
SHRYELVNLA IKQVLTNKSH IWNEEEVWRM EIYLSLGVLA LGMLSLLAVT SLPSIANSLN
WREFSFVQST LGFVALVLST LHTLTYGWTR AFEESRYKFF LPPTFTLTLL VPCVIILAKG
LFLLPCVSRR LTKIRRGWEK DGSVRFTLPV DHTLAQKTSH V
//
