ID A0A2Y9E9X4_TRIMA Unreviewed; 488 AA.
AC A0A2Y9E9X4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Metalloreductase STEAP3 {ECO:0000313|RefSeq:XP_004389738.1};
GN Name=LOC101358900 {ECO:0000313|RefSeq:XP_004389738.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004389738.1};
RN [1] {ECO:0000313|RefSeq:XP_004389738.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_004389738.1; XM_004389681.1.
DR AlphaFoldDB; A0A2Y9E9X4; -.
DR STRING; 127582.A0A2Y9E9X4; -.
DR GeneID; 101358900; -.
DR KEGG; tmu:101358900; -.
DR InParanoid; A0A2Y9E9X4; -.
DR OrthoDB; 5361at2759; -.
DR Proteomes; UP000248480; Unplaced.
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: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:UP000248480};
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 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..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..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..117
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"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 54323 MW; 519D972065D68A61 CRC64;
MSGDMDKPLI SHHLPDSNSG LTEAPPEAPR VGILGSGDFA RSLATRLVAS GFSVVVGSRN
PKRTAGLFPS TVHVTFQAEA VSSAEIIFVA VFREYYSSLC VLSDQLAGKI LVDVSNPTEQ
EHRQHQQSNA EYLASLFPTC TVVKAFNVIS AWTLQAGPRD GNRQVPICSN QLEAKRTVSE
LVLAMGFSPV DMGSLVSARE VEAMPLRLLP GWKVPTLLAL GLFICFYIYN FVRDVLQPYV
QEGKSKFYKL PVSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLWRGTKYLR FPDWLDHWLQ
HRKQIGLLSF FCAALHALYS FCLPLRRAYR YDLVNLAVEQ VLADNSYLWK EEEVWRLEIY
LSLGILALGM LSLLAVTSLP SIANSLSWRE FSFVQSTLGF VALVLSTLHT LTYGWARAFQ
ESSYKFYLPP TFTLTLLLPC AIILARGLLL LPCCSRRLAR IRRGWEKAGA AQFPLPEDHS
FAQKTSHV
//
