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Database: UniProt
Entry: L5JQE7_PTEAL
LinkDB: L5JQE7_PTEAL
Original site: L5JQE7_PTEAL 
ID   L5JQE7_PTEAL            Unreviewed;       552 AA.
AC   L5JQE7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Metalloreductase STEAP2 {ECO:0000313|EMBL:ELK00971.1};
GN   ORFNames=PAL_GLEAN10013625 {ECO:0000313|EMBL:ELK00971.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK00971.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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; KB031154; ELK00971.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5JQE7; -.
DR   STRING; 9402.L5JQE7; -.
DR   eggNOG; ENOG502QVSJ; Eukaryota.
DR   InParanoid; L5JQE7; -.
DR   Proteomes; UP000010552; 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:UP000010552};
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        273..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        367..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        453..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        494..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          94..181
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          323..466
FT                   /note="Ferric oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01794"
SQ   SEQUENCE   552 AA;  62778 MW;  C9F047D7DEB9FA83 CRC64;
     MRKKAHQKFE RLGLQDIIRT SGNALILCLA SYHDIDITVT LTYHLPPLGP QDIPGDLGRI
     HIMESISMMG SPKSLSATFL PNGINGIKDA RKVTVGVIGS GDFAKSLTIR LIRCGYHVVI
     GSRNPKFASE FFPHVVDVTH HEDALTKTNI IFVAIHREHY TSLWDLRHLL VGKILIDVSN
     NMRLNQYPES NAEYLASLFP DSLIVKGFNV ISAWALQLGP KDASRQVYIC SNNIQARQQV
     IELARQLNFI PVDLGSLSSA REIENLPLRL FTLWRGPVVV AISLATFFFL YSFVRDVIHP
     YARNQQSDFY KIPIEIVNKT LPIVAITLLS LVYLAGLLAA AYQLYYGTKY RRFPPWLETW
     LQCRKQLGLL SFFFASVHVA YSLCLPMRRS ERYLFLNMAY QQVHANIENS WNEEEVWRIE
     MYISFGIMSL GLLSLLAVTS IPSVSNALNW REFSFIQSTL GYVALLISTF HVLTYGWKRA
     FEEEYYRFYT PPNFVLALVL PSIVILGKSI LLLPCVSRKL KKIKKGWEKS QFLEESIGGA
     VPHLSPERVT VM
//
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