ID K7FTA0_PELSI Unreviewed; 472 AA.
AC K7FTA0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=STEAP4 metalloreductase {ECO:0000313|Ensembl:ENSPSIP00000011260.1};
GN Name=STEAP4 {ECO:0000313|Ensembl:ENSPSIP00000011260.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000011260.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000011260.1}
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; AGCU01158651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01158652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01158653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01158654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006134172.1; XM_006134110.2.
DR RefSeq; XP_006134173.1; XM_006134111.2.
DR AlphaFoldDB; K7FTA0; -.
DR STRING; 13735.ENSPSIP00000011260; -.
DR Ensembl; ENSPSIT00000011316.1; ENSPSIP00000011260.1; ENSPSIG00000010182.1.
DR GeneID; 102454498; -.
DR KEGG; pss:102454498; -.
DR CTD; 79689; -.
DR eggNOG; ENOG502R746; Eukaryota.
DR GeneTree; ENSGT00390000008042; -.
DR HOGENOM; CLU_034618_1_1_1; -.
DR OMA; GWERNPK; -.
DR OrthoDB; 5361at2759; -.
DR TreeFam; TF332031; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0008823; F:cupric reductase activity; IEA:Ensembl.
DR GO; GO:0009055; F:electron transfer activity; 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:0015677; P:copper ion import; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0033212; P:iron import into cell; IEA:Ensembl.
DR GO; GO:0070207; P:protein homotrimerization; 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:SF5; METALLOREDUCTASE STEAP4; 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:UP000007267};
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 204..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..107
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 249..394
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
SQ SEQUENCE 472 AA; 53455 MW; BC452E63EAB69D4D CRC64;
MEKNSSNMIP LAENSPNKQE TVCIFGTGDF GRSLGYKMLQ CGYSIVFGSR NAQTSSLIPK
GAEVLSHGEA AHKADIIIVA IQRQHYNFLT ELSDVLHGKV LVDVSNNLKI NQYPESNAEY
LAQLVPGAKV VKAFNTVSAW ALQSGTLDAS RQVFICGNDN KAKQMVMDIV RTLGLTPLDQ
GSLVAAKEIE NYPLQLFPMW KFPIYLAIGL SVFFFFYCLI REVIYPYVYE NKDVSFFIAI
TIPNRVCPIV ALILLALVYL PGIIAAILQL HRGTKYSRFP DWLDKWMLCR KQLGLVALVF
AFLHVLYTLV IPIRYYVRWR INVYVISQVK DNRTDPFYNT NGWISDSYVA LGILGFFLFI
LLGITSLPSV SNSVNWREFR FVQSKLGYLT LILCTAHTLV YGGKRFLSPS MYKWYLPAAY
MLSLIVPCFV LAIKFVLIFP CIDRPLTQIR QGWERNSKGS EQSHYNDSKS AV
//
