ID F1CNZ4_PIG Unreviewed; 470 AA.
AC F1CNZ4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Metalloreductase STEAP4 {ECO:0000313|EMBL:HCZ74549.1};
DE SubName: Full=STEAP family member 4 {ECO:0000313|EMBL:ADX43860.1};
DE SubName: Full=STEAP4 metalloreductase {ECO:0000313|Ensembl:ENSSSCP00000016224.2};
GN Name=STEAP4 {ECO:0000313|EMBL:ADX43860.1,
GN ECO:0000313|Ensembl:ENSSSCP00000016224.2,
GN ECO:0000313|VGNC:VGNC:93544};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016224.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000016224.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016224.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADX43860.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=White adipose {ECO:0000313|EMBL:ADX43860.1};
RX PubMed=23262293; DOI=10.1016/j.biocel.2012.12.011;
RA Wang S.B., Lei T., Zhou L.L., Zheng H.L., Zeng C.P., Liu N., Yang Z.Q.,
RA Chen X.D.;
RT "Functional analysis and transcriptional regulation of porcine six
RT transmembrane epithelial antigen of prostate 4 (STEAP4) gene and its novel
RT variant in hepatocytes.";
RL Int. J. Biochem. Cell Biol. 45:612-620(2013).
RN [3] {ECO:0000313|EMBL:HCZ74549.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [4] {ECO:0000313|Ensembl:ENSSSCP00000016224.2}
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; HQ533145; ADX43860.1; -; Genomic_DNA.
DR EMBL; DQIR01019074; HCZ74549.1; -; Transcribed_RNA.
DR STRING; 9823.ENSSSCP00000016224; -.
DR PaxDb; 9823-ENSSSCP00000016224; -.
DR Ensembl; ENSSSCT00000016670.5; ENSSSCP00000016224.2; ENSSSCG00000015299.5.
DR VGNC; VGNC:93544; STEAP4.
DR eggNOG; ENOG502R746; Eukaryota.
DR GeneTree; ENSGT00390000008042; -.
DR HOGENOM; CLU_034618_1_1_1; -.
DR OMA; GWERNPK; -.
DR TreeFam; TF332031; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Bgee; ENSSSCG00000015299; Expressed in blood and 30 other cell types or tissues.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008823; F:cupric reductase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR GO; GO:0015677; P:copper ion import; IBA:GO_Central.
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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:F1CNZ4};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
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 202..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..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 348..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..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 251..394
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
SQ SEQUENCE 470 AA; 53367 MW; CC6460375618010B CRC64;
MEKTSTDTLP LTMISSEKQE TVCIFGTGDF GRSLGLKMLQ CGYSIVFGSR NPGMSSLLPS
GAEVLNYSEA AQKSDIIILT VHREHYDFLT HLTEVLNGKI LVDVSNNLKI NQYPESNAEY
LAQLLPGAHV VKAFNTISAW ALQSGALDAS RQVFVCGNDR KAKQRVMDIV RTLGLTPLDK
GSLMAAKEIE NYPLQLFPMW KFPFRLSAVL CVFFFFYSVI RDVIYPYVYE RKDNTFRLAI
SIPNHIFPNT ALTLLALVYL PGVLAAILQL YRGTKYRRFP DWLDHWMLCR KQLGLVALGF
AFLHVLYTLV IPIRYYVRWR MNNRTVVQAI AKKENPFIIS TAWLSDSYLA LGILGFFLFV
LLGITSLPSV SNMVNWREFR FVQSKLGYLT LILCTAHTLV YGGRRFLDPS TLKWCLPSAY
VIALIIPCTL LVVKFILILP CIDKPLTRIR QGWERNPKFL ESALNGKTDL
//
