STEA1_PIG
ID STEA1_PIG Reviewed; 338 AA.
AC Q9GL50;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Metalloreductase STEAP1;
DE EC=1.16.1.-;
DE AltName: Full=Six transmembrane endothelial antigen of PAEC;
DE AltName: Full=Six-transmembrane epithelial antigen of prostate 1;
GN Name=STEAP1; Synonyms=STEAP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nagasaka T., Boulday G., Coupel S., Coulon F., Tesson L., Heslan J.-M.,
RA Soulillou J.-P., Charreau B.;
RT "Differential gene expression in endothelial cells during TNF-alpha- and
RT LPS-mediated activation.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metalloreductase that has the ability to reduce both Fe(3+)
CC to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor.
CC {ECO:0000250|UniProtKB:Q9CWR7}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q9CWR7};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9CWR7}.
CC -!- SIMILARITY: Belongs to the STEAP family. {ECO:0000305}.
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DR EMBL; AF319659; AAG33868.1; -; mRNA.
DR RefSeq; NP_999470.1; NM_214305.1.
DR RefSeq; XP_003484352.3; XM_003484304.3.
DR AlphaFoldDB; Q9GL50; -.
DR SMR; Q9GL50; -.
DR STRING; 9823.ENSSSCP00000016226; -.
DR PaxDb; Q9GL50; -.
DR Ensembl; ENSSSCT00000016672; ENSSSCP00000016226; ENSSSCG00000015301.
DR Ensembl; ENSSSCT00025069196; ENSSSCP00025029798; ENSSSCG00025050671.
DR Ensembl; ENSSSCT00055035290; ENSSSCP00055028026; ENSSSCG00055018019.
DR GeneID; 397573; -.
DR KEGG; ssc:397573; -.
DR CTD; 26872; -.
DR eggNOG; ENOG502QWI9; Eukaryota.
DR GeneTree; ENSGT00390000008042; -.
DR HOGENOM; CLU_034618_0_0_1; -.
DR InParanoid; Q9GL50; -.
DR OMA; KWHLPMK; -.
DR OrthoDB; 638341at2759; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000015301; Expressed in adipose tissue and 35 other tissues.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR Pfam; PF01794; Ferric_reduct; 1.
PE 2: Evidence at transcript level;
KW Copper; Electron transport; Endosome; FAD; Flavoprotein; Heme;
KW Ion transport; Iron; Iron transport; Membrane; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..338
FT /note="Metalloreductase STEAP1"
FT /id="PRO_0000191696"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 117..264
FT /note="Ferric oxidoreductase"
FT BINDING 139
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 174
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 253
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 267
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
SQ SEQUENCE 338 AA; 39918 MW; ED490E86E067A32B CRC64;
MESRQDITNQ EELWKMKPRK NLEDDYLNED SRENSMPKRP MLVHLHQTAH FDEFDCPPEL
QHKQELFPKW HLPIKIAAIV SSLTFLYTLL REVIHPFVTS HQQYFYKIPI LVINKVLPMV
SITLLALVYL PGVIAAIVQL HNGTKYKKFP HWLDRWMVTR KQFGLLSFFF AVLHAVYSLS
YPMRRSYRYK LLNWAYQQVQ QNKEDAWIEH DVWRMEIYVS LGIVTLAILA LLAVTSIPSV
SDSLTWREFH YIQSTLGIVS LLLGTIHALI FAWNKWVDIK QFIWYTPPTF MIAVFLPTVV
LICKVILLLP CLRRKILKIR HGWEDVTKIN KTEMSSQL
