GenomeNet

Database: UniProt
Entry: H0VH55_CAVPO
LinkDB: H0VH55_CAVPO
Original site: H0VH55_CAVPO 
ID   H0VH55_CAVPO            Unreviewed;       482 AA.
AC   H0VH55;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=STEAP4 metalloreductase {ECO:0000313|Ensembl:ENSCPOP00000009476.3};
GN   Name=STEAP4 {ECO:0000313|Ensembl:ENSCPOP00000009476.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000009476.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000009476.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000009476.3};
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; AAKN02016695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003475025.1; XM_003474977.3.
DR   RefSeq; XP_013013862.1; XM_013158408.1.
DR   AlphaFoldDB; H0VH55; -.
DR   STRING; 10141.ENSCPOP00000009476; -.
DR   Ensembl; ENSCPOT00000010651.3; ENSCPOP00000009476.3; ENSCPOG00000010556.4.
DR   GeneID; 100735486; -.
DR   KEGG; cpoc:100735486; -.
DR   CTD; 79689; -.
DR   VEuPathDB; HostDB:ENSCPOG00000010556; -.
DR   eggNOG; ENOG502R746; Eukaryota.
DR   GeneTree; ENSGT00390000008042; -.
DR   HOGENOM; CLU_034618_1_1_1; -.
DR   InParanoid; H0VH55; -.
DR   OMA; GWERNPK; -.
DR   OrthoDB; 5361at2759; -.
DR   TreeFam; TF332031; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000010556; Expressed in thyroid gland and 8 other cell types or tissues.
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:UP000005447};
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..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..374
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          249..393
FT                   /note="Ferric oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01794"
SQ   SEQUENCE   482 AA;  54552 MW;  B5DE67C462E0199D CRC64;
     MENPCMNALP LTMTSSQKQV TVCIFGTGDF GRSLGLKMLQ CGHAVVYGSR NPQMSSLLPS
     GAEVLSYPEA AQKSDIIIVA IHRDHYNFFI DLTEVLNGKI LVDVSNNLKI NQYPESNAEY
     LAQLVPGAHV VKAFNTISAW ALQSGALDAS RQVFVCGNDT NAKHRVMDIV RTLGLTPLDR
     GALVAAKEIE NYPLQLFPMW RFPLCLSAML CIFFFFYCVI RDIIYPYVYK KEDNTFRLAI
     SIPNRVFPIT ALVLLALVYL PGVIAAILQL YRGTKYFRFP DWLDHWMLCR KQLGLVALGF
     AFLHVIYTLV IPIRYYVRWR LRNITVTQAI NKKDDPFSIS LAWLSDSYVS LGILGFFLFL
     LLGITSLPSV SNMVNWREFR FVQSKLGYLT LTLCTAHTLV YGGKRFLTPS ALRWYLPSAY
     ILALIAPCTV LVVKFILIMP CIDKTLTRIR QGWEKNSKSS KPLLFRKSDV SNKAECTWAS
     EI
//
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