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Database: UniProt
Entry: T1HLH3_RHOPR
LinkDB: T1HLH3_RHOPR
Original site: T1HLH3_RHOPR 
ID   T1HLH3_RHOPR            Unreviewed;       368 AA.
AC   T1HLH3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:RPRC004897-PA};
DE   Flags: Fragment;
OS   Rhodnius prolixus (Triatomid bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX   NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC004897-PA, ECO:0000313|Proteomes:UP000015103};
RN   [1] {ECO:0000313|Proteomes:UP000015103}
RP   NUCLEOTIDE SEQUENCE.
RA   Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:RPRC004897-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2015) to UniProtKB.
CC   -!- FUNCTION: May be involved in the metabolism of insect hormones and in
CC       the breakdown of synthetic insecticides.
CC       {ECO:0000256|ARBA:ARBA00003690}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004174}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; ACPB03018046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1HLH3; -.
DR   STRING; 13249.T1HLH3; -.
DR   EnsemblMetazoa; RPRC004897-RA; RPRC004897-PA; RPRC004897.
DR   VEuPathDB; VectorBase:RPRC004897; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   HOGENOM; CLU_001570_5_2_1; -.
DR   InParanoid; T1HLH3; -.
DR   OMA; VFIMREK; -.
DR   OrthoDB; 1611592at2759; -.
DR   Proteomes; UP000015103; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11056; CYP6-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24292; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24292:SF54; CYTOCHROME P450 28A5-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW   Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015103}.
FT   BINDING         313
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:0000256|PIRSR:PIRSR602403-1"
SQ   SEQUENCE   368 AA;  42004 MW;  F919D26D4AB971A4 CRC64;
     RWKIMRNSHI GSMTPAKLKG MVPFTIDVCK NLVTAIGSKH SVPIEARDLC ASYATDNVAS
     CAFGLQCDSL INPNAAFGKV ARQVFEGDKM TGLVTMMSFF IPSLLNVFRL VYTLKDISDY
     FIQIINDTIH HREKQGVQRE DFLNLMIKTM KNDEKGYNNV LITSQCFAML LDGFFTTSIA
     MSFILYELAV HPEIQQNLRK EIQTISAKIQ DFDYDKVQSL NYLDMVIYES LRLHPPIQTL
     TKVCTKNTIL SCNGSHYKLE KGTPVTVPIT AIHMDEKFYP KPKEFIPERF SEEQKAKRDR
     YLYLAFGEGP RICLGMKFAI MQIKLGLIAI LLNFDVTPRD NKPIELDPNS FLFHIAKDGI
     WLNFNKIA
//
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