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Database: UniProt
Entry: H2TL54_TAKRU
LinkDB: H2TL54_TAKRU
Original site: H2TL54_TAKRU 
ID   H2TL54_TAKRU            Unreviewed;       407 AA.
AC   H2TL54;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=cytochrome-b5 reductase {ECO:0000256|ARBA:ARBA00012011};
DE            EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000025409.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000025409.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000025409.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC         H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC         COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00029341};
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|RuleBase:RU362121}.
CC   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC       reductase family. {ECO:0000256|ARBA:ARBA00006105}.
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DR   AlphaFoldDB; H2TL54; -.
DR   STRING; 31033.ENSTRUP00000025409; -.
DR   Ensembl; ENSTRUT00000025512.3; ENSTRUP00000025409.3; ENSTRUG00000010094.3.
DR   GeneTree; ENSGT00940000155536; -.
DR   InParanoid; H2TL54; -.
DR   OMA; WYMLDSA; -.
DR   Proteomes; UP000005226; Chromosome 7.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06183; cyt_b5_reduct_like; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR46237:SF1; CYTOCHROME B5 REDUCTASE 4; 1.
DR   PANTHER; PTHR46237; CYTOCHROME B5 REDUCTASE 4 FAMILY MEMBER; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51203; CS; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT   DOMAIN          57..133
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          144..235
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   DOMAIN          252..362
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  45924 MW;  6241F13731576842 CRC64;
     MLNIPTQSFP SPSSQQRVSP SGQSGRSKVA LKPGHSLMDW IRFSKSGKDL TGLRGRLIEV
     SQEELRKHNN RDDCWTCIRG LVYNVTPYMD YHPGGEDELM KAAGIDGTDL FDQVHRWVNY
     ESMLKECLVG RMDSIFMLFM SNLCCLPRYD WFQTDVSVHL VVYAKRKIPS AGCTSVDLEA
     GVLRLEALLG KMSYMIHLRL ADEVEGNVAV HTAFSVGKIQ VSLRKKGKTK WTNLGQPLEF
     HNTFVLKKER APHYCQGVLV SKTEVNHNTL IFRVKLPPGT IRHVPVGTHV YLKAVVKDAE
     LVRPYTPVDQ SLTAAPQHPS EETDLFLMVK IYPDGMFSSY LNDLHVGDRL SVSGPEGAFS
     LRPLRDVTHL YLLAAGTGLT PMTRLIRLAT QEMGHIRLFF CNYNYLQ
//
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