ID A0A1I8G5M9_9PLAT Unreviewed; 428 AA.
AC A0A1I8G5M9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0000903-snap-gene-0.7-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0000903-snap-gene-0.7-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0000903-snap-gene-0.7-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295}.
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DR AlphaFoldDB; A0A1I8G5M9; -.
DR WBParaSite; maker-uti_cns_0000903-snap-gene-0.7-mRNA-1; maker-uti_cns_0000903-snap-gene-0.7-mRNA-1; maker-uti_cns_0000903-snap-gene-0.7.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:UniProt.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProt.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProt.
DR CDD; cd03506; Delta6-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353:SF88; DELTA(5) FATTY ACID DESATURASE FAT-4; 1.
DR PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..79
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 428 AA; 50269 MW; AD7B714BE97794D2 CRC64;
MSNEFSWEEI RSHTSPDSRW LVVDNAVYDV SRWAQKHPGG SRLLSHYAGQ DATEAFRAFH
LDQSTVAKWL APLRIGRVCS NDPERLVAMR TDFERLRKDA QARGLFKPSL VFYALMLAHI
FALEAIAYAC LRFWGTGWLP YIVALCLYAT AQSQASWLQH DFGHLSVFHN RRWDGWLHQL
TMSYFKGASA HWWKHLHYQH HSKPNVMNKD PDVRIQPLFV VGKTMPKETA ANPKSPYVPY
HFQHRYFFAI GPPLLFPVYF QIATFRHAIS RRCYVDLACM ALFFAKIVVL YRPLLGLGGA
FLYYFLVRMI ESHWFTWVSQ SNHIPMEIEH DRAEPWLALQ LHATCDIEKS PFNDWFTGHL
NFQIEHHLFP TMPRHNYYKI QPDVQHLCQK YGIRHEIKPL WRAFCDVIGS LRHSGEIWHA
AYHAHHMD
//