FS2P1_HUMAN
ID FS2P1_HUMAN Reviewed; 482 AA.
AC A8MWK0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Putative fatty acid desaturase 2-like protein FADS2B;
DE AltName: Full=Fatty acid desaturase 2 pseudogene 1;
DE AltName: Full=Fatty acid desaturase 2B, pseudogene {ECO:0000312|HGNC:HGNC:43618};
GN Name=FADS2B {ECO:0000312|HGNC:HGNC:43618}; Synonyms=FADS2P1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95864}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AP000479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A8MWK0; -.
DR BioMuta; HGNC:43618; -.
DR MassIVE; A8MWK0; -.
DR PeptideAtlas; A8MWK0; -.
DR PRIDE; A8MWK0; -.
DR GeneCards; FADS2B; -.
DR HGNC; HGNC:43618; FADS2B.
DR neXtProt; NX_A8MWK0; -.
DR InParanoid; A8MWK0; -.
DR PhylomeDB; A8MWK0; -.
DR UniPathway; UPA00658; -.
DR Pharos; A8MWK0; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A8MWK0; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.120.10; -; 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; PTHR19353; 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; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 5: Uncertain;
KW Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..482
FT /note="Putative fatty acid desaturase 2-like protein
FT FADS2B"
FT /id="PRO_0000348957"
FT TOPO_DOM 1..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..190
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..343
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 56..132
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 217..221
FT /note="Histidine box-1"
FT MOTIF 254..258
FT /note="Histidine box-2"
FT MOTIF 421..425
FT /note="Histidine box-3"
FT BINDING 90
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:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 113
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:0000255|PROSITE-ProRule:PRU00279"
SQ SEQUENCE 482 AA; 56358 MW; 8036A3CABC5D8751 CRC64;
MKFEEKCGDN GSIVGRNQSY PGEKHQPKGK PIANGEAEVY AKQEANGKCS TPRKSLSMYT
WLEIQRHNHE ADQLVINCKV YNVSSWADRH PGGHQVLNHC AGEDAMDVFR AMHPELDIVQ
LYLKPLLIGE LAPGEPSQER HKNSQLVKDF QELWSIAEAM NMFHANLGFF FLHFVQILIL
EVLAWLIVYH FGSGWPVTMF ISFLLTISQA SSSFLQHDAG HLSIFRKSKW NHVVHKFVMC
HLKGLSADRW NYWHFEQHVK PNIYPKDPDI DTDPLFLLGD SQPVKYGKKK IKYINYEEQH
LYFYKVWLPL FMPVYLKLPS MQAMYLQRYW VCFSLQDITW VSSFYIYFIT FGLYYGIFGT
MLLIYLVKFL ESPWIVYVTQ MSHITMRMST EENRDWLTTQ VLATCNTESF FNDFTGHLNF
QIEHHLFPTM PRHNYHKVAP LVRSLCAKHG LHYVNKPMLR AFGDIVRALK KSAALWADAY
YE
