FS2P1_MOUSE
ID FS2P1_MOUSE Reviewed; 487 AA.
AC Q0VAX3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Fatty acid desaturase 2-like protein FADS2B;
DE AltName: Full=Fatty acid desaturase 2B, pseudogene {ECO:0000312|MGI:MGI:2687041};
GN Name=Fads2b {ECO:0000312|MGI:MGI:2687041};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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DR EMBL; BC120879; AAI20880.1; -; mRNA.
DR EMBL; AL929147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38168.1; -.
DR RefSeq; NP_001075133.1; NM_001081664.2.
DR AlphaFoldDB; Q0VAX3; -.
DR SMR; Q0VAX3; -.
DR STRING; 10090.ENSMUSP00000097507; -.
DR iPTMnet; Q0VAX3; -.
DR PhosphoSitePlus; Q0VAX3; -.
DR SwissPalm; Q0VAX3; -.
DR PaxDb; Q0VAX3; -.
DR PRIDE; Q0VAX3; -.
DR ProteomicsDB; 267527; -.
DR Ensembl; ENSMUST00000099923; ENSMUSP00000097507; ENSMUSG00000075217.
DR GeneID; 228151; -.
DR KEGG; mmu:228151; -.
DR UCSC; uc008kkj.1; mouse.
DR CTD; 643181; -.
DR MGI; MGI:2687041; Fads2b.
DR VEuPathDB; HostDB:ENSMUSG00000075217; -.
DR eggNOG; KOG4232; Eukaryota.
DR GeneTree; ENSGT00950000182990; -.
DR HOGENOM; CLU_016265_0_1_1; -.
DR InParanoid; Q0VAX3; -.
DR OMA; YAKQEAN; -.
DR OrthoDB; 1060606at2759; -.
DR PhylomeDB; Q0VAX3; -.
DR TreeFam; TF313604; -.
DR UniPathway; UPA00658; -.
DR BioGRID-ORCS; 228151; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q0VAX3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q0VAX3; protein.
DR Bgee; ENSMUSG00000075217; Expressed in uterine cervix and 82 other tissues.
DR Genevisible; Q0VAX3; MM.
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 2: Evidence at transcript level;
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..487
FT /note="Fatty acid desaturase 2-like protein FADS2B"
FT /id="PRO_0000348958"
FT TOPO_DOM 1..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..201
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..349
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 62..139
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 224..228
FT /note="Histidine box-1"
FT MOTIF 261..265
FT /note="Histidine box-2"
FT MOTIF 426..430
FT /note="Histidine box-3"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
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 120
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 487 AA; 57082 MW; 7DFA1834775F1AA6 CRC64;
MKLEEKLEHN ESLVGKSRPC LHDTHQANGK PIANGNPTAN GKVEVYEKQE ANGKGNRLGK
CLNLYTWQEI QRHSQEADQW LVIDRKVYNV TDWAGKHPGG RRVLNHYAGQ DATDAFRAMH
LDLGMVKLYL KPLLIGELSP EEPSQEKNKN AQLVEDFREL RKTLEAMNMF SANLRFFFLH
LAQILILEIS AWLILHHFGS SWLVTILISF LLTVSQAQCS FLQHDLGHLS MFKKSKWNHL
MHKFVMCHLK GLSADWWNYR HFQHHVKPNI YPKDPDIDVG PLFLVGDTQP IKYGKKKIKY
IDYEKQHLYF YMVALPFLMP VYFNLQSMQV MYLRKYWMDI AWVSSFYIRY FITFGPFYGI
FGTVLLIYLV KFIESPWIAY VTQMSHIPMK MSSEENHDWL STQVVATCNI EQSFFNDWFT
GHLNFQIEHH LFPTMPRHNY HKVAPLVKSL CAKHGLQYIN KPILKAFGDI VRSLKKSASL
WMNAYYE
