FADS2_PAPAN
ID FADS2_PAPAN Reviewed; 444 AA.
AC B8R1K0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Acyl-CoA 6-desaturase {ECO:0000303|PubMed:19202133};
DE EC=1.14.19.3 {ECO:0000269|PubMed:19202133};
DE AltName: Full=Delta-6 fatty acid desaturase;
DE Short=Delta(6) desaturase;
DE Short=Delta-6 desaturase {ECO:0000250|UniProtKB:O95864};
DE AltName: Full=Fatty acid desaturase 2 {ECO:0000303|PubMed:19202133};
GN Name=FADS2 {ECO:0000303|PubMed:19202133};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP DOMAIN.
RX PubMed=19202133; DOI=10.1194/jlr.m800630-jlr200;
RA Park W.J., Kothapalli K.S., Lawrence P., Tyburczy C., Brenna J.T.;
RT "An alternate pathway to long-chain polyunsaturates: the FADS2 gene product
RT Delta8-desaturates 20:2n-6 and 20:3n-3.";
RL J. Lipid Res. 50:1195-1202(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of highly unsaturated fatty
CC acids (HUFA) from the essential polyunsaturated fatty acids (PUFA)
CC linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3)
CC precursors, acting as a fatty acyl-coenzyme A (CoA) desaturase that
CC introduces a cis double bond at carbon 6 of the fatty acyl chain.
CC Catalyzes the first and rate limiting step in this pathway which is the
CC desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleate
CC (GLA) (18:3n-6) and stearidonate (18:4n-3), respectively (By
CC similarity). Subsequently, in the biosynthetic pathway of HUFA n-3
CC series, it desaturates tetracosapentaenoate (24:5n-3) to
CC tetracosahexaenoate (24:6n-3), which is then converted to
CC docosahexaenoate (DHA)(22:6n-3), an important lipid for nervous system
CC function (By similarity). It can also desaturate (11E)-octadecenoate
CC (trans-vaccenoate) at carbon 6 generating (6Z,11E)-octadecadienoate (By
CC similarity). In addition to Delta-6 activity, this enzyme exhibits
CC Delta-8 activity with slight biases toward n-3 fatty acyl-CoA
CC substrates (PubMed:19202133). {ECO:0000250|UniProtKB:O95864,
CC ECO:0000250|UniProtKB:Q9Z122, ECO:0000269|PubMed:19202133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:47140, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57363,
CC ChEBI:CHEBI:57383; EC=1.14.19.3;
CC Evidence={ECO:0000269|PubMed:19202133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47141;
CC Evidence={ECO:0000269|PubMed:19202133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:47144, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:71489, ChEBI:CHEBI:74034; EC=1.14.19.3;
CC Evidence={ECO:0000269|PubMed:19202133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47145;
CC Evidence={ECO:0000269|PubMed:19202133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z,18Z,21Z)-tetracosapentaenoyl-CoA + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z,18Z,21Z)-
CC tetracosahexaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:36999, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74083,
CC ChEBI:CHEBI:74086; Evidence={ECO:0000250|UniProtKB:Q9Z122};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37000;
CC Evidence={ECO:0000250|UniProtKB:Q9Z122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) +
CC O2 = (6Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2
CC H2O; Xref=Rhea:RHEA:46064, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74296,
CC ChEBI:CHEBI:85652; Evidence={ECO:0000250|UniProtKB:Q9Z122};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46065;
CC Evidence={ECO:0000250|UniProtKB:Q9Z122};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z)-eicosadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2
CC H(+) + O2 = (8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:39567, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74264,
CC ChEBI:CHEBI:76410; Evidence={ECO:0000269|PubMed:19202133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39568;
CC Evidence={ECO:0000269|PubMed:19202133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z,17Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] +
CC 2 H(+) + O2 = (8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(III)-
CC [cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:39571, Rhea:RHEA-COMP:10438,
CC Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:74265, ChEBI:CHEBI:74328;
CC Evidence={ECO:0000269|PubMed:19202133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39572;
CC Evidence={ECO:0000269|PubMed:19202133};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000305|PubMed:19202133}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The protein sequence includes a number of characteristic
CC features of microsomal fatty acid desaturases including the three
CC histidine boxes HXXXH, HXXHH, and QXXHH (these domains may contain the
CC active site and/or be involved in metal ion binding), and the N-
CC terminal cytochrome b5 domain containing the heme-binding motif, HPGG,
CC similar to that of other fatty acid desaturases.
CC {ECO:0000303|PubMed:19202133}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AHZZ02006386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EU780003; ACI46980.1; -; mRNA.
DR RefSeq; NP_001138559.1; NM_001145087.1.
DR AlphaFoldDB; B8R1K0; -.
DR SMR; B8R1K0; -.
DR STRING; 9555.ENSPANP00000007895; -.
DR SwissLipids; SLP:000000444; -.
DR Ensembl; ENSPANT00000027105; ENSPANP00000007895; ENSPANG00000015652.
DR GeneID; 100126749; -.
DR KEGG; panu:100126749; -.
DR CTD; 9415; -.
DR GeneTree; ENSGT00950000182990; -.
DR OrthoDB; 1060606at2759; -.
DR BRENDA; 1.14.19.3; 4519.
DR BRENDA; 1.14.19.31; 4519.
DR BRENDA; 1.14.19.4; 4519.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000028761; Chromosome 12.
DR Bgee; ENSPANG00000015652; Expressed in pigmented layer of retina and 65 other tissues.
DR ExpressionAtlas; B8R1K0; baseline.
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:0016213; F:linoleoyl-CoA desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:Ensembl.
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 PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Electron transport; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..444
FT /note="Acyl-CoA 6-desaturase"
FT /id="PRO_0000451726"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..157
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..305
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 18..95
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT MOTIF 180..184
FT /note="Histidine box-1"
FT /evidence="ECO:0000303|PubMed:19202133"
FT MOTIF 217..221
FT /note="Histidine box-2"
FT /evidence="ECO:0000303|PubMed:19202133"
FT MOTIF 382..386
FT /note="Histidine box-3"
FT /evidence="ECO:0000303|PubMed:19202133"
SQ SEQUENCE 444 AA; 52301 MW; 6A57B278995FE52E CRC64;
MGKGGNQGEG AAEREVPMPT FSWEEIQKHN LRTDRWLVID RKVYNITKWS TQHPGGQRVI
GHYAGEDATD AFRAFHPDLK FVGKFLKPLL IGELAPEEPS QDHGKNSKII EDFRALKKTA
EDMNLFKTNH VFFLLLLAHI IALESIAWFT VFYFGNGWIP TLITAFVLAT SQAQAGWLQH
DYGHLSVYRK PKWNHLVHKF VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDVNMLHVFV
LGEWQPIEYG KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMIVH KNWVDLAWAI
SYYIRFFVTY IPFYGILGAL LFLNFIRFLE SHWFVWVTQM NHIVMEIDQE AYRDWFSSQL
TATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA PLVKSLCAKH GIEYQEKPLL
RALLDIIRSL RKSGKLWLDA YLHK
