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Database: UniProt
Entry: A0A135UZK0_9PEZI
LinkDB: A0A135UZK0_9PEZI
Original site: A0A135UZK0_9PEZI 
ID   A0A135UZK0_9PEZI        Unreviewed;       382 AA.
AC   A0A135UZK0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Sphingolipid delta(4)-desaturase {ECO:0000256|PIRNR:PIRNR017228};
DE            EC=1.14.19.17 {ECO:0000256|PIRNR:PIRNR017228};
GN   ORFNames=CSAL01_09253 {ECO:0000313|EMBL:KXH65772.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH65772.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH65772.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH65772.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Delta(4)-fatty-acid desaturase which introduces a double bond
CC       at the 4-position in the long-chain base (LCB) of ceramides.
CC       {ECO:0000256|PIRNR:PIRNR017228}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC         = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC         Xref=Rhea:RHEA:46544, 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:31488,
CC         ChEBI:CHEBI:52639; EC=1.14.19.17;
CC         Evidence={ECO:0000256|PIRNR:PIRNR017228};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|PIRNR:PIRNR017228}.
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. DEGS
CC       subfamily. {ECO:0000256|ARBA:ARBA00006146,
CC       ECO:0000256|PIRNR:PIRNR017228}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXH65772.1}.
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DR   EMBL; JFFI01000826; KXH65772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135UZK0; -.
DR   STRING; 1209931.A0A135UZK0; -.
DR   OrthoDB; 5485164at2759; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000070121; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IEA:InterPro.
DR   CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR   InterPro; IPR011388; DES1/DES2.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR   PANTHER; PTHR12879; SPHINGOLIPID DELTA 4 DESATURASE/C-4 HYDROXYLASE PROTEIN DES2; 1.
DR   PANTHER; PTHR12879:SF8; SPHINGOLIPID DELTA(4)-DESATURASE DES1; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   Pfam; PF08557; Lipid_DES; 1.
DR   PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
DR   SMART; SM01269; Lipid_DES; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR017228};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR017228};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR017228};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW   Sphingolipid metabolism {ECO:0000256|PIRNR:PIRNR017228};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        75..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        136..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..76
FT                   /note="Sphingolipid delta4-desaturase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01269"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  43176 MW;  5C03DF6E9C62FB59 CRC64;
     MASSAASTVT QPSKRKSAAA PDGVAAGKLT TDAPTETSKE KDFFWTYTEE PHRTRRLAII
     KAHPEVTKLC GPEPLTKYVV AGVVAMQIFW AWYLRDTSFF SWKFWLVGYV FGATANQNLF
     LAIHEISHNL AFRSPLANRL FAIFANLPIG VPYSASFRPY HLTHHKSLGV DGLDTDLPTA
     LEVVFFDSIL GKAFFCTFQI FFYAVRPTLV YSVPFTWVHY LNIAVQLAFD YALYSAFGFN
     TILYFLLSSF LAGSLHPLAG HFIAEHYVYE TVTPAQRDAA NNIPVPETFS YYGPLNFLTY
     NVGLHNEHHD FPAVPWTRLP KLRAIASEFY DELPRHESWT YVIWRFILDP NVGITSRVKR
     KQGGRNVGGG AVAHWTREEI EA
//
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