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DES1L_ORYSJ
ID   DES1L_ORYSJ             Reviewed;         328 AA.
AC   Q6H5U3; A0A0P0VMI9;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Sphingolipid delta(4)-desaturase DES1-like;
DE            EC=1.14.19.17 {ECO:0000250|UniProtKB:Q9ZPH4};
GN   OrderedLocusNames=Os02g0639600, LOC_Os02g42660;
GN   ORFNames=OsJ_07673, OSJNBa0014E22.44, P0010C01.20;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Sphingolipid-delta-4-desaturase required for the biosynthesis
CC       of delta-4-unsaturated sphingolipids and derivatives. {ECO:0000250}.
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:0000250|UniProtKB:Q9ZPH4};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AP004768; BAD25351.1; -; Genomic_DNA.
DR   EMBL; AP005513; BAD25906.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09454.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79967.1; -; Genomic_DNA.
DR   EMBL; CM000139; EEE57453.1; -; Genomic_DNA.
DR   EMBL; AK101968; BAG95317.1; -; mRNA.
DR   RefSeq; XP_015623789.1; XM_015768303.1.
DR   AlphaFoldDB; Q6H5U3; -.
DR   STRING; 4530.OS02T0639600-01; -.
DR   PaxDb; Q6H5U3; -.
DR   PRIDE; Q6H5U3; -.
DR   EnsemblPlants; Os02t0639600-01; Os02t0639600-01; Os02g0639600.
DR   GeneID; 4330104; -.
DR   Gramene; Os02t0639600-01; Os02t0639600-01; Os02g0639600.
DR   KEGG; osa:4330104; -.
DR   eggNOG; KOG2987; Eukaryota.
DR   HOGENOM; CLU_032156_0_0_1; -.
DR   InParanoid; Q6H5U3; -.
DR   OMA; FTYIHLL; -.
DR   OrthoDB; 1255438at2759; -.
DR   PlantReactome; R-OSA-1119325; Sphingolipid metabolism.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6H5U3; OS.
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:0042284; F:sphingolipid delta-4 desaturase activity; IBA:GO_Central.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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   Pfam; PF00487; FA_desaturase; 1.
DR   Pfam; PF08557; Lipid_DES; 1.
DR   PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
DR   SMART; SM01269; Lipid_DES; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..328
FT                   /note="Sphingolipid delta(4)-desaturase DES1-like"
FT                   /id="PRO_0000430304"
FT   TRANSMEM        50..70
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   MOTIF           98..102
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           135..139
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           266..270
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   328 AA;  37869 MW;  98821042BDC2DFFB CRC64;
     MGAAAGDGRE EEGVMATDFF WSYTDEPHAT RRREILAKHP QIKELFGPDP LAFLKIAAVV
     SLQLWTATLL RDASWVKILT VAYFFGSFLN HNLFLAIHEL SHNLAFTTPS YNRWLGIFAN
     LPIGVPMSIT FQKYHLEHHR FQGVDGIDMD IPSQAEAHAV KNTLSKSVWV VFQLFFYALR
     PLFLKPKPPG LWEFTNLIIQ IALDASMVYF FGWKSLAYLI LSTFVGGGMH PMAGHFISEH
     YVFNPDQETY SYYGPLNLMT WHVGYHNEHH DFPRIPGTRL YKVREIAPEY YNNLKSYKSW
     SQVIYMYIMD QTVGPFSRMK RKAPKKDS
 
 
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