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IPCS_ORYSJ
ID   IPCS_ORYSJ              Reviewed;         326 AA.
AC   Q5N7A7; A0A0P0VAB0;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Phosphatidylinositol:ceramide inositolphosphotransferase;
DE            EC=2.7.8.-;
DE   AltName: Full=Inositol-phosphorylceramide synthase;
DE            Short=IPC synthase;
DE   AltName: Full=Protein ENHANCING RPW8-MEDIATED HR-LIKE CELL DEATH 1;
DE   AltName: Full=Sphingolipid synthase;
GN   Name=ERH1; OrderedLocusNames=Os01g0850100;
GN   ORFNames=OsJ_04087, P0414E03.14, P0529H11.3;
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=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19001565; DOI=10.1105/tpc.108.060053;
RA   Wang W., Yang X., Tangchaiburana S., Ndeh R., Markham J.E., Tsegaye Y.,
RA   Dunn T.M., Wang G.-L., Bellizzi M., Parsons J.F., Morrissey D., Bravo J.E.,
RA   Lynch D.V., Xiao S.;
RT   "An inositolphosphorylceramide synthase is involved in regulation of plant
RT   programmed cell death associated with defense in Arabidopsis.";
RL   Plant Cell 20:3163-3179(2008).
CC   -!- FUNCTION: Catalyzes the transfer of the phosphorylinositol group from
CC       phosphatidylinositol (PI) to phytoceramide, an essential step in
CC       sphingolipid biosynthesis. May play an important role in modulating
CC       plant programmed cell death (PCD) associated with defense by promoting
CC       sphingolipid metabolism and regulating ceramide accumulation.
CC       {ECO:0000269|PubMed:19001565}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Reduced plant stature. Spontaneous HR-like cell
CC       death (SHL). {ECO:0000269|PubMed:19001565}.
CC   -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AP003242; BAD81774.1; -; Genomic_DNA.
DR   EMBL; AP004072; BAD82642.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF06726.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS75239.1; -; Genomic_DNA.
DR   EMBL; CM000138; EEE55674.1; -; Genomic_DNA.
DR   EMBL; AK071523; BAG92539.1; -; mRNA.
DR   RefSeq; XP_015622359.1; XM_015766873.1.
DR   AlphaFoldDB; Q5N7A7; -.
DR   STRING; 4530.OS01T0850100-01; -.
DR   PaxDb; Q5N7A7; -.
DR   PRIDE; Q5N7A7; -.
DR   EnsemblPlants; Os01t0850100-01; Os01t0850100-01; Os01g0850100.
DR   GeneID; 4324799; -.
DR   Gramene; Os01t0850100-01; Os01t0850100-01; Os01g0850100.
DR   KEGG; osa:4324799; -.
DR   eggNOG; KOG3058; Eukaryota.
DR   HOGENOM; CLU_078641_1_0_1; -.
DR   InParanoid; Q5N7A7; -.
DR   OMA; QINGMIM; -.
DR   OrthoDB; 599210at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q5N7A7; OS.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0047493; F:ceramide cholinephosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0045140; F:inositol phosphoceramide synthase activity; IBA:GO_Central.
DR   GO; GO:0033188; F:sphingomyelin synthase activity; IBA:GO_Central.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR045221; Sphingomyelin_synth-like.
DR   InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR   PANTHER; PTHR21290; PTHR21290; 1.
DR   Pfam; PF14360; PAP2_C; 1.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Plant defense; Reference proteome; Sphingolipid metabolism; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..326
FT                   /note="Phosphatidylinositol:ceramide
FT                   inositolphosphotransferase"
FT                   /id="PRO_0000419958"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          306..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   326 AA;  37555 MW;  119AE8AA00D7841A CRC64;
     MAVYIAREAT KLWRKVCAEI AVELQLLFEK WRLLLAGLVF QYIHGLAARG VHYLHRPGPL
     LQDLGFMALP ELGQDKGYVS ESVFTFIFIS FLLWSFHPFI YHSKRFYTVL LWRRVLAFLV
     ASQFLRIITF YSTQLPGPNY HCREGSKMAT LPPPHNVLEV LLINFPRGVL FGCGDLIFSS
     HMIFTLVFVR TYHKYGSKRL IKILAWLMAI IQSLLIIASR KHYSVDVVVA WYTVNLVVFF
     IDNKLPEMPD RTNGSSLLPV TAKDKDGRTK EELHKLEKDC KMKEEFHKLL NGNTVDSTDR
     RQRVQMNGKH GEDINHTLSD ATPNGT
 
 
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