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NCER2_ARATH
ID   NCER2_ARATH             Reviewed;         757 AA.
AC   Q304B9; F4IRY2; Q3EBK8; Q7XJQ9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Neutral ceramidase 2 {ECO:0000303|PubMed:26150824};
DE            Short=AtNCER2 {ECO:0000303|PubMed:26150824};
DE            Short=N-CDase 2 {ECO:0000303|PubMed:26150824};
DE            Short=NCDase 2 {ECO:0000303|PubMed:26150824};
DE            EC=3.5.1.23 {ECO:0000250|UniProtKB:O06769};
DE   AltName: Full=Acylsphingosine deacylase 2;
DE   AltName: Full=N-acylsphingosine amidohydrolase 2;
DE   Flags: Precursor;
GN   Name=NCER2 {ECO:0000303|PubMed:26150824};
GN   OrderedLocusNames=At2g38010 {ECO:0000312|Araport:AT2G38010};
GN   ORFNames=T8P21.8 {ECO:0000305};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=26150824; DOI=10.3389/fpls.2015.00460;
RA   Li J., Bi F.-C., Yin J., Wu J.-X., Rong C., Wu J.-L., Yao N.;
RT   "An Arabidopsis neutral ceramidase mutant ncer1 accumulates
RT   hydroxyceramides and is sensitive to oxidative stress.";
RL   Front. Plant Sci. 6:460-460(2015).
CC   -!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and
CC       free fatty acid. {ECO:0000250|UniProtKB:F4HQM3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine;
CC         Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23;
CC         Evidence={ECO:0000250|UniProtKB:O06769};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9VA70}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:F4HQM3}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q0JL46}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q304B9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q304B9-2; Sequence=VSP_058912;
CC   -!- SIMILARITY: Belongs to the neutral ceramidase family. {ECO:0000305}.
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DR   EMBL; CP002685; AEC09477.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09478.1; -; Genomic_DNA.
DR   PIR; H84799; H84799.
DR   RefSeq; NP_181337.2; NM_129358.3. [Q304B9-1]
DR   RefSeq; NP_973628.1; NM_201899.2. [Q304B9-2]
DR   AlphaFoldDB; Q304B9; -.
DR   SMR; Q304B9; -.
DR   BioGRID; 3723; 1.
DR   STRING; 3702.AT2G38010.2; -.
DR   MetOSite; Q304B9; -.
DR   PaxDb; Q304B9; -.
DR   PRIDE; Q304B9; -.
DR   ProteomicsDB; 251251; -. [Q304B9-1]
DR   EnsemblPlants; AT2G38010.1; AT2G38010.1; AT2G38010. [Q304B9-1]
DR   EnsemblPlants; AT2G38010.2; AT2G38010.2; AT2G38010. [Q304B9-2]
DR   GeneID; 818379; -.
DR   Gramene; AT2G38010.1; AT2G38010.1; AT2G38010. [Q304B9-1]
DR   Gramene; AT2G38010.2; AT2G38010.2; AT2G38010. [Q304B9-2]
DR   KEGG; ath:AT2G38010; -.
DR   Araport; AT2G38010; -.
DR   TAIR; locus:2065685; AT2G38010.
DR   eggNOG; KOG2232; Eukaryota.
DR   HOGENOM; CLU_011300_2_0_1; -.
DR   InParanoid; Q304B9; -.
DR   OrthoDB; 967085at2759; -.
DR   PhylomeDB; Q304B9; -.
DR   BioCyc; ARA:AT2G38010-MON; -.
DR   PRO; PR:Q304B9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q304B9; baseline and differential.
DR   Genevisible; Q304B9; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IBA:GO_Central.
DR   GO; GO:0046514; P:ceramide catabolic process; IBA:GO_Central.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 2.60.40.2300; -; 1.
DR   InterPro; IPR006823; Ceramidase_alk.
DR   InterPro; IPR038445; NCDase_C_sf.
DR   InterPro; IPR031331; NEUT/ALK_ceramidase_C.
DR   InterPro; IPR031329; NEUT/ALK_ceramidase_N.
DR   PANTHER; PTHR12670; PTHR12670; 1.
DR   Pfam; PF04734; Ceramidase_alk; 1.
DR   Pfam; PF17048; Ceramidse_alk_C; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Lipid metabolism; Reference proteome; Secreted; Signal;
KW   Sphingolipid metabolism.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..757
FT                   /note="Neutral ceramidase 2"
FT                   /id="PRO_0000247110"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR71"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        657
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   VAR_SEQ         282
FT                   /note="D -> ESYPFLELPNVAILYIAVAERLMWKVMVLFYFVSES (in
FT                   isoform 2)"
FT                   /id="VSP_058912"
SQ   SEQUENCE   757 AA;  83264 MW;  6586793BC42B1E42 CRC64;
     MAVSLPLFQF ILFLLLLLLS RTVYAYLIGV GSYDITGPAA DVNMMGYANS DQIASGIHFR
     LRARAFIVAE PQGNRVVFVN LDACMASQIV TIKVLERLKA RYGELYTEKN VAISGIHTHA
     GPGGYLQYVT YIVTSLGFVR QSFDVVVNGI EQSIVQAHES LRPGSAFVNK GDLLDAGVNR
     SPSSYLNNPA AERSKYKYDV DKEMTLVKFV DSQLGPTGSF NWFATHGTSM SRTNSLISGD
     NKGAAARFME DWFENGQKNS VSSRNIPRRV STIVSDFSRN RDRLLDIAAT YKSSRGHSVD
     KSLDVKTRVR NGSKRKFVSA FCQSNCGDVS PNTLGTFCID TGLPCDFNHS TCNGQNELCY
     GRGPGYPDEF ESTRIIGEKQ FKMAVELFNK ATEKLQGKIG YQHAYLDFSN LDVTVPKAGG
     GSETVKTCPA AMGFGFAAGT TDGPGAFDFK QGDDQGNVFW RLVRNVLRTP GPEQVQCQKP
     KPILLDTGEM KEPYDWAPSI LPIQILRIGQ LVILSVPGEF TTMAGRRLRD AIKSFLISSD
     PKEFSNNMHV VIAGLTNTYS QYIATFEEYE VQRYEGASTL YGRHTLTAYI QEFKKLATAL
     VNGLTLPRGP QPPDLLDKQI SLLSPVVVDS TPLGVKFGDV KADVPPKSTF RRGQQVNATF
     WSGCPRNDLM TEGSFAVVET LREGGKWAPV YDDDDFSLKF KWSRPAKLSS ESQATIEWRV
     PESAVAGVYR IRHYGASKSL FGSISSFSGS SSAFVVV
 
 
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