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NTE1_CANAL
ID   NTE1_CANAL              Reviewed;        1386 AA.
AC   Q5A368; A0A1D8PTQ9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Lysophospholipase NTE1;
DE            EC=3.1.1.5;
DE   AltName: Full=Intracellular phospholipase B;
DE   AltName: Full=Neuropathy target esterase homolog;
GN   Name=NTE1; OrderedLocusNames=CAALFM_CR08300CA;
GN   ORFNames=CaO19.13754, CaO19.6396;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: Intracellular phospholipase B that catalyzes the double
CC       deacylation of phosphatidylcholine (PC) to glycerophosphocholine
CC       (GroPCho). Plays an important role in membrane lipid homeostasis.
CC       Responsible for the rapid PC turnover in response to inositol, elevated
CC       temperatures, or when choline is present in the growth medium (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC   -!- ACTIVITY REGULATION: Inhibited by organophosphorus esters.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR   EMBL; CP017630; AOW31511.1; -; Genomic_DNA.
DR   RefSeq; XP_716236.1; XM_711143.2.
DR   AlphaFoldDB; Q5A368; -.
DR   SMR; Q5A368; -.
DR   BioGRID; 1225170; 1.
DR   STRING; 237561.Q5A368; -.
DR   PRIDE; Q5A368; -.
DR   GeneID; 3642076; -.
DR   KEGG; cal:CAALFM_CR08300CA; -.
DR   CGD; CAL0000194621; orf19.13754.
DR   VEuPathDB; FungiDB:CR_08300C_A; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q5A368; -.
DR   OMA; FTMNFTT; -.
DR   OrthoDB; 253518at2759; -.
DR   PRO; PR:Q5A368; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 2.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; SSF51206; 2.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1386
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295314"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..65
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..1386
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1081..1245
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          394..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1085..1090
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1112..1116
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1232..1234
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1232
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         577..701
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         697..821
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1386 AA;  155704 MW;  30459D16F3477170 CRC64;
     MGPEFEDSIP LVHSDNRTTT IYSVYIIISD IFSFVQWLLF KVLNLIIIDS PAFVLRLLSK
     NFEINLHLSS ILATLIGVSV VTYLVIRYKF LTGYSHSNDQ KEGAGKKGIH PASSKVFVGK
     SKQDKKPSNY LDEFLLAIKV FGYLDKAVFH ELTKSMTTQK LSHEEILCLD ESLGFSIVVE
     GVAQVYTKKS KENSSKYKQR YFEEIEEERD EFLILGDKQY QLLNEVKSGA PLSSLFSTLD
     LFRPRNKNEE MALTPNDEDG NSVVALNMDY LSKSEPATDS KLSNSDDDEN GQDYPEIIVR
     PKKSHNNGTI TIAIIPHTAF ERVQSKYPKA TSHIVTMVLT RLYKVTMSTV QNYLGLTSEI
     LKSEIKLNEE NATSLPRYFV DGLLERLNKK EEAEAEAENL PKKLKHHHRN QLQRTTSRYV
     SLDSKVKSNH PGDLLSSVPI SRSEFQKKVL PKSSTTSLSD GDNKRMNFTD EMEETEENSL
     RVAIIENIFK MVGIEETNGI VERTGYFQSL SSSTSSSIVG LDSLNQSIMS GATTPTTKRS
     HPVFNNQGSL MNTINLAELR KPSTAENSTL PKLSGKKRLL SDMNIKDAFA KSLEIKYIGP
     DSTIVSQNSA ITGLYYVIDG SLEIYNRSAD VSAPNRYIYT VESGGIAGYL TSVVGFRSMV
     TIKTPKKTGA VVAYIPKNDY NKLLDKYYFL QLPVALKLKN LLSKQILTID YALEWCHIPA
     GEVLCSQGDL ANGFHVVLSG RFRVVRSTNK NTEKEDVEVL GEYGHGESIG EVEVLTASRR
     SNTLIAVRDS ETARIPRSLF EMLSNENPSI MVSVSRLVAS KVLASQYQPR ERNFITSTTS
     QESFTSANYK TITILPTVSG LPVRQFAEKL VQALRQIGRN VIALDQASIL THLGRHAFDE
     SLARLKLSGY FAYLEEEYET IVYICDTPVQ SNWTSTCISQ GDCILLLADA EDDSTTIGEY
     EQLLVKLKTT ARTDLCLLHQ DKVVRAGSTS PWLKNRIWVQ GHHHIQMKFE QGANVLPHKK
     SFISDLAAKL SQNKAIKSTF EATKQHIKWY VKENDQSKVL KIYKDDFMRL ARILSNEAVG
     LVLGGGGSRG ISHVGVVTSL ERHGIPVDII GGTSIGSFVG GLYAKEYNIV SIYAMAKKFS
     KRISSVWRML FDLTYPVTSY ITGYEFNRGI WKVFGFAEIE DFWIKYFCNS ANITNSTMDI
     HEKGYAWRFI RASMSLAGLL PPIAFNGCML LDGGYLDNLP VNEMKKRGVK HIIAVDVGSV
     DDRTPMNYGD TLSGFWVLLN RWNPFSSHPN IPTMMDIQMR LTYVSSVNAL EEAKRTPGVY
     YLRPPIDPYA TLDFGKFDEI YKVGLKYADD LFADWKSKGK FPRIAGLVEK KKDGEEKKIL
     YRRNSI
 
 
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