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ZDH24_ARATH
ID   ZDH24_ARATH             Reviewed;         407 AA.
AC   Q8VYS8; F4K7H9; F6MDM7; Q9FGA9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable protein S-acyltransferase 9;
DE            EC=2.3.1.225;
DE   AltName: Full=Probable palmitoyltransferase At5g50020;
DE   AltName: Full=Zinc finger DHHC domain-containing protein At5g50020;
GN   Name=PAT09; OrderedLocusNames=At5g50020; ORFNames=MPF21.3;
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 [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=22968831; DOI=10.1104/pp.112.203968;
RA   Batistic O.;
RT   "Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-
RT   acyltransferase protein family.";
RL   Plant Physiol. 160:1597-1612(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   GENE FAMILY, AND FUNCTION.
RA   Hemsley P.A., Taylor L., Grierson C.S.;
RT   "S-acylation: dynamic control of plant development and sigalling by lipid
RT   modification of proteins.";
RL   (In) Proceedings of the 18th international conference on Arabidopsis
RL   research, abstract#139, Beijing (2007).
CC   -!- FUNCTION: Palmitoyl acyltransferase. {ECO:0000250, ECO:0000269|Ref.5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VYS8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VYS8-2; Sequence=VSP_047438, VSP_047439;
CC       Name=3;
CC         IsoId=Q8VYS8-3; Sequence=VSP_047439;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in seeds.
CC       {ECO:0000269|PubMed:22968831}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB10288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; JF792493; AEF58502.1; -; mRNA.
DR   EMBL; AB026650; BAB10288.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED95886.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95887.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM68839.1; -; Genomic_DNA.
DR   EMBL; AY070050; AAL49807.1; -; mRNA.
DR   EMBL; AY096683; AAM20317.1; -; mRNA.
DR   RefSeq; NP_001190503.1; NM_001203574.1. [Q8VYS8-2]
DR   RefSeq; NP_001330558.1; NM_001344870.1. [Q8VYS8-3]
DR   RefSeq; NP_199813.2; NM_124381.3. [Q8VYS8-1]
DR   AlphaFoldDB; Q8VYS8; -.
DR   SMR; Q8VYS8; -.
DR   BioGRID; 20312; 2.
DR   IntAct; Q8VYS8; 2.
DR   STRING; 3702.AT5G50020.2; -.
DR   iPTMnet; Q8VYS8; -.
DR   PaxDb; Q8VYS8; -.
DR   PRIDE; Q8VYS8; -.
DR   ProteomicsDB; 232339; -. [Q8VYS8-1]
DR   EnsemblPlants; AT5G50020.1; AT5G50020.1; AT5G50020. [Q8VYS8-1]
DR   EnsemblPlants; AT5G50020.2; AT5G50020.2; AT5G50020. [Q8VYS8-2]
DR   EnsemblPlants; AT5G50020.3; AT5G50020.3; AT5G50020. [Q8VYS8-3]
DR   GeneID; 835066; -.
DR   Gramene; AT5G50020.1; AT5G50020.1; AT5G50020. [Q8VYS8-1]
DR   Gramene; AT5G50020.2; AT5G50020.2; AT5G50020. [Q8VYS8-2]
DR   Gramene; AT5G50020.3; AT5G50020.3; AT5G50020. [Q8VYS8-3]
DR   KEGG; ath:AT5G50020; -.
DR   Araport; AT5G50020; -.
DR   TAIR; locus:2170046; AT5G50020.
DR   eggNOG; KOG1311; Eukaryota.
DR   InParanoid; Q8VYS8; -.
DR   OrthoDB; 1264614at2759; -.
DR   PhylomeDB; Q8VYS8; -.
DR   BRENDA; 2.3.1.225; 399.
DR   PRO; PR:Q8VYS8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8VYS8; baseline and differential.
DR   Genevisible; Q8VYS8; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Alternative splicing; Cell membrane; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..407
FT                   /note="Probable protein S-acyltransferase 9"
FT                   /id="PRO_0000315352"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          136..179
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          300..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        166
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1
FT                   /note="M -> MNDSWSAGPDRILQFVRECSEECLIRSLILM (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047438"
FT   VAR_SEQ         168
FT                   /note="W -> WVGQCIGV (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:22968831"
FT                   /id="VSP_047439"
SQ   SEQUENCE   407 AA;  47105 MW;  D404CBF9F4B5CBB7 CRC64;
     MAGRVFEAWK GSNKFLFGGR LIFGPDAWSI PFTFLLIITP VCFFSVFVAT HLRRELLPNN
     AGHVFLVAGV LFTVFVLILL FLTSARDPGI VPRNSHPPEE ELCYDTTVSS DGRQTPTVQI
     PRTKEVMVYG VSVRVKYCDT CMLYRPPRCS HCSICNNCVE RFDHHCPWRN YRYFFMFVSS
     ATILCIYIFS MSALYIKVLM DNHQGTVWRA MRESPWAVML MIYCFISLWF VGGLTGFHLY
     LISTNQTTYE NFRYRSDNRI NVYNRGCSNN FFETFCSKVK PSRNDFRAFI KEEPPRNITL
     ATTWERPEEA DEENREERRQ KVEDDLDIDE DVMKLQQRLN DEEGSDTAHH KIDIDQMRIG
     SNERAPTIRS EARHGNWGAR SNAQEEDVIA GSSVRESRSY AAAEEGR
 
 
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