GenomeNet

Database: UniProt
Entry: A0A1I9LQT3_ARATH
LinkDB: A0A1I9LQT3_ARATH
Original site: A0A1I9LQT3_ARATH 
ID   A0A1I9LQT3_ARATH        Unreviewed;       335 AA.
AC   A0A1I9LQT3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=S-acyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
DE   AltName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
GN   Name=PAT10 {ECO:0000313|EMBL:ANM64941.1, ECO:0000313|TAIR:AT3G51390};
GN   Synonyms=AtPAT10 {ECO:0000313|EMBL:ANM64941.1}, PROTEIN S-ACYL
GN   TRANSFERASE 10 {ECO:0000313|EMBL:ANM64941.1};
GN   OrderedLocusNames=At3g51390 {ECO:0000313|Araport:AT3G51390,
GN   ECO:0000313|EMBL:ANM64941.1};
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 {ECO:0000313|EMBL:ANM64941.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:ANM64941.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=11130713; DOI=10.1038/35048706;
RG   European Union Chromosome 3 Arabidopsis Sequencing Consortium;
RG   Institute for Genomic Research;
RG   Kazusa DNA Research Institute;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Blocker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M.,
RA   Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N.,
RA   Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L.,
RA   Weissenbach J., Saurin W., Quetier F., Schafer M., Muller-Auer S.,
RA   Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N.,
RA   Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P.,
RA   Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S.,
RA   Simionati B., Conrad A., Hornischer K., Kauer G., Lohnert T.H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schon O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwalder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.W., Mayer K.F., Kaul S.,
RA   Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
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; Evidence={ECO:0000256|RuleBase:RU079119};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00008574, ECO:0000256|RuleBase:RU079119}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002686; ANM64941.1; -; Genomic_DNA.
DR   RefSeq; NP_001326942.1; NM_001339514.1.
DR   AlphaFoldDB; A0A1I9LQT3; -.
DR   ProteomicsDB; 200091; -.
DR   EnsemblPlants; AT3G51390.2; AT3G51390.2; AT3G51390.
DR   GeneID; 824302; -.
DR   Gramene; AT3G51390.2; AT3G51390.2; AT3G51390.
DR   Araport; AT3G51390; -.
DR   TAIR; AT3G51390; PAT10.
DR   OMA; ANCIGER; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; A0A1I9LQT3; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR22883:SF301; PALMITOYLTRANSFERASE ZDHHC12; 1.
DR   PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU079119};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A1I9LQT3,
KW   ECO:0007829|ProteomicsDB:A0A1I9LQT3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        66..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        202..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        235..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          156..273
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
SQ   SEQUENCE   335 AA;  38648 MW;  F031E4F57E71A8E2 CRC64;
     MGVCCPFLQP WDRARDQCLL NLPCLSDPVR RSSLLLKLAL VALHLVFIGF LFLFDAEFIE
     KTKRDPWYMG CYILLFSATL LQYFVTSGSS PGYVVDAMRD VCEASAMYRN PSTTSIKSES
     VVVNVEGGSA SCPRRPPTPW GKLVLDLYPP GTSIRNLTCG YCHVEQPPRT KHCHDCDRCV
     LQFDHHCVWL GTCIGQKNHS KFWWYICEET TLCIWTLIMY VDYLSNVAKP WWKNAIIILL
     LVILAISLIF VLLLLIFHSY LILTNQSTYE LVRRRRIPYM RNIPGRVHPF SRGIRRNLYN
     VCCGNYNLDS LPTAFELEDR SRPYTCIDML KCRCC
//
DBGET integrated database retrieval system