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Protein S-acyltransferase 24 (EC 2.3.1.225) (Ankyrin repeat-containing S-palmitoyltransferase) (Palmitoyltransferase TIP1) (Protein TIP GROWTH DEFECTIVE 1) (AtTIP1) (Zinc finger DHHC domain-containing protein TIP1)

 ZDH22_ARATH             Reviewed;         620 AA.
Q52T38; Q0WQT8;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
25-OCT-2017, entry version 106.
RecName: Full=Protein S-acyltransferase 24;
EC=2.3.1.225;
AltName: Full=Ankyrin repeat-containing S-palmitoyltransferase;
AltName: Full=Palmitoyltransferase TIP1;
AltName: Full=Protein TIP GROWTH DEFECTIVE 1;
Short=AtTIP1;
AltName: Full=Zinc finger DHHC domain-containing protein TIP1;
Name=PAT24; Synonyms=TIP1; OrderedLocusNames=At5g20350;
ORFNames=F5O24.240;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=16100337; DOI=10.1105/tpc.105.031237;
Hemsley P.A., Kemp A.C., Grierson C.S.;
"The TIP GROWTH DEFECTIVE1 S-acyltransferase regulates plant cell
growth in Arabidopsis.";
Plant Cell 17:2554-2563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
DISRUPTION PHENOTYPE.
PubMed=8022944; DOI=10.1104/pp.103.3.979;
Schiefelbein J., Galway M., Masucci J., Ford S.;
"Pollen tube and root-hair tip growth is disrupted in a mutant of
Arabidopsis thaliana.";
Plant Physiol. 103:979-985(1993).
[6]
DISRUPTION PHENOTYPE.
AGRICOLA=IND20904399; DOI=10.1046/j.1469-8137.1998.00896.x;
Ryan E., Grierson C.S., Cavell A., Steer M., Dolan L.;
"TIP1 is required for both tip growth and non-tip growth in
Arabidopsis.";
New Phytol. 138:49-58(1998).
[7]
GENE FAMILY, AND FUNCTION.
Hemsley P.A., Taylor L., Grierson C.S.;
"S-acylation: dynamic control of plant development and sigalling by
lipid modification of proteins.";
(In) Proceedings of the 18th international conference on Arabidopsis
research, abstract#139, Beijing (2007).
[8]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GENE FAMILY, AND
NOMENCLATURE.
PubMed=22968831; DOI=10.1104/pp.112.203968;
Batistic O.;
"Genomics and localization of the Arabidopsis DHHC-cysteine-rich
domain S-acyltransferase protein family.";
Plant Physiol. 160:1597-1612(2012).
-!- FUNCTION: Palmitoyltransferase involved in cell growth regulation.
{ECO:0000269|Ref.7}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + [protein]-L-cysteine =
[protein]-S-palmitoyl-L-cysteine + CoA.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in root, leaf, inflorescence stem,
pollen and floral tissue. {ECO:0000269|PubMed:16100337,
ECO:0000269|PubMed:22968831}.
-!- DOMAIN: The DHHC domain is required for palmitoyltransferase
activity.
-!- DISRUPTION PHENOTYPE: Plants have defects in root hair growth and
pollen tube germination. {ECO:0000269|PubMed:16100337,
ECO:0000269|PubMed:8022944, ECO:0000269|Ref.6}.
-!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
{ECO:0000305}.
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EMBL; AY965346; AAX89384.1; -; mRNA.
EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED92834.1; -; Genomic_DNA.
EMBL; AK228596; BAF00511.1; -; mRNA.
RefSeq; NP_197535.2; NM_122042.4.
UniGene; At.22462; -.
ProteinModelPortal; Q52T38; -.
SMR; Q52T38; -.
STRING; 3702.AT5G20350.1; -.
iPTMnet; Q52T38; -.
SwissPalm; Q52T38; -.
PaxDb; Q52T38; -.
EnsemblPlants; AT5G20350.1; AT5G20350.1; AT5G20350.
GeneID; 832157; -.
Gramene; AT5G20350.1; AT5G20350.1; AT5G20350.
KEGG; ath:AT5G20350; -.
Araport; AT5G20350; -.
TAIR; locus:2149309; AT5G20350.
eggNOG; KOG0509; Eukaryota.
eggNOG; COG0666; LUCA.
eggNOG; COG5273; LUCA.
HOGENOM; HOG000243854; -.
InParanoid; Q52T38; -.
KO; K20032; -.
OMA; QAKGYDS; -.
OrthoDB; EOG093605DC; -.
PhylomeDB; Q52T38; -.
BRENDA; 2.3.1.225; 399.
PRO; PR:Q52T38; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q52T38; baseline and differential.
Genevisible; Q52T38; AT.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0000035; F:acyl binding; IDA:TAIR.
GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009932; P:cell tip growth; IMP:TAIR.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR001594; Palmitoyltrfase_DHHC.
Pfam; PF12796; Ank_2; 2.
Pfam; PF01529; DHHC; 1.
SMART; SM00248; ANK; 7.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
PROSITE; PS50216; DHHC; 1.
2: Evidence at transcript level;
Acyltransferase; ANK repeat; Complete proteome; Cytoplasmic vesicle;
Golgi apparatus; Lipoprotein; Membrane; Palmitate; Reference proteome;
Repeat; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 620 Protein S-acyltransferase 24.
/FTId=PRO_0000212915.
TRANSMEM 277 297 Helical. {ECO:0000255}.
TRANSMEM 308 328 Helical. {ECO:0000255}.
TRANSMEM 416 436 Helical. {ECO:0000255}.
TRANSMEM 462 482 Helical. {ECO:0000255}.
REPEAT 64 93 ANK 1.
REPEAT 97 126 ANK 2.
REPEAT 164 193 ANK 3.
REPEAT 197 226 ANK 4.
REPEAT 232 261 ANK 5.
DOMAIN 371 421 DHHC. {ECO:0000255|PROSITE-
ProRule:PRU00067}.
ACT_SITE 401 401 S-palmitoyl cysteine intermediate.
{ECO:0000250}.
SEQUENCE 620 AA; 68234 MW; BF6247CB99911659 CRC64;
MSSEIEVVEE IQSNPKENGE SSSKGIEEES LKNDVYTAAA YGDLEKLHRL VECEGSSVSE
PDALGYYALQ WSALNNRVAV AQYLIEHGGD VNATDHTGQT ALHWSAVRGA IQVAELLLQE
GARVDATDMY GYQATHVAAQ YGQTAFLCHV VSKWNADPDV PDNDGRSPLH WAAYKGFADS
IRLLLFLDAY RGRQDKEGCT PLHWAAIRGN LEACTVLVQA GKKEDLMITD KTGLTPAQLA
AEKNHRQVSF FLGNARSLLE KRCDGSSPLG RLSKLGLAPV LWIMILLLLL VYTNSVVLAS
NLPKLTTGIG ALAWLGFILA TAGLFLFYRC SRKDPGYIRM NIHDPQTMKD DEPLLKIELN
NPALLAGNWT QLCATCKIIR PLRAKHCSTC DRCVEQFDHH CPWVSNCVGK KNKWEFFLFL
LLEVLAMLIT GGVTLARVLS DPSAPSSFGA WMSHVASNHV GALSFLLVEF CLFFSVAVLT
VIQASQISRN ITTNEMANAL RYSYLRGPGG RFRNPYDLGC RRNCSDFLVK GYNEDIECHE
EDATQRPEGI SMMQMQRNPN LQNGNGHVAI DVNPTHNSQS AHVHSANCSH SHNSKSKSDN
VPLGLGLGLS RNPTRPVVSP


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