HACD_ARATH
ID HACD_ARATH Reviewed; 221 AA.
AC Q8VZB2; A8MQH5; Q9LXA0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PASTICCINO 2 {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000305|PubMed:18799749};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase PASTICCINO 2;
DE Short=AtPAS2;
DE Short=HACD;
DE Short=HCD;
DE AltName: Full=Protein PEPINO;
DE Short=PEP;
DE AltName: Full=Protein tyrosine phosphatase-like protein;
GN Name=PAS2; Synonyms=PEP; OrderedLocusNames=At5g10480; ORFNames=F12B17.170;
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 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12472687; DOI=10.1046/j.1365-313x.2002.01456.x;
RA Bellec Y., Harrar Y., Butaeye C., Darnet S., Bellini C., Faure J.-D.;
RT "Pasticcino2 is a protein tyrosine phosphatase-like involved in cell
RT proliferation and differentiation in Arabidopsis.";
RL Plant J. 32:713-722(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND MUTAGENESIS OF
RP SER-72.
RC TISSUE=Leaf, and Shoot;
RX PubMed=12459923; DOI=10.1007/s00427-002-0273-9;
RA Haberer G., Erschadi S., Torres-Ruiz R.A.;
RT "The Arabidopsis gene PEPINO/PASTICCINO2 is required for proliferation
RT control of meristematic and non-meristematic cells and encodes a putative
RT anti-phosphatase.";
RL Dev. Genes Evol. 212:542-550(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=12857804; DOI=10.1104/pp.102.019026;
RA Harrar Y., Bellec Y., Bellini C., Faure J.-D.;
RT "Hormonal control of cell proliferation requires PASTICCINO genes.";
RL Plant Physiol. 132:1217-1227(2003).
RN [7]
RP FUNCTION, INTERACTION WITH CDKA-1, AND SUBCELLULAR LOCATION.
RX PubMed=16698944; DOI=10.1105/tpc.105.040485;
RA Da Costa M., Bach L., Landrieu I., Bellec Y., Catrice O., Brown S.,
RA De Veylder L., Lippens G., Inze D., Faure J.-D.;
RT "Arabidopsis PASTICCINO2 is an antiphosphatase involved in regulation of
RT cyclin-dependent kinase A.";
RL Plant Cell 18:1426-1437(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18799749; DOI=10.1073/pnas.0805089105;
RA Bach L., Michaelson L.V., Haslam R., Bellec Y., Gissot L., Marion J.,
RA Da Costa M., Boutin J.P., Miquel M., Tellier F., Domergue F., Markham J.E.,
RA Beaudoin F., Napier J.A., Faure J.D.;
RT "The very-long-chain hydroxy fatty acyl-CoA dehydratase PASTICCINO2 is
RT essential and limiting for plant development.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14727-14731(2008).
RN [9]
RP INTERACTION WITH PAS1.
RX PubMed=20145257; DOI=10.1105/tpc.109.071209;
RA Roudier F., Gissot L., Beaudoin F., Haslam R., Michaelson L., Marion J.,
RA Molino D., Lima A., Bach L., Morin H., Tellier F., Palauqui J.C.,
RA Bellec Y., Renne C., Miquel M., Dacosta M., Vignard J., Rochat C.,
RA Markham J.E., Moreau P., Napier J., Faure J.D.;
RT "Very-long-chain fatty acids are involved in polar auxin transport and
RT developmental patterning in Arabidopsis.";
RL Plant Cell 22:364-375(2010).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21896643; DOI=10.1242/jcs.074575;
RA Bach L., Gissot L., Marion J., Tellier F., Moreau P.,
RA Satiat-Jeunemaitre B., Palauqui J.C., Napier J.A., Faure J.D.;
RT "Very-long-chain fatty acids are required for cell plate formation during
RT cytokinesis in Arabidopsis thaliana.";
RL J. Cell Sci. 124:3223-3234(2011).
CC -!- FUNCTION: Catalyzes the third of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of two carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme
CC catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into
CC trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation.
CC Thereby, it participates in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators. May be an anti-
CC phosphatase that prevents CDKA-1 dephosphorylation and activation.
CC Involved in the hormonal control of cell division and differentiation.
CC Required for proliferation control of meristematic and non-meristematic
CC cells. Negative regulator of the cell cycle.
CC {ECO:0000269|PubMed:12459923, ECO:0000269|PubMed:12472687,
CC ECO:0000269|PubMed:12857804, ECO:0000269|PubMed:16698944,
CC ECO:0000269|PubMed:18799749, ECO:0000269|PubMed:21896643}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain
CC (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; EC=4.2.1.134;
CC Evidence={ECO:0000305|PubMed:18799749};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000305|PubMed:18799749}.
CC -!- SUBUNIT: Interacts with CDKA-1; but only with the 'Tyr-15'
CC phosphorylated protein. Interacts with PAS1. Part of the fatty acid
CC elongase complex which contains a beta-ketoacyl-CoA synthase (KCS), a
CC beta-ketoacyl-CoA reductase (KCR), a beta-hydroxyacyl-CoA dehydratase
CC (HCD) and an enoyl-CoA reductase (ECR) (Probable).
CC {ECO:0000305|PubMed:16698944, ECO:0000305|PubMed:20145257}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18799749}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:16698944}. Nucleus
CC {ECO:0000269|PubMed:16698944}. Note=Found in the cytoplasm of dividing
CC cells but moves into the nucleus upon cell differentiation.
CC {ECO:0000269|PubMed:16698944}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VZB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VZB2-2; Sequence=VSP_037155, VSP_037156;
CC -!- TISSUE SPECIFICITY: High expression in young seedlings, roots, root
CC tips, flowers and young siliques. Lower levels in leaves and stems.
CC {ECO:0000269|PubMed:12472687, ECO:0000269|PubMed:21896643}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal when homozygote.
CC {ECO:0000269|PubMed:18799749, ECO:0000269|PubMed:21896643}.
CC -!- MISCELLANEOUS: Plants with reduced expression of PAS2 show impaired
CC embryo and seedling development associated with cell de-differentiation
CC and proliferation. Root growth is reduced, due to a delay in cell plate
CC establishment during cytokinesis (PubMed:21896643).
CC {ECO:0000305|PubMed:21896643}.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC family. {ECO:0000305}.
CC -!- CAUTION: Shares some similarity with tyrosine phosphatase proteins but
CC it has probably no phosphatase activity since the potential active site
CC Cys residue in position 65 is replaced by Gly. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB89395.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY047708; AAL05403.1; -; mRNA.
DR EMBL; AJ506746; CAD45041.1; -; mRNA.
DR EMBL; AL353995; CAB89395.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91548.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91549.1; -; Genomic_DNA.
DR EMBL; AY065090; AAL38266.1; -; mRNA.
DR EMBL; BT006269; AAP13377.1; -; mRNA.
DR PIR; T49991; T49991.
DR RefSeq; NP_001078566.1; NM_001085097.1. [Q8VZB2-2]
DR RefSeq; NP_196610.2; NM_121086.5. [Q8VZB2-1]
DR AlphaFoldDB; Q8VZB2; -.
DR BioGRID; 16190; 11.
DR STRING; 3702.AT5G10480.3; -.
DR PaxDb; Q8VZB2; -.
DR ProteomicsDB; 247215; -. [Q8VZB2-1]
DR EnsemblPlants; AT5G10480.1; AT5G10480.1; AT5G10480. [Q8VZB2-1]
DR EnsemblPlants; AT5G10480.2; AT5G10480.2; AT5G10480. [Q8VZB2-2]
DR GeneID; 830912; -.
DR Gramene; AT5G10480.1; AT5G10480.1; AT5G10480. [Q8VZB2-1]
DR Gramene; AT5G10480.2; AT5G10480.2; AT5G10480. [Q8VZB2-2]
DR KEGG; ath:AT5G10480; -.
DR Araport; AT5G10480; -.
DR eggNOG; KOG3187; Eukaryota.
DR InParanoid; Q8VZB2; -.
DR PhylomeDB; Q8VZB2; -.
DR BioCyc; ARA:AT5G10480-MON; -.
DR BioCyc; MetaCyc:AT5G10480-MON; -.
DR BRENDA; 4.2.1.134; 399.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q8VZB2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZB2; baseline and differential.
DR Genevisible; Q8VZB2; AT.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0102343; F:3-hydroxy-arachidoyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0102344; F:3-hydroxy-behenoyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0102345; F:3-hydroxy-lignoceroyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IBA:GO_Central.
DR GO; GO:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; PTHR11035; 1.
DR Pfam; PF04387; PTPLA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..221
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT PASTICCINO 2"
FT /id="PRO_0000372480"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..51
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..100
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..184
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 154
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037155"
FT VAR_SEQ 26
FT /note="Q -> M (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037156"
FT MUTAGEN 72
FT /note="S->F: Loss of proliferation control."
FT /evidence="ECO:0000269|PubMed:12459923"
SQ SEQUENCE 221 AA; 25327 MW; 8FD3F79DDF8AE1B7 CRC64;
MAGFLSVVRR VYLTLYNWIV FAGWAQVLYL AITTLKETGY ENVYDAIEKP LQLAQTAAVL
EILHGLVGLV RSPVSATLPQ IGSRLFLTWG ILYSFPEVRS HFLVTSLVIS WSITEIIRYS
FFGFKEALGF APSWHLWLRY SSFLLLYPTG ITSEVGLIYL ALPHIKTSEM YSVRMPNILN
FSFDFFYATI LVLAIYVPGS PHMYRYMLGQ RKRALSKSKR E
