PAS1_ARATH
ID PAS1_ARATH Reviewed; 635 AA.
AC Q7DMA9; O64403; Q93ZT7; Q9M326;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase PASTICCINO1;
DE EC=5.2.1.8;
DE AltName: Full=70 kDa peptidyl-prolyl isomerase;
DE AltName: Full=FK506-binding protein 72;
DE Short=AtFKBP72;
DE AltName: Full=Immunophilin FKBP72;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase FKBP72;
DE Short=PPIase FKBP72;
DE AltName: Full=Rotamase;
GN Name=PAS1; Synonyms=DEI1, FKBP70, FKBP72; OrderedLocusNames=At3g54010;
GN ORFNames=F5K20.310;
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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=9566922; DOI=10.1128/mcb.18.5.3034;
RA Vittorioso P., Cowling R., Faure J.-D., Caboche M., Bellini C.;
RT "Mutation in the Arabidopsis PASTICCINO1 gene, which encodes a new FK506-
RT binding protein-like protein, has a dramatic effect on plant development.";
RL Mol. Cell. Biol. 18:3034-3043(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder 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.X.,
RA Kaul S., 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 [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 FUNCTION.
RX PubMed=9449673; DOI=10.1242/dev.125.5.909;
RA Faure J.-D., Vittorioso P., Santoni V., Fraisier V., Prinsen E.,
RA Barlier I., Van Onckelen H., Caboche M., Bellini C.;
RT "The PASTICCINO genes of Arabidopsis thaliana are involved in the control
RT of cell division and differentiation.";
RL Development 125:909-918(1998).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CALMODULIN.
RX DOI=10.1016/S0168-9452(01)00437-X;
RA Carol R.J., Breiman A., Erel N., Vittorioso P., Bellini C.;
RT "PASTICCINO1 (AtFKBP70) is a nuclear-localised immunophilin required during
RT Arabidopsis thaliana embryogenesis.";
RL Plant Sci. 161:527-535(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [8]
RP INTERACTION WITH RPM1.
RX PubMed=15133126; DOI=10.1091/mbc.e03-11-0831;
RA Geisler M., Girin M., Brandt S., Vincenzetti V., Plaza S., Paris N.,
RA Kobae Y., Maeshima M., Billion K., Kolukisaoglu U.H., Schulz B.,
RA Martinoia E.;
RT "Arabidopsis immunophilin-like TWD1 functionally interacts with vacuolar
RT ABC transporters.";
RL Mol. Biol. Cell 15:3393-3405(2004).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15047905; DOI=10.1104/pp.103.031005;
RA He Z., Li L., Luan S.;
RT "Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in
RT Arabidopsis.";
RL Plant Physiol. 134:1248-1267(2004).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH NAC089, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16803883; DOI=10.1074/jbc.m601815200;
RA Smyczynski C., Roudier F., Gissot L., Vaillant E., Grandjean O., Morin H.,
RA Masson T., Bellec Y., Geelen D., Faure J.D.;
RT "The C terminus of the immunophilin PASTICCINO1 is required for plant
RT development and for interaction with a NAC-like transcription factor.";
RL J. Biol. Chem. 281:25475-25484(2006).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH THE ELONGASE COMPLEX.
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).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). Essential protein regulating cell
CC division, adhesion and elongation throughout the plant development and
CC embryogenesis. Required for the spatial organization of apical
CC meristems. Involved in the hormonal control of cell division and
CC differentiation mediated by cytokinins and auxin. Regulates the
CC function of NAC089 transcription factor by controlling its targeting to
CC the nucleus upon plant cell division. Interacts with enzymes of the
CC fatty acid elongase complex and favors the generation of very-long-
CC chain fatty acids (VLCFAs) required for polar auxin transport and
CC tissue patterning during plant development. {ECO:0000250,
CC ECO:0000269|PubMed:12857804, ECO:0000269|PubMed:16803883,
CC ECO:0000269|PubMed:20145257, ECO:0000269|PubMed:9449673,
CC ECO:0000269|PubMed:9566922, ECO:0000269|Ref.6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBUNIT: Interacts with calmodulin (CaM). Interacts with RPM1 and
CC NAC089. Interacts with the elongase complex core members KCR1, PAS2 and
CC CER10. {ECO:0000269|PubMed:15133126, ECO:0000269|PubMed:16803883,
CC ECO:0000269|PubMed:20145257, ECO:0000269|Ref.6}.
CC -!- INTERACTION:
CC Q7DMA9; Q94F58: NAC089; NbExp=6; IntAct=EBI-637668, EBI-2319707;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type IV membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000305}. Nucleus {ECO:0000269|PubMed:16803883,
CC ECO:0000269|Ref.6}. Note=Relocalization from the cytoplasm into the
CC nucleus is induced by auxin treatment and in association with NAC089.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PAS1-D;
CC IsoId=Q7DMA9-1; Sequence=Displayed;
CC Name=2; Synonyms=PAS1-A;
CC IsoId=Q7DMA9-2; Sequence=VSP_015492;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:9566922}.
CC -!- INDUCTION: By cytokinins, and to a lower extent by auxin.
CC {ECO:0000269|PubMed:9566922}.
CC -!- DISRUPTION PHENOTYPE: Plants fail to develop apical hook in the dark
CC and exhibit abnormal embryogenesis from the heart stage. Deficiency in
CC lateral root formation and abnormal patterning of the embryo apex,
CC which leads to defective cotyledon organogenesis like small and thick
CC hypocotyl, finger-shaped cotyledons and small fused leaves. Ectopic
CC cell proliferation in the presence of cytokinins.
CC {ECO:0000269|PubMed:12857804, ECO:0000269|PubMed:16803883,
CC ECO:0000269|PubMed:20145257}.
CC -!- MISCELLANEOUS: 'Pasticcino' means 'small cake' in Italian.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88363.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U77365; AAC39444.1; -; mRNA.
DR EMBL; U77366; AAC39445.1; -; mRNA.
DR EMBL; AL132960; CAB88363.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79174.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79175.1; -; Genomic_DNA.
DR EMBL; AY056265; AAL07114.1; -; mRNA.
DR EMBL; AY096635; AAM20285.1; -; mRNA.
DR PIR; T45941; T45941.
DR RefSeq; NP_566993.1; NM_115261.4. [Q7DMA9-1]
DR RefSeq; NP_850701.1; NM_180370.3. [Q7DMA9-2]
DR AlphaFoldDB; Q7DMA9; -.
DR SMR; Q7DMA9; -.
DR BioGRID; 9885; 5.
DR IntAct; Q7DMA9; 3.
DR STRING; 3702.AT3G54010.1; -.
DR PaxDb; Q7DMA9; -.
DR PRIDE; Q7DMA9; -.
DR ProteomicsDB; 226057; -. [Q7DMA9-1]
DR EnsemblPlants; AT3G54010.1; AT3G54010.1; AT3G54010. [Q7DMA9-1]
DR EnsemblPlants; AT3G54010.2; AT3G54010.2; AT3G54010. [Q7DMA9-2]
DR GeneID; 824568; -.
DR Gramene; AT3G54010.1; AT3G54010.1; AT3G54010. [Q7DMA9-1]
DR Gramene; AT3G54010.2; AT3G54010.2; AT3G54010. [Q7DMA9-2]
DR KEGG; ath:AT3G54010; -.
DR Araport; AT3G54010; -.
DR TAIR; locus:2084435; AT3G54010.
DR eggNOG; KOG0543; Eukaryota.
DR InParanoid; Q7DMA9; -.
DR OrthoDB; 897391at2759; -.
DR PhylomeDB; Q7DMA9; -.
DR PRO; PR:Q7DMA9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7DMA9; baseline and differential.
DR Genevisible; Q7DMA9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0005634; C:nucleus; ISS:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IMP:TAIR.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:TAIR.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:TAIR.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 3.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00254; FKBP_C; 3.
DR Pfam; PF13174; TPR_6; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Auxin signaling pathway; Cytokinin signaling pathway;
KW Cytoplasm; Endoplasmic reticulum; Isomerase; Membrane; Nucleus;
KW Reference proteome; Repeat; Rotamase; TPR repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..635
FT /note="Peptidyl-prolyl cis-trans isomerase PASTICCINO1"
FT /id="PRO_0000075336"
FT TRANSMEM 609..629
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 51..147
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 175..260
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 291..383
FT /note="PPIase FKBP-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 400..433
FT /note="TPR 1"
FT REPEAT 449..482
FT /note="TPR 2"
FT REPEAT 483..516
FT /note="TPR 3"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..546
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 569..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9566922"
FT /id="VSP_015492"
FT CONFLICT 88
FT /note="N -> K (in Ref. 1; AAC39445)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="Missing (in Ref. 1; AAC39444/AAC39445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 635 AA; 71797 MW; 561EEBAC77BFE241 CRC64;
MAVGDQTEQN YLPKKKKSET EDDKRRKKIV PGSLLKAVVR PGGGDSSPVD GDQVIYHCTV
RTLDGVVVES TRSESGGRGV PIRDVLGNSK MILGLLEGIP TMHKGEIAMF KMKPEMHYAE
IDCPVSAPEN FPKDDELHFE IELLDFSKAK IASDDLGVIK KILNEGEGWE SPREPYEVKA
RISAKSGDGH VIFSHTEEPY FFTFGKSEVP KGLEIGIGTM ARKEKAVIYV RKQYLTESPL
LHIDQDLEEV HFEVELVHFI QVRDMLGDGR LIKRRIRDGR GEFPMDCPLQ DSRLSVHYKG
MLLNEEKTVF YDSKIDNNDQ PLEFSSGEGL VPEGFEMCTR LMLPGEIALV TCPPDYAYDK
FPRPPGVSEG AHVQWEIELL GFETPRDWTG LNFQSIMDEA DKIRSTGNRL FKEGKFELAK
AKYEKVLREF NHVNPQDEDE GKIFGDTRNM LHLNVAACLL KMGEWRKSIE TCNKVLEAKP
GHVKGLYRRG MAYIAGGEYD DARNDFNMMI KVDKSSEADA TAALLKLKQK EQEAESKARK
QFKGLFDKRP GEITEVGSEI REESKTIEEV DETKDNDDDE TLEEEGATTV STERKRKWSE
KAWPFLKNVM LQIGIQLGVV LIGILIFQFV SAKFT
