PATL1_ARATH
ID PATL1_ARATH Reviewed; 573 AA.
AC Q56WK6; Q9C7U0;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Patellin-1;
GN Name=PATL1; OrderedLocusNames=At1g72150; ORFNames=T9N14.1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-573.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15466235; DOI=10.1104/pp.104.045369;
RA Peterman T.K., Ohol Y.M., McReynolds L.J., Luna E.J.;
RT "Patellin1, a novel Sec14-like protein, localizes to the cell plate and
RT binds phosphoinositides.";
RL Plant Physiol. 136:3080-3094(2004).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-285, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=19292762; DOI=10.1111/j.1365-313x.2009.03862.x;
RA Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.;
RT "Tandem affinity purification and mass spectrometric analysis of
RT ubiquitylated proteins in Arabidopsis.";
RL Plant J. 59:344-358(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP INTERACTION WITH AMSH3.
RX PubMed=20543027; DOI=10.1105/tpc.110.075952;
RA Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D.,
RA Geldner N., Chory J., Schwechheimer C.;
RT "The deubiquitinating enzyme AMSH3 is required for intracellular
RT trafficking and vacuole biogenesis in Arabidopsis thaliana.";
RL Plant Cell 22:1826-1837(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Carrier protein that may be involved in membrane-trafficking
CC events associated with cell plate formation during cytokinesis. Binds
CC to some hydrophobic molecules and promotes their transfer between the
CC different cellular sites. Binds to phosphoinositides with a preference
CC for PtdIns(5)P, PtdIns(4,5)P2 and PtdIns(3)P.
CC {ECO:0000269|PubMed:15466235}.
CC -!- SUBUNIT: Interacts with the deubiquitinating enzyme AMSH3.
CC {ECO:0000269|PubMed:20543027}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15466235}. Cytoplasm
CC {ECO:0000269|PubMed:15466235}. Note=Mainly membrane-associated. Also
CC cytoplasmic. Cell plate during cell division.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously with higher levels in
CC expanding roots and leaves (at protein level).
CC {ECO:0000269|PubMed:15466235}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during flower development (at protein
CC level). {ECO:0000269|PubMed:15466235}.
CC -!- MISCELLANEOUS: 'Patella' means 'small plate' in Latin.
CC -!- SIMILARITY: Belongs to the patellin family. {ECO:0000305}.
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DR EMBL; AC067754; AAG51793.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35282.1; -; Genomic_DNA.
DR EMBL; AY045913; AAK76587.1; -; mRNA.
DR EMBL; AY113865; AAM44913.1; -; mRNA.
DR EMBL; AK222034; BAD94747.1; -; mRNA.
DR PIR; H96744; H96744.
DR RefSeq; NP_177360.1; NM_105873.3.
DR AlphaFoldDB; Q56WK6; -.
DR SMR; Q56WK6; -.
DR BioGRID; 28766; 7.
DR IntAct; Q56WK6; 2.
DR MINT; Q56WK6; -.
DR STRING; 3702.AT1G72150.1; -.
DR iPTMnet; Q56WK6; -.
DR MetOSite; Q56WK6; -.
DR PaxDb; Q56WK6; -.
DR PRIDE; Q56WK6; -.
DR ProteomicsDB; 236435; -.
DR EnsemblPlants; AT1G72150.1; AT1G72150.1; AT1G72150.
DR GeneID; 843546; -.
DR Gramene; AT1G72150.1; AT1G72150.1; AT1G72150.
DR KEGG; ath:AT1G72150; -.
DR Araport; AT1G72150; -.
DR TAIR; locus:2207001; AT1G72150.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_023762_1_0_1; -.
DR InParanoid; Q56WK6; -.
DR OMA; LAACEFN; -.
DR OrthoDB; 1182715at2759; -.
DR PhylomeDB; Q56WK6; -.
DR PRO; PR:Q56WK6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q56WK6; baseline and differential.
DR Genevisible; Q56WK6; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009860; P:pollen tube growth; IEP:TAIR.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR044834; PATL.
DR PANTHER; PTHR45932; PTHR45932; 2.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Isopeptide bond; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..573
FT /note="Patellin-1"
FT /id="PRO_0000215585"
FT DOMAIN 295..468
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 471..572
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..157
FT /evidence="ECO:0000255"
FT COMPBIAS 40..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 29
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q56Z59"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19292762"
SQ SEQUENCE 573 AA; 64046 MW; 1F0AC3BB0784FC5D CRC64;
MAQEEVQKSA DVAAAPVVKE KPITDKEVTI PTPVAEKEEV AAPVSDEKAV PEKEVTPEKE
APAAEAEKSV SVKEEETVVV AEKVVVLTAE EVQKKALEEF KELVREALNK REFTAPVTPV
KEEKTEEKKT EEETKEEEKT EEKKEETTTE VKVEEEKPAV PAAEEEKSSE AAPVETKSEE
KPEEKAEVTT EKASSAEEDG TKTVEAIEES IVSVSPPESA VAPVVVETVA VAEAEPVEPE
EVSIWGVPLL QDERSDVILT KFLRARDFKV KEALTMLKNT VQWRKENKID ELVESGEEVS
EFEKMVFAHG VDKEGHVVIY SSYGEFQNKE LFSDKEKLNK FLSWRIQLQE KCVRAIDFSN
PEAKSSFVFV SDFRNAPGLG KRALWQFIRR AVKQFEDNYP EFAAKELFIN VPWWYIPYYK
TFGSIITSPR TRSKMVLAGP SKSADTIFKY IAPEQVPVKY GGLSKDTPLT EETITEAIVK
PAANYTIELP ASEACTLSWE LRVLGADVSY GAQFEPTTEG SYAVIVSKTR KIGSTDEPVI
TDSFKVGEPG KIVITIDNQT SKKKKVLYRF KTQ
