PATL3_ARATH
ID PATL3_ARATH Reviewed; 490 AA.
AC Q56Z59; Q94AG3; Q9C7T9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Patellin-3;
GN Name=PATL3; OrderedLocusNames=At1g72160; ORFNames=T9N14.8;
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 380-490.
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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, 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 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 such as phosphoinositides and promotes
CC their transfer between the different cellular sites (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly membrane-
CC associated. Also cytoplasmic (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: 'Patella' means 'small plate' in Latin.
CC -!- SIMILARITY: Belongs to the patellin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK82462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC067754; AAG51796.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35283.1; -; Genomic_DNA.
DR EMBL; AY048199; AAK82462.1; ALT_INIT; mRNA.
DR EMBL; AY133553; AAM91383.1; -; mRNA.
DR EMBL; AK221110; BAD95021.1; -; mRNA.
DR PIR; A96745; A96745.
DR RefSeq; NP_177361.1; NM_105874.4.
DR AlphaFoldDB; Q56Z59; -.
DR SMR; Q56Z59; -.
DR BioGRID; 28767; 5.
DR IntAct; Q56Z59; 1.
DR STRING; 3702.AT1G72160.1; -.
DR iPTMnet; Q56Z59; -.
DR PaxDb; Q56Z59; -.
DR PRIDE; Q56Z59; -.
DR ProteomicsDB; 226055; -.
DR EnsemblPlants; AT1G72160.1; AT1G72160.1; AT1G72160.
DR GeneID; 843547; -.
DR Gramene; AT1G72160.1; AT1G72160.1; AT1G72160.
DR KEGG; ath:AT1G72160; -.
DR Araport; AT1G72160; -.
DR TAIR; locus:2207016; AT1G72160.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_023762_1_0_1; -.
DR InParanoid; Q56Z59; -.
DR OMA; CTIFQVN; -.
DR OrthoDB; 1182715at2759; -.
DR PhylomeDB; Q56Z59; -.
DR PRO; PR:Q56Z59; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q56Z59; baseline and differential.
DR Genevisible; Q56Z59; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; 1.
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; Cytoplasm; Isopeptide bond;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..490
FT /note="Patellin-3"
FT /id="PRO_0000215587"
FT DOMAIN 202..377
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 353..487
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..99
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 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT CROSSLNK 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q56WK6"
FT CONFLICT 1
FT /note="M -> K (in Ref. 3; AAK82462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 56105 MW; 7E2024BFCBB5C321 CRC64;
MAEEPTTTTL VTPEKLPSPS LTPSEVSEST QDALPTETET LEKVTETNPP ETADTTTKPE
EETAAEHHPP TVTETETAST EKQEVKDEAS QKEVAEEKKS MIPQNLGSFK EESSKLSDLS
NSEKKSLDEL KHLVREALDN HQFTNTPEEV KIWGIPLLED DRSDVVLLKF LRAREFKVKD
SFAMLKNTIK WRKEFKIDEL VEEDLVDDLD KVVFMHGHDR EGHPVCYNVY GEFQNKELYN
KTFSDEEKRK HFLRTRIQFL ERSIRKLDFS SGGVSTIFQV NDMKNSPGLG KKELRSATKQ
AVELLQDNYP EFVFKQAFIN VPWWYLVFYT VIGPFMTPRS KSKLVFAGPS RSAETLFKYI
SPEQVPVQYG GLSVDPCDCN PDFSLEDSAS EITVKPGTKQ TVEIIIYEKC ELVWEIRVTG
WEVSYKAEFV PEEKDAYTVV IQKPRKMRPS DEPVLTHSFK VNELGKVLLT VDNPTSKKKK
LVYRFNVKPL
