PATL2_ARATH
ID PATL2_ARATH Reviewed; 683 AA.
AC Q56ZI2; Q9SK94;
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-2;
GN Name=PATL2; OrderedLocusNames=At1g22530; ORFNames=F12K8.13;
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 620-683.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, 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 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 -!- SUBUNIT: Interacts with the deubiquitinating enzyme AMSH3.
CC {ECO:0000269|PubMed:20543027}.
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}.
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DR EMBL; AC006551; AAF18525.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30253.1; -; Genomic_DNA.
DR EMBL; AY091145; AAM14094.1; -; mRNA.
DR EMBL; AY133810; AAM91744.1; -; mRNA.
DR EMBL; AK220983; BAD94580.1; -; mRNA.
DR PIR; E86358; E86358.
DR RefSeq; NP_173669.1; NM_102102.3.
DR AlphaFoldDB; Q56ZI2; -.
DR SMR; Q56ZI2; -.
DR BioGRID; 24098; 5.
DR STRING; 3702.AT1G22530.1; -.
DR iPTMnet; Q56ZI2; -.
DR PaxDb; Q56ZI2; -.
DR PRIDE; Q56ZI2; -.
DR ProteomicsDB; 236792; -.
DR EnsemblPlants; AT1G22530.1; AT1G22530.1; AT1G22530.
DR GeneID; 838859; -.
DR Gramene; AT1G22530.1; AT1G22530.1; AT1G22530.
DR KEGG; ath:AT1G22530; -.
DR Araport; AT1G22530; -.
DR TAIR; locus:2009502; AT1G22530.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_023762_1_0_1; -.
DR InParanoid; Q56ZI2; -.
DR OrthoDB; 1182715at2759; -.
DR PhylomeDB; Q56ZI2; -.
DR PRO; PR:Q56ZI2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q56ZI2; baseline and differential.
DR Genevisible; Q56ZI2; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071365; P:cellular response to auxin stimulus; IGI:TAIR.
DR GO; GO:1901703; P:protein localization involved in auxin polar transport; IGI: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; 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; 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..683
FT /note="Patellin-2"
FT /id="PRO_0000215586"
FT DOMAIN 404..576
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 580..681
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..163
FT /evidence="ECO:0000255"
FT COMPBIAS 124..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..279
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 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CROSSLNK 394
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q56WK6"
SQ SEQUENCE 683 AA; 76008 MW; E0626F746EDC15AB CRC64;
MAQEEIQKPT ASVPVVKEET PAPVKEVEVP VTTEKAVAAP APEATEEKVV SEVAVPETEV
TAVKEEEVAT GKEILQSESF KEEGYLASEL QEAEKNALAE LKELVREALN KREFTAPPPP
PAPVKEEKVE EKKTEETEEK KEEVKTEEKS LEAETKEEEK SAAPATVETK KEEILAAPAP
IVAETKKEET PVAPAPVETK PAAPVVAETK KEEILPAAPV TTETKVEEKV VPVETTPAAP
VTTETKEEEK AAPVTTETKE EEKAAPGETK KEEKATASTQ VKRASKFIKD IFVSVTTSEK
KKEEEKPAVV TIEKAFAADQ EEETKTVEAV EESIVSITLP ETAAYVEPEE VSIWGIPLLE
DERSDVILLK FLRARDFKVK EAFTMLKNTV QWRKENKIDD LVSEDLEGSE FEKLVFTHGV
DKQGHVVIYS SYGEFQNKEI FSDKEKLSKF LKWRIQFQEK CVRSLDFSPE AKSSFVFVSD
FRNAPGLGQR ALWQFIKRAV KQFEDNYPEF VAKELFINVP WWYIPYYKTF GSIITSPRTR
SKMVLSGPSK SAETIFKYVA PEVVPVKYGG LSKDSPFTVE DGVTEAVVKS TSKYTIDLPA
TEGSTLSWEL RVLGADVSYG AQFEPSNEAS YTVIVSKNRK VGLTDEPVIT DSFKASEAGK
VVITIDNQTF KKKKVLYRSK TQA
