PATL4_ARATH
ID PATL4_ARATH Reviewed; 540 AA.
AC Q94C59; Q9SA84;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Patellin-4;
GN Name=PATL4; OrderedLocusNames=At1g30690; ORFNames=T5I8.14;
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP IDENTIFICATION BY 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 IDENTIFICATION BY 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).
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}.
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DR EMBL; AC007060; AAD25756.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31260.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31261.1; -; Genomic_DNA.
DR EMBL; AY035162; AAK59666.1; -; mRNA.
DR EMBL; BT000959; AAN41359.1; -; mRNA.
DR PIR; D86432; D86432.
DR RefSeq; NP_001031119.1; NM_001036042.3.
DR RefSeq; NP_564360.1; NM_102805.3.
DR AlphaFoldDB; Q94C59; -.
DR SMR; Q94C59; -.
DR BioGRID; 25184; 9.
DR IntAct; Q94C59; 1.
DR STRING; 3702.AT1G30690.2; -.
DR iPTMnet; Q94C59; -.
DR PaxDb; Q94C59; -.
DR PRIDE; Q94C59; -.
DR ProteomicsDB; 236355; -.
DR EnsemblPlants; AT1G30690.1; AT1G30690.1; AT1G30690.
DR EnsemblPlants; AT1G30690.2; AT1G30690.2; AT1G30690.
DR GeneID; 839949; -.
DR Gramene; AT1G30690.1; AT1G30690.1; AT1G30690.
DR Gramene; AT1G30690.2; AT1G30690.2; AT1G30690.
DR KEGG; ath:AT1G30690; -.
DR Araport; AT1G30690; -.
DR TAIR; locus:2204594; AT1G30690.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_023762_1_0_1; -.
DR InParanoid; Q94C59; -.
DR OMA; WYYAFHA; -.
DR OrthoDB; 1182715at2759; -.
DR PhylomeDB; Q94C59; -.
DR PRO; PR:Q94C59; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94C59; baseline and differential.
DR Genevisible; Q94C59; AT.
DR GO; GO:0005829; C:cytosol; 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: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; 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; 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 Cell cycle; Cell division; Coiled coil; Cytoplasm; Isopeptide bond;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Transport;
KW Ubl conjugation.
FT CHAIN 1..540
FT /note="Patellin-4"
FT /id="PRO_0000215588"
FT DOMAIN 258..428
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 433..534
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 89..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..183
FT /evidence="ECO:0000255"
FT COMPBIAS 89..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q56WK6"
FT CONFLICT 286
FT /note="H -> N (in Ref. 3; AAK59666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 61189 MW; 0C2590D518ACFB58 CRC64;
MTAEVKVEEK QVESEVVIAP AVVPEETTVK AVVEETKVEE DESKPEGVEK SASFKEESDF
FADLKESEKK ALSDLKSKLE EAIVDNTLLK TKKKESSPMK EKKEEVVKPE AEVEKKKEEA
AEEKVEEEKK SEAVVTEEAP KAETVEAVVT EEIIPKEEVT TVVEKVEEET KEEEKKTEDV
VTEEVKAETI EVEDEDESVD KDIELWGVPL LPSKGAESTD VILLKFLRAR DFKVNEAFEM
LKKTLKWRKQ NKIDSILGEE FGEDLATAAY MNGVDRESHP VCYNVHSEEL YQTIGSEKNR
EKFLRWRFQL MEKGIQKLNL KPGGVTSLLQ IHDLKNAPGV SRTEIWVGIK KVIETLQDNY
PEFVSRNIFI NVPFWFYAMR AVLSPFLTQR TKSKFVVARP AKVRETLLKY IPADELPVQY
GGFKTVDDTE FSNETVSEVV VKPGSSETIE IPAPETEGTL VWDIAVLGWE VNYKEEFVPT
EEGAYTVIVQ KVKKMGANEG PIRNSFKNSQ AGKIVLTVDN VSGKKKKVLY RYRTKTESSS
