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PATL5_ARATH
ID   PATL5_ARATH             Reviewed;         668 AA.
AC   Q9M0R2; Q0WP99;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Patellin-5;
GN   Name=PATL5; OrderedLocusNames=At4g09160; ORFNames=T8A17.90;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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-290, 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, 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).
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=CAB78040.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL161514; CAB78040.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82730.1; -; Genomic_DNA.
DR   EMBL; AK229180; BAF01050.1; -; mRNA.
DR   PIR; H85092; H85092.
DR   RefSeq; NP_192655.2; NM_116985.3.
DR   AlphaFoldDB; Q9M0R2; -.
DR   SMR; Q9M0R2; -.
DR   STRING; 3702.AT4G09160.1; -.
DR   iPTMnet; Q9M0R2; -.
DR   PaxDb; Q9M0R2; -.
DR   PRIDE; Q9M0R2; -.
DR   ProteomicsDB; 236367; -.
DR   EnsemblPlants; AT4G09160.1; AT4G09160.1; AT4G09160.
DR   GeneID; 826497; -.
DR   Gramene; AT4G09160.1; AT4G09160.1; AT4G09160.
DR   KEGG; ath:AT4G09160; -.
DR   Araport; AT4G09160; -.
DR   TAIR; locus:2141563; AT4G09160.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_023762_2_0_1; -.
DR   InParanoid; Q9M0R2; -.
DR   OrthoDB; 1182715at2759; -.
DR   PhylomeDB; Q9M0R2; -.
DR   PRO; PR:Q9M0R2; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M0R2; baseline and differential.
DR   Genevisible; Q9M0R2; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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   Cell cycle; Cell division; Cytoplasm; Lipid-binding; Membrane;
KW   Phosphoprotein; Reference proteome; Transport.
FT   CHAIN           1..668
FT                   /note="Patellin-5"
FT                   /id="PRO_0000215589"
FT   DOMAIN          377..552
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   DOMAIN          556..662
FT                   /note="GOLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT   REGION          1..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862,
FT                   ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   668 AA;  75748 MW;  AEAA9C15C82E80FA CRC64;
     MSQDSATTTP PPPLTSDVSM PSGEEDEPKH VTSEEEAPVT SETNLKLPLM PELEESNHTA
     EVVSEKVTPE TMTLESEGLN HAAEDSEQTH EVTPETETAK LEVLNHTAED SEQTHEVTPE
     KETVKSEFLN HVAEDSEQTH EVTPETETVK SEVLNHAAED SEQPRGVTPT PETETSEADT
     SLLVTSETEE PNHAAEDYSE TEPSQKLMLE QRRKYMEVED WTEPELPDEA VLEAAASVPE
     PKQPEPQTPP PPPSTTTSTV ASRSLAEMMN REEAEVEEKQ KIQIPRSLGS FKEETNKISD
     LSETELNALQ ELRHLLQVSQ DSSKTSIWGV PLLKDDRTDV VLLKFLRARD FKPQEAYSML
     NKTLQWRIDF NIEELLDENL GDDLDKVVFM QGQDKENHPV CYNVYGEFQN KDLYQKTFSD
     EEKRERFLRW RIQFLEKSIR NLDFVAGGVS TICQVNDLKN SPGPGKTELR LATKQALHLL
     QDNYPEFVSK QIFINVPWWY LAFYRIISPF MSQRSKSKLV FAGPSRSAET LLKYISPEHV
     PVQYGGLSVD NCECNSDFTH DDIATEITVK PTTKQTVEII VYEKCTIVWE IRVVGWEVSY
     GAEFVPENKE GYTVIIQKPR KMTAKNELVV SHSFKVGEVG RILLTVDNPT STKKMLIYRF
     KVKPLACE
 
 
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