FPP3_ARATH
ID FPP3_ARATH Reviewed; 615 AA.
AC Q9MA92;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Filament-like plant protein 3 {ECO:0000303|PubMed:11972898};
DE Short=AtFPP3 {ECO:0000303|PubMed:11972898};
DE AltName: Full=Protein VESICLE TETHERING 1 {ECO:0000303|PubMed:25541219};
GN Name=FPP3 {ECO:0000303|PubMed:11972898};
GN Synonyms=VETH1 {ECO:0000303|PubMed:25541219};
GN OrderedLocusNames=At3g05270 {ECO:0000312|Araport:AT3G05270};
GN ORFNames=T12H1.24 {ECO:0000312|EMBL:AAF27033.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11972898; DOI=10.1186/1471-2164-3-9;
RA Gindullis F., Rose A., Patel S., Meier I.;
RT "Four signature motifs define the first class of structurally related large
RT coiled-coil proteins in plants.";
RL BMC Genomics 3:9-9(2002).
RN [4]
RP FUNCTION, INTERACTION WITH COG2, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25541219; DOI=10.1093/pcp/pcu197;
RA Oda Y., Iida Y., Nagashima Y., Sugiyama Y., Fukuda H.;
RT "Novel coiled-coil proteins regulate exocyst association with cortical
RT microtubules in xylem cells via the conserved oligomeric golgi-complex 2
RT protein.";
RL Plant Cell Physiol. 56:277-286(2015).
CC -!- FUNCTION: Ensures, when in complex with COG2 and FPP2/VETH2, the
CC correct secondary cell wall (SCW) deposition pattern by recruiting
CC exocyst components to cortical microtubules in xylem cells during
CC secondary cell wall deposition by recruiting EXO70A1.
CC {ECO:0000269|PubMed:25541219}.
CC -!- SUBUNIT: Interacts with WPP/MAF proteins (By similarity). Binds to
CC COG2; this interaction promotes the association between cortical
CC microtubules and EXO70A1 (PubMed:25541219). {ECO:0000250,
CC ECO:0000269|PubMed:25541219}.
CC -!- SUBCELLULAR LOCATION: Vesicle {ECO:0000269|PubMed:25541219}.
CC Note=Present in vesicle-like small compartments which exhibit
CC microtubule plus-end-directed and end-tracking dynamics.
CC {ECO:0000269|PubMed:25541219}.
CC -!- TISSUE SPECIFICITY: Accumulates in preferentially xylem cells.
CC {ECO:0000269|PubMed:25541219}.
CC -!- SIMILARITY: Belongs to the FPP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27033.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009177; AAF27033.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74213.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74214.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64796.1; -; Genomic_DNA.
DR RefSeq; NP_001118579.1; NM_001125107.2.
DR RefSeq; NP_001326801.1; NM_001337574.1.
DR RefSeq; NP_187178.2; NM_111400.3.
DR AlphaFoldDB; Q9MA92; -.
DR SMR; Q9MA92; -.
DR BioGRID; 5026; 1.
DR STRING; 3702.AT3G05270.2; -.
DR iPTMnet; Q9MA92; -.
DR PaxDb; Q9MA92; -.
DR PRIDE; Q9MA92; -.
DR ProteomicsDB; 229998; -.
DR EnsemblPlants; AT3G05270.1; AT3G05270.1; AT3G05270.
DR EnsemblPlants; AT3G05270.2; AT3G05270.2; AT3G05270.
DR EnsemblPlants; AT3G05270.3; AT3G05270.3; AT3G05270.
DR GeneID; 819691; -.
DR Gramene; AT3G05270.1; AT3G05270.1; AT3G05270.
DR Gramene; AT3G05270.2; AT3G05270.2; AT3G05270.
DR Gramene; AT3G05270.3; AT3G05270.3; AT3G05270.
DR KEGG; ath:AT3G05270; -.
DR Araport; AT3G05270; -.
DR TAIR; locus:2096304; AT3G05270.
DR eggNOG; ENOG502QQJ4; Eukaryota.
DR HOGENOM; CLU_012828_1_0_1; -.
DR InParanoid; Q9MA92; -.
DR OMA; PMESTCE; -.
DR OrthoDB; 190231at2759; -.
DR PhylomeDB; Q9MA92; -.
DR PRO; PR:Q9MA92; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MA92; baseline and differential.
DR Genevisible; Q9MA92; AT.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:TAIR.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:TAIR.
DR GO; GO:0060178; P:regulation of exocyst localization; IDA:TAIR.
DR InterPro; IPR008587; FPP_plant.
DR Pfam; PF05911; FPP; 3.
PE 1: Evidence at protein level;
KW Coiled coil; Reference proteome.
FT CHAIN 1..615
FT /note="Filament-like plant protein 3"
FT /id="PRO_0000347201"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..121
FT /evidence="ECO:0000255"
FT COILED 148..211
FT /evidence="ECO:0000255"
FT COILED 327..563
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 69646 MW; 0BC30870AA6B8DE3 CRC64;
MDRRSWLWRR KSSEKSPGET ESTGSVSSHS ERFSDDQRSQ SPELNSKPVT REEEATADIK
ILTERLSAAL LNVSLKEDLA KQHAKVAEEA VSGWEKAENE AAALKQQLDA STSKVSALED
RNSHLDSALK ECVRQLWQGR EEQNQKIEEA INNKCKEWET TKSQLEARIE ELQARQDVTT
SSVHEDLYPK LEALEKENSA LKLQLLSKSE EVKIRTIERD LSTQAAESAS KQQLEGIKKL
TKLEAECRKL RVMVRRSDNS SDLKSSIDNQ SDYSGRVSFS DNEMQSPSEK IIGKSSMATS
VDIGLMDDFL EMEKLAALPH SEPGRKHSES NKELEKSNAH VNQLKHELKT SLRRISELEE
KVEMVEVEKL QLEMALNGSK EQIEALQSRL KEIEGKLSEM KKLEAENQEL ELLLGESGKQ
MEDLQRQLNK AQVNLSELET RRAEKLELTM CLNGTKKQLE TSQNRLKETE RKLTELQTLL
HLTKDAKEAA EDGLKAANGK TEAIESRLKD VEAEAESLIL KIKSLEDVTE KERALSAKHN
SKCNELQDEI SKLKQELEHH QETEPAPNHI KGFELKQEKE LAVAASKFAE CQRTIASLGQ
RLQSLATFED FLIES
