4ON1_ARATH
ID 4ON1_ARATH Reviewed; 247 AA.
AC Q1PE49; A0MF98; Q84UC5; Q9SZH6;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein At-4/1;
DE AltName: Full=Tomato spotted wilt virus movement protein-interacting protein 4/1;
DE Short=At-4/1;
GN OrderedLocusNames=At4g26020; ORFNames=F20B18.130;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH VIRAL TOMATO SPOTTED WILT VIRUS NSM PROTEIN, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16903353; DOI=10.1094/mpmi-19-0874;
RA Paape M., Solovyev A.G., Erokhina T.N., Minina E.A., Schepetilnikov M.V.,
RA Lesemann D.-E., Schiemann J., Morozov S.Y., Kellmann J.-W.;
RT "At-4/1, an interactor of the Tomato spotted wilt virus movement protein,
RT belongs to a new family of plant proteins capable of directed intra- and
RT intercellular trafficking.";
RL Mol. Plant Microbe Interact. 19:874-883(2006).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-247.
RX DOI=10.1016/S0981-9428(01)01331-6;
RA von Bargen S., Salchert K., Paape M., Piechulla B., Kellmann J.W.;
RT "Interactions between the tomato spotted wilt virus movement protein and
RT plant proteins showing homologies to myosin, kinesin and DnaJ-like
RT chaperones.";
RL Plant Physiol. Biochem. 39:1083-1093(2001).
CC -!- FUNCTION: Involved in intra- and inter-cellular trafficking through
CC plasmodesmata (PD). {ECO:0000269|PubMed:16903353}.
CC -!- SUBUNIT: Interacts with viral tomato spotted wilt virus (TSWV) movement
CC protein NSM, which is involved in cell-to cell spread of viral genome
CC and enlargement of the host plasmodesmata size exclusion limit (SEL).
CC {ECO:0000269|PubMed:16903353}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16903353}. Cell junction, plasmodesma
CC {ECO:0000269|PubMed:16903353}. Note=Accumulates intracellularly in a
CC polarized fashion, into punctate spots at the cell periphery. Located
CC at both orifices of the plasmodesmatal pore of adjacent cells. Can move
CC through plasmodesmata.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q1PE49-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves (at protein level).
CC {ECO:0000269|PubMed:16903353}.
CC -!- DOMAIN: The C-terminal part of the protein in required for plasmodesma
CC localization.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28649.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB39667.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79457.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049483; CAB39667.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161564; CAB79457.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85145.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67465.1; -; Genomic_DNA.
DR EMBL; DQ446869; ABE66090.1; -; mRNA.
DR EMBL; DQ653224; ABK28649.1; ALT_SEQ; mRNA.
DR EMBL; AY212284; AAO32317.1; -; mRNA.
DR PIR; T04257; T04257.
DR RefSeq; NP_001329294.1; NM_001341773.1. [Q1PE49-1]
DR RefSeq; NP_194332.2; NM_118735.3. [Q1PE49-1]
DR AlphaFoldDB; Q1PE49; -.
DR SMR; Q1PE49; -.
DR STRING; 3702.AT4G26020.2; -.
DR PaxDb; Q1PE49; -.
DR PRIDE; Q1PE49; -.
DR EnsemblPlants; AT4G26020.1; AT4G26020.1; AT4G26020. [Q1PE49-1]
DR EnsemblPlants; AT4G26020.3; AT4G26020.3; AT4G26020. [Q1PE49-1]
DR GeneID; 828708; -.
DR Gramene; AT4G26020.1; AT4G26020.1; AT4G26020. [Q1PE49-1]
DR Gramene; AT4G26020.3; AT4G26020.3; AT4G26020. [Q1PE49-1]
DR KEGG; ath:AT4G26020; -.
DR Araport; AT4G26020; -.
DR eggNOG; ENOG502RBMV; Eukaryota.
DR HOGENOM; CLU_085523_0_0_1; -.
DR InParanoid; Q1PE49; -.
DR OMA; AAHKSHM; -.
DR PhylomeDB; Q1PE49; -.
DR PRO; PR:Q1PE49; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q1PE49; baseline and differential.
DR Genevisible; Q1PE49; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; IDA:UniProtKB.
DR GO; GO:0010496; P:intercellular transport; IDA:UniProtKB.
DR GO; GO:0046907; P:intracellular transport; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Coiled coil; Endoplasmic reticulum;
KW Host-virus interaction; Reference proteome; Transport.
FT CHAIN 1..247
FT /note="Protein At-4/1"
FT /id="PRO_0000408301"
FT COILED 39..126
FT /evidence="ECO:0000255"
FT COILED 182..247
FT /evidence="ECO:0000255"
FT CONFLICT 189
FT /note="K -> R (in Ref. 5; AAO32317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 29136 MW; 7F0544E6710DEAF5 CRC64;
MAATSDEQMN LLLSSFDQIY EDFKIGLNEI NVYRSKSNVE SSRREVLEIS NKNLKEENER
LKKLYTESLN NFADQLEHRT KCHSLKEELK RVNDENKSKE HEHRNALESL RQKHVTKVEE
LEYKIRSLLV EKATNDMVID RLRQDLTANK SHIQAMSKKL DRVVTEVECK YELEIQDLKD
CLLMEQAEKN DISNKLQSLQ KELLISRTSI AEKQRDTTSN RQVETLKQKL MKLRKENEIL
KRKLSSS
