NET1A_ARATH
ID NET1A_ARATH Reviewed; 1728 AA.
AC Q9LUI2; A0A1I9LP68;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Protein NETWORKED 1A {ECO:0000303|PubMed:22840520};
GN Name=NET1A {ECO:0000303|PubMed:22840520};
GN OrderedLocusNames=At3g22790 {ECO:0000312|Araport:AT3G22790};
GN ORFNames=MWI23.16 {ECO:0000312|EMBL:BAB01254.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP DOMAIN, GENE FAMILY, NOMENCLATURE, AND INTERACTION WITH F-ACTIN.
RX PubMed=22840520; DOI=10.1016/j.cub.2012.06.041;
RA Deeks M.J., Calcutt J.R., Ingle E.K., Hawkins T.J., Chapman S.,
RA Richardson A.C., Mentlak D.A., Dixon M.R., Cartwright F., Smertenko A.P.,
RA Oparka K., Hussey P.J.;
RT "A superfamily of actin-binding proteins at the actin-membrane nexus of
RT higher plants.";
RL Curr. Biol. 22:1595-1600(2012).
RN [4]
RP GENE FAMILY.
RX PubMed=24926301; DOI=10.3389/fpls.2014.00254;
RA Hawkins T.J., Deeks M.J., Wang P., Hussey P.J.;
RT "The evolution of the actin binding NET superfamily.";
RL Front. Plant Sci. 5:254-254(2014).
CC -!- FUNCTION: Plant-specific actin binding protein. Associates with F-actin
CC at the plasma membrane and plasmodesmata. May be part of a membrane-
CC cytoskeletal adapter complex. {ECO:0000269|PubMed:22840520}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:22840520}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22840520}. Cell membrane
CC {ECO:0000269|PubMed:22840520}. Cell junction, plasmodesma
CC {ECO:0000269|PubMed:22840520}. Note=Localizes to the cell cortex and
CC shows polar enrichment at the apical and basal cell boundaries.
CC {ECO:0000269|PubMed:22840520}.
CC -!- TISSUE SPECIFICITY: Expressed in root meristems and at very low levels
CC throughout mature vasculature. {ECO:0000269|PubMed:22840520}.
CC -!- DOMAIN: The NAB domain, also called NAB (NET actin-binding) domain, is
CC sufficient for F-actin binding. {ECO:0000269|PubMed:22840520}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC NET1B. Net1a and net1b double mutant shows a significant acceleration
CC in root-cell expansion. {ECO:0000269|PubMed:22840520}.
CC -!- SIMILARITY: Belongs to the NET family. {ECO:0000305}.
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DR EMBL; AB022223; BAB01254.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76677.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64376.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64377.1; -; Genomic_DNA.
DR RefSeq; NP_001319620.1; NM_001338597.1.
DR RefSeq; NP_001326409.1; NM_001338598.1.
DR RefSeq; NP_188918.2; NM_113178.3.
DR AlphaFoldDB; Q9LUI2; -.
DR SMR; Q9LUI2; -.
DR STRING; 3702.AT3G22790.1; -.
DR iPTMnet; Q9LUI2; -.
DR PaxDb; Q9LUI2; -.
DR PRIDE; Q9LUI2; -.
DR ProteomicsDB; 250556; -.
DR EnsemblPlants; AT3G22790.1; AT3G22790.1; AT3G22790.
DR EnsemblPlants; AT3G22790.2; AT3G22790.2; AT3G22790.
DR EnsemblPlants; AT3G22790.3; AT3G22790.3; AT3G22790.
DR GeneID; 821850; -.
DR Gramene; AT3G22790.1; AT3G22790.1; AT3G22790.
DR Gramene; AT3G22790.2; AT3G22790.2; AT3G22790.
DR Gramene; AT3G22790.3; AT3G22790.3; AT3G22790.
DR KEGG; ath:AT3G22790; -.
DR Araport; AT3G22790; -.
DR TAIR; locus:2094379; AT3G22790.
DR eggNOG; ENOG502QQ6M; Eukaryota.
DR HOGENOM; CLU_001229_1_1_1; -.
DR InParanoid; Q9LUI2; -.
DR OMA; NIRQKRV; -.
DR OrthoDB; 60151at2759; -.
DR PhylomeDB; Q9LUI2; -.
DR PRO; PR:Q9LUI2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUI2; baseline and differential.
DR Genevisible; Q9LUI2; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR InterPro; IPR011684; NAB.
DR Pfam; PF07765; KIP1; 1.
DR PROSITE; PS51774; NAB; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Reference proteome.
FT CHAIN 1..1728
FT /note="Protein NETWORKED 1A"
FT /id="PRO_0000431849"
FT DOMAIN 13..92
FT /note="NAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01110"
FT REGION 1419..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 155..446
FT /evidence="ECO:0000255"
FT COILED 476..827
FT /evidence="ECO:0000255"
FT COILED 857..885
FT /evidence="ECO:0000255"
FT COILED 954..1016
FT /evidence="ECO:0000255"
FT COILED 1090..1323
FT /evidence="ECO:0000255"
FT COILED 1403..1431
FT /evidence="ECO:0000255"
FT COILED 1576..1684
FT /evidence="ECO:0000255"
SQ SEQUENCE 1728 AA; 198852 MW; 0F393BC8C839B6D0 CRC64;
MATVLHSESR RLYSWWWDSH IPKNSKWIQQ NLSDMDSKVK AMIKLIEEDA DSFARRAEMY
YKKRPELMKL VEEFYRAYRA LAERYDHATV ELCHAHKTMA EAFPNQVPFD MIEDSASSSC
SEPRTPEKMP PGIQPFYDSD SATSKRGLSQ LTEYLGNSET EVESLKRTLV ELGAEKEALN
LQYQLSLNKF SRLEKDLEVA QKDVSGLDER ASKAEIETKI LAEALAKLEA ERDAALLRYN
ESMQKITELE ESFSHAQEDV KGLTNRATKA ETEVENLKQA HSRLHSEKEA GLAEYNRCLE
MISNLEKKVR DAEENAQNFS NQSAKAEDEI KALRHELVKV NEVKDGLRLR YQQCLETISK
LEREVSHAQD NAKRLSSEVL AGAAKLKTVE DQCTLLESSN ETLKLEADGL THKLAAKDQE
IFQKQNELEK FQSLIEDEHS RYLEIEVSLK TLQSLYSQSQ EEQKVITSEL QSRIGMLRDL
ETRNLKLEGD ISSVKEENQN LSELNDSSMI FLETQKCEIS SLKEIKEKLE EEVARHINQS
SAFQEEIRRL KDEIDSLNKR YQAIMEQVNL AGLDPKSLAC SVRKLQDENS KLTELCNHQS
DDKDALTEKL RELDNILRKN VCLEKLLLES NTKLDGSREK TKDLQERCES LRGEKYEFIA
ERANLLSQLQ IMTENMQKLL EKNSLLETSL SGANIELQCV KEKSKCFEEF FQLLKNDKAE
LIKERESLIS QLNAVKEKLG VLEKKFTELE GKYADLQREK QFKNLQVEEL RVSLATEKQE
RASYERSTDT RLADLQNNVS FLREECRSRK KEFEEELDRA VNAQVEIFIL QKFIEDLEQK
NFSLLIECQK YAEASSFSEK LIAELESENL EQQMEAEFLV HEIDNFRGAI CQVFKALQVE
ADCKTADQKI AKERIPVSRV LGEINELKCS LSSAEYETQR LVIENSVLLS LLGQFQSDGM
KLESEKRDVE KDLETIVHHY GMLKKDRLEL LEMNRQLKSE LIDREQRELE LKAELQTEHL
KFENLHESYM ALHQDYSDAL GKNKSLHLKF SELKGEICIL EEENGAILEE AIALNNVSVV
YQSLGSEKAE QAEAFAKNLN SLQNINSGLK QKVETLEEIL KGKEVDSQEL NSKLEKLQES
LEEANELNDL LEHQILVKEE TLRQKAIELL EAEEMLKATH NANAELCEAV EELRKDCKES
RKLKGNLEKR NSELCDLAGR QDEEIKILSN LKENLESEVK LLHKEIQEHR VREEFLSSEL
QEKSNEFGLW DAEATSFYFD LQISAVREVL LENKVQELTG VCENLKDEAV TKTTEINQIK
ETVGFLEFEV SELKTQLSAY DPVVASLAED VRSLEQNALS LMKLPVPAGR RREGVQNDEH
QEAAVSQEPV GHCSTNLDNG IVLLQDMKTR IKTIKQAVAE EKKRRGKLRR RSSSHRSKDR
KLFEEIELED QFSGEIRQPR SPAMTESKNG SLMKDIPLDQ VADTTSYGRS RRTSRGSSDQ
MLELWEEAAE PESSIKFLIN NKNSKKPLIP RLHRRSRNPS VESQSEKMVG VVDKLELSRS
TEDNAKILER LLSDSRRLAS LRISLRDLKS KLEINEKPGK FTNPDFARVR KQMKEMEEAI
FQLANTNEIL SNEIEETGDV RDIYRKVVME KSRIGSEKIE QMQQEMQNIE RTVLKLEEGA
TKSKGRRKFS ESRTVILLRD IIHKGGKRTA RKKKNRFCGC MRSSGNEE
