NET3C_ARATH
ID NET3C_ARATH Reviewed; 225 AA.
AC O82259; Q8VZA9;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein NETWORKED 3C {ECO:0000303|PubMed:22840520};
GN Name=NET3C {ECO:0000303|PubMed:22840520};
GN OrderedLocusNames=At2g47920 {ECO:0000312|Araport:AT2G47920};
GN ORFNames=F17A22.31 {ECO:0000312|EMBL:AAC63646.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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;
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=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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, SUBUNIT, INTERACTION WITH
RP PVA11/VAP27, AND MUTAGENESIS OF 210-PHE-PHE-211; PHE-211 AND LYS-223.
RX PubMed=24909329; DOI=10.1016/j.cub.2014.05.003;
RA Wang P., Hawkins T.J., Richardson C., Cummins I., Deeks M.J., Sparkes I.,
RA Hawes C., Hussey P.J.;
RT "The plant cytoskeleton, NET3C, and VAP27 mediate the link between the
RT plasma membrane and endoplasmic reticulum.";
RL Curr. Biol. 24:1397-1405(2014).
RN [6]
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. Part of a membrane-
CC cytoskeletal adapter complex that forms a bridge between the
CC endoplasmic reticulum and the plasma membrane.
CC {ECO:0000269|PubMed:24909329}.
CC -!- SUBUNIT: Dimer or oligomer. Interacts with PVA11/VAP27.
CC {ECO:0000269|PubMed:24909329}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24909329}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:24909329}. Cell
CC membrane {ECO:0000269|PubMed:24909329}. Note=Localized in immobile
CC puncta that associate with ER membranes and ER-plasma membrane contact
CC sites. This association is independent of F-actin.
CC {ECO:0000269|PubMed:24909329}.
CC -!- DOMAIN: The C-terminus is involved in oligomerization and is essential
CC for membrane association. The NAB domain, also called NAB (NET actin-
CC binding) domain, is involved in F-actin binding.
CC {ECO:0000269|PubMed:24909329}.
CC -!- SIMILARITY: Belongs to the NET family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005309; AAC63646.1; -; Genomic_DNA.
DR EMBL; AC006072; AAM15121.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10912.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62448.1; -; Genomic_DNA.
DR EMBL; AY065094; AAL38270.1; -; mRNA.
DR EMBL; AY114555; AAM47874.1; -; mRNA.
DR PIR; B84921; B84921.
DR RefSeq; NP_001324605.1; NM_001337284.1.
DR RefSeq; NP_182313.1; NM_130359.3.
DR AlphaFoldDB; O82259; -.
DR SMR; O82259; -.
DR STRING; 3702.AT2G47920.1; -.
DR PaxDb; O82259; -.
DR PRIDE; O82259; -.
DR EnsemblPlants; AT2G47920.1; AT2G47920.1; AT2G47920.
DR EnsemblPlants; AT2G47920.2; AT2G47920.2; AT2G47920.
DR GeneID; 819404; -.
DR Gramene; AT2G47920.1; AT2G47920.1; AT2G47920.
DR Gramene; AT2G47920.2; AT2G47920.2; AT2G47920.
DR KEGG; ath:AT2G47920; -.
DR Araport; AT2G47920; -.
DR TAIR; locus:2043363; AT2G47920.
DR eggNOG; ENOG502R3Z2; Eukaryota.
DR HOGENOM; CLU_072690_1_0_1; -.
DR InParanoid; O82259; -.
DR OMA; HETHVVT; -.
DR OrthoDB; 1214013at2759; -.
DR PhylomeDB; O82259; -.
DR PRO; PR:O82259; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82259; baseline and differential.
DR Genevisible; O82259; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR InterPro; IPR011684; NAB.
DR Pfam; PF07765; KIP1; 1.
DR PROSITE; PS51774; NAB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Endoplasmic reticulum; Membrane;
KW Reference proteome.
FT CHAIN 1..225
FT /note="Protein NETWORKED 3C"
FT /id="PRO_0000431859"
FT DOMAIN 8..89
FT /note="NAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01110"
FT COILED 139..197
FT /evidence="ECO:0000255"
FT MUTAGEN 210..211
FT /note="FF->AA: No effect on the interaction with
FT PVA11/VAP27."
FT /evidence="ECO:0000269|PubMed:24909329"
FT MUTAGEN 211
FT /note="F->A: Increased association with F-actin and
FT distorted ER network."
FT /evidence="ECO:0000269|PubMed:24909329"
FT MUTAGEN 223
FT /note="K->A: No effect on the association with actin and
FT endoplasmic reticulum, but reduced association with plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:24909329"
FT CONFLICT 107
FT /note="C -> S (in Ref. 3; AAL38270/AAM47874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 26489 MW; 35C2F42EA032A631 CRC64;
MVREEEKSRW WWFESHKSSK HSQWLQSTLA EIDAKTKAML KLLDGNADSF AQRAETYYKK
RPELISFVED FYRAHRSLAV NFDHLKSSDH YGSRSAKVPQ QSMESVCDSN SHFEDADSEI
EDPLQDDASA ADCKEDETWQ LEQERLKLIE ETDALRKQLL DKDEEKREVI RQLSLTLETL
KDENLSLKRR LAHHSLKQRT VLEFKPLNKF FGKLFYIMCD GNKVL
