SNX2A_ARATH
ID SNX2A_ARATH Reviewed; 587 AA.
AC Q8L5Z7; Q9FGH8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Sorting nexin 2A;
GN Name=SNX2A; OrderedLocusNames=At5g58440; ORFNames=MQJ2.4;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION.
RX PubMed=14555783; DOI=10.1104/pp.103.023846;
RA Vanoosthuyse V., Tichtinsky G., Dumas C., Gaude T., Cock J.M.;
RT "Interaction of calmodulin, a sorting nexin and kinase-associated protein
RT phosphatase with the Brassica oleracea S locus receptor kinase.";
RL Plant Physiol. 133:919-929(2003).
RN [5]
RP COMPONENT OF THE RETROMER COMPLEX.
RX PubMed=16582012; DOI=10.1105/tpc.105.035907;
RA Oliviusson P., Heinzerling O., Hillmer S., Hinz G., Tse Y.C., Jiang L.,
RA Robinson D.G.;
RT "Plant retromer, localized to the prevacuolar compartment and microvesicles
RT in Arabidopsis, may interact with vacuolar sorting receptors.";
RL Plant Cell 18:1239-1252(2006).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=19825596; DOI=10.1093/mp/ssn057;
RA Phan N.Q., Kim S.J., Bassham D.C.;
RT "Overexpression of Arabidopsis sorting nexin AtSNX2b inhibits endocytic
RT trafficking to the vacuole.";
RL Mol. Plant 1:961-976(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, 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).
RN [8]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=21156856; DOI=10.1105/tpc.110.078451;
RA Pourcher M., Santambrogio M., Thazar N., Thierry A.M., Fobis-Loisy I.,
RA Miege C., Jaillais Y., Gaude T.;
RT "Analyses of sorting nexins reveal distinct retromer-subcomplex functions
RT in development and protein sorting in Arabidopsis thaliana.";
RL Plant Cell 22:3980-3991(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19796370; DOI=10.1111/j.1365-313x.2009.04034.x;
RA Niemes S., Langhans M., Viotti C., Scheuring D., San Wan Yan M., Jiang L.,
RA Hillmer S., Robinson D.G., Pimpl P.;
RT "Retromer recycles vacuolar sorting receptors from the trans-Golgi
RT network.";
RL Plant J. 61:107-121(2010).
CC -!- FUNCTION: Plays a role in vesicular protein sorting (By similarity).
CC Acts at the crossroads between the secretory and endocytic pathways. Is
CC involved in the endosome to vacuole protein transport and, as component
CC of the membrane-associated retromer complex, is also involved in
CC endosome-to-Golgi retrograde transport (By similarity). Also involved
CC in the efficient sorting of seed storage protein globulin 12S.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Heterodimer with SNX1 or SNX2A. Component of the
CC retromer complex which consists of VPS29 (MAG1), VPS26 (VPS26A or
CC VPS26B), VPS35 (VPS35A or VPS35B or VPS35C), VPS5/17 (SNX1 or SNX2A or
CC SNX2B). {ECO:0000269|PubMed:21156856}.
CC -!- INTERACTION:
CC Q8L5Z7; Q9FG38: SNX1; NbExp=6; IntAct=EBI-5258249, EBI-1543026;
CC Q8L5Z7; B9DFS6: SNX2B; NbExp=4; IntAct=EBI-5258249, EBI-5258273;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Prevacuolar compartment membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed but at a lower level in
CC flowers, siliques, and senescing leaves. {ECO:0000269|PubMed:19825596,
CC ECO:0000269|PubMed:21156856}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced rosette size and inflorescence length as
CC well as root gravitropism defects in snx2a and snx2b double mutant.
CC Accumulation of storage protein globulin 12S in dry seeds.
CC {ECO:0000269|PubMed:21156856}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10259.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB025632; BAB10259.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED97053.1; -; Genomic_DNA.
DR EMBL; AY099775; AAM20626.1; -; mRNA.
DR EMBL; BT000285; AAN15604.1; -; mRNA.
DR RefSeq; NP_200652.2; NM_125230.6.
DR AlphaFoldDB; Q8L5Z7; -.
DR SMR; Q8L5Z7; -.
DR IntAct; Q8L5Z7; 2.
DR STRING; 3702.AT5G58440.1; -.
DR iPTMnet; Q8L5Z7; -.
DR PaxDb; Q8L5Z7; -.
DR PRIDE; Q8L5Z7; -.
DR ProteomicsDB; 232664; -.
DR EnsemblPlants; AT5G58440.1; AT5G58440.1; AT5G58440.
DR GeneID; 835957; -.
DR Gramene; AT5G58440.1; AT5G58440.1; AT5G58440.
DR KEGG; ath:AT5G58440; -.
DR Araport; AT5G58440; -.
DR TAIR; locus:2171218; AT5G58440.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_029979_0_0_1; -.
DR InParanoid; Q8L5Z7; -.
DR OMA; TWLESAI; -.
DR OrthoDB; 947320at2759; -.
DR PhylomeDB; Q8L5Z7; -.
DR PRO; PR:Q8L5Z7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L5Z7; baseline and differential.
DR Genevisible; Q8L5Z7; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0030904; C:retromer complex; TAS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0032502; P:developmental process; IGI:TAIR.
DR GO; GO:0051604; P:protein maturation; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0090351; P:seedling development; IGI:TAIR.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR044279; SNX2A/B.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR46757; PTHR46757; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endosome; Golgi apparatus; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..587
FT /note="Sorting nexin 2A"
FT /id="PRO_0000414720"
FT DOMAIN 157..277
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 331..586
FT /note="BAR"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 201
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 587 AA; 65527 MW; BA7FD93D5629AC5C CRC64;
MMGSENADGF EETNLNAQRD DMENLDLGVD GGDHPLKISD VNGDTSNSGY RSAMSTLSNV
RDPLSPPPTV MIPADSDPLL APSSYEDFRS SFSSKPISSD NSYIEPPSYA DVIFSPFDEN
SDSEINGTED NSLHSQFSDS LSRSPSSSSS DYIKITVSNP QKEQEISNSI VGGNTYITYQ
ITTRTNLPDF GGPSEFSVRR RFRDVVTLAD RLAETYRGFC IPPRPDKSVV ESQVMQKQEF
VEQRRVALEK YLRRLSAHPV IRNSDELKVF LQVQGKLPLP MSTDVASRML DGAVKLPKQL
FGEGGASAVP VTEVGQPARG GRDLLRLFKE LRQSVSNDWG GSKPPVVEED KEFLEKKEKM
HDLEQQIINA SQQAESLVKA QQDMGETMGE LGLAFIKLTK FENEEAVCNP QRTRANDMKN
LATAAVKASR FYRELNSQTV KHLDTLHEYL GMMMAVQGAF ADRSSALLTV QTLLSELPSL
QTRVEKLEAA SSKVFGGDKS RIRKIEELKE TIKVTEDAKN VAIKGYERIK ENNRSEVERL
DRERRADFMN MMKGFVVNQV GYAEKMGNVW AKVAEETSQY DREKQSS
