SNX1_ARATH
ID SNX1_ARATH Reviewed; 402 AA.
AC Q9FG38; Q8RXM2;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sorting nexin 1;
DE Short=AtSNX1;
DE AltName: Full=Vacuolar protein sorting-associated protein 5 homolog;
GN Name=SNX1; Synonyms=VPS5; OrderedLocusNames=At5g06140;
GN ORFNames=K16F4.11, MBL20;
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 (MAY-2000) 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;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-402.
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 [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=16936718; DOI=10.1038/nature05046;
RA Jaillais Y., Fobis-Loisy I., Miege C., Rollin C., Gaude T.;
RT "AtSNX1 defines an endosome for auxin-carrier trafficking in Arabidopsis.";
RL Nature 443:106-109(2006).
RN [7]
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17999644; DOI=10.1111/j.1365-313x.2007.03338.x;
RA Jaillais Y., Fobis-Loisy I., Miege C., Gaude T.;
RT "Evidence for a sorting endosome in Arabidopsis root cells.";
RL Plant J. 53:237-247(2008).
RN [9]
RP FUNCTION.
RX PubMed=19004783; DOI=10.1073/pnas.0808073105;
RA Kleine-Vehn J., Leitner J., Zwiewka M., Sauer M., Abas L., Luschnig C.,
RA Friml J.;
RT "Differential degradation of PIN2 auxin efflux carrier by retromer-
RT dependent vacuolar targeting.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17812-17817(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, 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 [11]
RP FUNCTION, AND INTERACTION WITH BLOS1 AND BLOS2.
RX PubMed=20971704; DOI=10.1242/jcs.069732;
RA Cui Y., Li X., Chen Q., He X., Yang Q., Zhang A., Yu X., Chen H., Liu N.,
RA Xie Q., Yang W., Zuo J., Palme K., Li W.;
RT "BLOS1, a putative BLOC-1 subunit, interacts with SNX1 and modulates root
RT growth in Arabidopsis.";
RL J. Cell Sci. 123:3727-3733(2010).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND 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 [13]
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. Acts at the
CC crossroads between the secretory and endocytic pathways. Is involved in
CC the endosome to vacuole protein transport via its interaction with the
CC BLOS1/2 proteins and, as component of the membrane-associated retromer
CC complex, is also involved in endosome-to-Golgi retrograde transport.
CC Required for the auxin-carrier protein PIN2 sorting to the lytic
CC vacuolar pathway and the trafficking of several plasma membrane
CC proteins. Also involved in the efficient sorting of seed storage
CC protein globulin 12S. {ECO:0000269|PubMed:16936718,
CC ECO:0000269|PubMed:17999644, ECO:0000269|PubMed:19004783,
CC ECO:0000269|PubMed:20971704, ECO:0000269|PubMed:21156856}.
CC -!- SUBUNIT: Homodimer. Heterodimer with SNX2A or SNX2B. 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). Interacts with BLOS1 and BLOS2. {ECO:0000269|PubMed:20971704,
CC ECO:0000269|PubMed:21156856}.
CC -!- INTERACTION:
CC Q9FG38; O22929: BLOS1; NbExp=5; IntAct=EBI-1543026, EBI-4406998;
CC Q9FG38; Q8L5Z7: SNX2A; NbExp=6; IntAct=EBI-1543026, EBI-5258249;
CC Q9FG38; B9DFS6: SNX2B; NbExp=7; IntAct=EBI-1543026, EBI-5258273;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Prevacuolar compartment membrane; Peripheral
CC membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi
CC network membrane; Peripheral membrane protein; Cytoplasmic side.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:21156856}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization.
CC -!- DISRUPTION PHENOTYPE: Shorter primary roots, fewer secondary roots and
CC an altered root gravitropic response. Accumulation of storage protein
CC globulin 12S in dry seeds. {ECO:0000269|PubMed:16936718}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AP002030; BAB10207.1; -; Genomic_DNA.
DR EMBL; AP002544; BAB10207.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED90975.1; -; Genomic_DNA.
DR EMBL; BT029777; ABM06047.1; -; mRNA.
DR EMBL; AY080809; AAL87289.1; -; mRNA.
DR RefSeq; NP_196232.1; NM_120696.4.
DR AlphaFoldDB; Q9FG38; -.
DR SMR; Q9FG38; -.
DR BioGRID; 15780; 4.
DR IntAct; Q9FG38; 6.
DR STRING; 3702.AT5G06140.1; -.
DR iPTMnet; Q9FG38; -.
DR PaxDb; Q9FG38; -.
DR PRIDE; Q9FG38; -.
DR ProteomicsDB; 234477; -.
DR EnsemblPlants; AT5G06140.1; AT5G06140.1; AT5G06140.
DR GeneID; 830501; -.
DR Gramene; AT5G06140.1; AT5G06140.1; AT5G06140.
DR KEGG; ath:AT5G06140; -.
DR Araport; AT5G06140; -.
DR TAIR; locus:2152850; AT5G06140.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_022783_1_0_1; -.
DR InParanoid; Q9FG38; -.
DR OMA; AYKQPEF; -.
DR OrthoDB; 947320at2759; -.
DR PhylomeDB; Q9FG38; -.
DR PRO; PR:Q9FG38; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG38; baseline and differential.
DR Genevisible; Q9FG38; AT.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005771; C:multivesicular body; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0030904; C:retromer complex; IDA:TAIR.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0010252; P:auxin homeostasis; IDA:TAIR.
DR GO; GO:0008333; P:endosome to lysosome transport; TAS:TAIR.
DR GO; GO:0006896; P:Golgi to vacuole transport; IDA:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP: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; IPR028648; Vps5-like.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR10555:SF170; PTHR10555:SF170; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; SSF103657; 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..402
FT /note="Sorting nexin 1"
FT /id="PRO_0000414719"
FT DOMAIN 24..143
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 160..402
FT /note="BAR"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
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 93
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 109
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 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 402 AA; 46523 MW; 42EC6B67942F7D20 CRC64;
MESTEQPRNI SGSMQSPRSP SSHPYLSVSV TDPVKLGNGV QAYISYRVIT KTNLPEYQGP
EKIVIRRYSD FVWLRDRLFE KYKGIFIPPL PEKSAVEKFR FSAEFIEMRR AALDIFVNRI
ALHPELQQSE DLRTFLQADE ETMDRFRFQE TSIFKKPADL MQMFRDVQSK VSDAVLGKEK
PVEETTADYE KLKHYIFELE NHLTEAQKHA YRLVKRHREL GQSLLDFGKA VKLLGACEGE
PTGKAFSDLG TKSELLSIKL QKEAQQVLMN FEEPLKDYVR YVQSIKATIA ERGTAFKQHC
ELSETTKLKE INLDKLMLTR SDKVGEAEIE YREIKAESEE ATRRFERIVK RMEDEIVRFQ
EQKTEEMGVA FHQFAKGQAR LANSVADAWR SLLPKLEASY SV
