SNX2B_ARATH
ID SNX2B_ARATH Reviewed; 572 AA.
AC B9DFS6; Q0WLC3; Q570X1; Q9LYQ3;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Sorting nexin 2B;
GN Name=SNX2B; OrderedLocusNames=At5g07120; ORFNames=T28J14_60;
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;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-341, AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 533-572.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHATIDYLINOSITOL
RP 3-PHOSPHATE BINDING, AND MUTAGENESIS OF 233-ARG-ARG-234.
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 [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).
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 and, as component of the
CC membrane-associated retromer complex, is also involved in endosome-to-
CC Golgi retrograde transport. {ECO:0000269|PubMed:19825596}.
CC -!- SUBUNIT: Homodimer. Heterodimer with SNX1 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). {ECO:0000269|PubMed:21156856}.
CC -!- INTERACTION:
CC B9DFS6; Q9FG38: SNX1; NbExp=7; IntAct=EBI-5258273, EBI-1543026;
CC B9DFS6; Q8L5Z7: SNX2A; NbExp=4; IntAct=EBI-5258273, EBI-5258249;
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:19825596, ECO:0000269|PubMed:21156856}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization.
CC -!- DISRUPTION PHENOTYPE: Reduced rosette size and inflorescence length as
CC well as root gravitropism defects in snx2a and snx2b double mutant.
CC {ECO:0000269|PubMed:21156856}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87268.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL163652; CAB87268.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91112.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70224.1; -; Genomic_DNA.
DR EMBL; AK316886; BAH19593.1; -; mRNA.
DR EMBL; AK220586; BAD94882.1; -; mRNA.
DR EMBL; AK230282; BAF02084.1; -; mRNA.
DR PIR; T48483; T48483.
DR RefSeq; NP_001331853.1; NM_001342920.1.
DR RefSeq; NP_196329.2; NM_120794.4.
DR AlphaFoldDB; B9DFS6; -.
DR SMR; B9DFS6; -.
DR IntAct; B9DFS6; 2.
DR STRING; 3702.AT5G07120.1; -.
DR iPTMnet; B9DFS6; -.
DR PaxDb; B9DFS6; -.
DR PRIDE; B9DFS6; -.
DR ProteomicsDB; 232608; -.
DR EnsemblPlants; AT5G07120.1; AT5G07120.1; AT5G07120.
DR EnsemblPlants; AT5G07120.2; AT5G07120.2; AT5G07120.
DR GeneID; 830603; -.
DR Gramene; AT5G07120.1; AT5G07120.1; AT5G07120.
DR Gramene; AT5G07120.2; AT5G07120.2; AT5G07120.
DR KEGG; ath:AT5G07120; -.
DR Araport; AT5G07120; -.
DR TAIR; locus:2182880; AT5G07120.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_029979_0_0_1; -.
DR InParanoid; B9DFS6; -.
DR OMA; KERMHDL; -.
DR OrthoDB; 947320at2759; -.
DR PhylomeDB; B9DFS6; -.
DR PRO; PR:B9DFS6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B9DFS6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0032585; C:multivesicular body membrane; IDA:TAIR.
DR GO; GO:0030904; C:retromer complex; TAS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IDA:TAIR.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR GO; GO:0032502; P:developmental process; IGI:TAIR.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:UniProtKB.
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 GO; GO:0016192; P:vesicle-mediated transport; 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; 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..572
FT /note="Sorting nexin 2B"
FT /id="PRO_0000414721"
FT DOMAIN 147..266
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 318..572
FT /note="BAR"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190
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 216
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 233
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8L5Z7"
FT MUTAGEN 233..234
FT /note="RR->LG: Abolishes phosphatidylinositol 3-phosphate
FT binding."
FT /evidence="ECO:0000269|PubMed:19825596"
FT CONFLICT 235
FT /note="V -> F (in Ref. 4; BAD94882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 64282 MW; C04F54BA66125DFE CRC64;
MMGSENDEES HLHSSKEEME KLFLREDGDP LTKSNVNGDK SNSNYRSAMS TLFDSRHPSI
VVTPADSDPL FAPPSYYSES RSPRSKPNGG DRVSSYLEPP SYADVIFSPF DDISEINGSE
DGHSQSSDSL SRSPSSLSSD YIKITVSNPQ KEQEATNSMI PGGSTYITYQ ITTRTNLSDY
GGSEFSVRRR FRDIVTLADR LAESYRGFCI PPRPDKSIVE SQVMQKQEFV EQRRVALEKY
LRRLVAHPVI RNSDELKVFL QAQGKLPLAT STDVASRMLD GAVKLPKQLF GEGGGASSVE
VVQPGRGGRD FLRMFKELRQ SVSNDWGGSK PPVVEEDKEF LEKKEKMYDL EQQIINASQQ
AESLVKAQQD MGETMGELGL AFIKLTKFEN EEAVFNSQRA RANDMKNLAT SAVKASRFYR
ELNSQTVKHL DTLHDYLGLM MAVQGAFADR SSALLTVQTL LSELSSLEAR AEKLEVASSK
VFGGDKSRIK KIEELKETIK VTEDSKNVAI REYEQIKENN WSEVERLDRE RRADFLNMMK
GFVANQVGYA EKIANVWTKV AEETRQYDRE SS
