ID SNX2_MACFA Reviewed; 523 AA.
AC P0C220;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Sorting nexin-2;
GN Name=SNX2; ORFNames=QorA-14039;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Occipital cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in several stages of intracellular trafficking.
CC Interacts with membranes containing phosphatidylinositol 3-phosphate
CC (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC Acts in part as component of the retromer membrane-deforming SNX-BAR
CC subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo
CC proteins from endosomes to the trans-Golgi network (TGN) and is
CC involved in endosome-to-plasma membrane transport for cargo protein
CC recycling. The SNX-BAR subcomplex functions to deform the donor
CC membrane into a tubular profile called endosome-to-TGN transport
CC carrier (ETC). Can sense membrane curvature and has in vitro vesicle-
CC to-membrane remodeling activity. Required for retrograde endosome-to-
CC TGN transport of TGN38. Promotes KALRN- and RHOG-dependent but
CC retromer-independent membrane remodeling such as lamellipodium
CC formation; the function is dependent on GEF activity of KALRN (By
CC similarity). {ECO:0000250|UniProtKB:O60749}.
CC -!- SUBUNIT: Predominantly forms heterodimers with BAR domain-containing
CC sorting nexins SNX5, SNX6 and SNX32; can self-associate to form
CC homodimers. The heterodimers are proposed to self-assemble into helical
CC arrays on the membrane to stabilize and expand local membrane curvature
CC underlying endosomal tubule formation. Thought to be a component of the
CC originally described retromer complex (also called SNX-BAR retromer)
CC which is a pentamer containing the heterotrimeric retromer cargo-
CC selective complex (CSC), also described as vacuolar protein sorting
CC subcomplex (VPS), and a heterodimeric membrane-deforming subcomplex
CC formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR
CC subcomplex); the respective CSC and SNX-BAR subcomplexes associate with
CC low affinity. Interacts with SNX5, SNX6, SNX32, VPS26A, VPS29, VPS35,
CC FNBP1, KALRN, RHOG (GDP-bound form) (By similarity).
CC {ECO:0000250|UniProtKB:O60749}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side {ECO:0000250|UniProtKB:O60749}. Cell
CC projection, lamellipodium. Note=Colocalized with SORT1 to tubular
CC endosomal membrane structures called endosome-to-TGN transport carriers
CC (ETCs) which are budding from early endosome vacuoles just before
CC maturing into late endosome vacuoles. Colocalized with F-actin at the
CC leading edge of lamellipodia in cells in a KALRN-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:O60749}.
CC -!- DOMAIN: The BAR domain is able to sense membrane curvature upon
CC dimerization. Membrane remodeling seems to implicate insertion of a N-
CC terminal amphipathic helix (AH) in the membrane (By similarity).
CC {ECO:0000250|UniProtKB:O60749}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AB171301; BAE88364.1; -; mRNA.
DR RefSeq; NP_001271755.1; NM_001284826.1.
DR AlphaFoldDB; P0C220; -.
DR SMR; P0C220; -.
DR STRING; 9541.ENSMFAP00000013948; -.
DR Ensembl; ENSMFAT00000064410.2; ENSMFAP00000013948.2; ENSMFAG00000029999.2.
DR eggNOG; KOG2273; Eukaryota.
DR GeneTree; ENSGT00940000155798; -.
DR OrthoDB; 1891044at2759; -.
DR Proteomes; UP000233100; Chromosome 6.
DR Bgee; ENSMFAG00000029999; Expressed in spleen and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030904; C:retromer complex; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072673; P:lamellipodium morphogenesis; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR CDD; cd07282; PX_SNX2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR037918; SNX2_PX.
DR InterPro; IPR005329; Sorting_nexin_N.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR10555; SORTING NEXIN; 1.
DR PANTHER; PTHR10555:SF31; SORTING NEXIN-2; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF03700; Sorting_nexin; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell projection; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..523
FT /note="Sorting nexin-2"
FT /id="PRO_0000236194"
FT DOMAIN 140..269
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 299..523
FT /note="BAR"
FT /evidence="ECO:0000250|UniProtKB:Q13596"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..523
FT /note="Interaction with RhoG"
FT /evidence="ECO:0000250|UniProtKB:O60749"
FT REGION 278..295
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000250|UniProtKB:O60749"
FT COMPBIAS 27..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183
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|UniProtKB:Q96L94"
FT BINDING 185
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|UniProtKB:Q96L94"
FT BINDING 211
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|UniProtKB:Q96L94"
FT BINDING 235
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|UniProtKB:Q96L94"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CWK8"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60749"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60749"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60749"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60749"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60749"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60749"
FT MOD_RES 473
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60749"
SQ SEQUENCE 523 AA; 58901 MW; F68DBEC6F9600B90 CRC64;
MAAEREPPPL GDGKPTDFED LEDGEDLFTS TVSTLESSPS SPEPASLPAE DISANSNGPK
PTEVGLDDDR EDLFAEATEE VSLDSPEREP ILSSEPSPAV TPVTPTTLIA PRIESKSMSA
PVIFDRSREE IEEEANGDIF DIEIGVSDPE KVGDGMNAYM AYRVTTKTSL SMFSKSEFSV
KRRFSDFLGL HSKLASKYLH VGYIVPPAPE KSIVGMTKVK VGKEDSSSTE FVEKRRAALE
RYLQRTVKHP TLLQDPDLRQ FLESSELPRA VNTQALSGAG ILRMVNKAAD AVNKMTIKMN
ESDAWFEEKQ QQFENLDQQL RKLHASVEAL VCHRKELSAN TAAFAKSAAM LGNSEDHTAL
SRALSQLAEV EEKIDQLHQE QAFADFYMFS ELLSDYIRLI AAVKGVFDHR MKCWQKWEDA
QITLLKKREA EAKMMVANKP DKIQQAKNEI REEIEEWEAK VQQGERDFEQ ISKTIRKEVG
RFEKERVKDF KTVIIKYLES LVQTQQQLIK YWEAFLPEAK AIA
//
