SNX1_BOVIN
ID SNX1_BOVIN Reviewed; 522 AA.
AC Q05B62;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Sorting nexin-1;
GN Name=SNX1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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. Involved in retrograde endosome-to-TGN
CC transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1). Plays
CC a role in targeting ligand-activated EGFR to the lysosomes for
CC degradation after endocytosis from the cell surface and release from
CC the Golgi. Involvement in retromer-independent endocytic trafficking of
CC P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R.
CC Promotes KALRN- and RHOG-dependent but retromer-independent membrane
CC remodeling such as lamellipodium formation; the function is dependent
CC on GEF activity of KALRN. Required for endocytosis of DRD5 upon agonist
CC stimulation but not for basal receptor trafficking (By similarity).
CC {ECO:0000250|UniProtKB:Q13596}.
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 DRD5, DENND5A, KALRN, RHOG (GDP-bound form). The interaction with SNX2
CC is reported controversially. Interacts with DNAJC13; prevented by
CC presence of HGS. Interacts with HGS (By similarity).
CC {ECO:0000250|UniProtKB:Q13596, ECO:0000250|UniProtKB:Q99N27}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q13596};
CC Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-
CC Golgi network membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cell projection,
CC lamellipodium {ECO:0000250|UniProtKB:Q13596}. Note=Enriched on tubular
CC elements of the early endosome membrane. Binds preferentially to highly
CC curved membranes enriched in phosphatidylinositol 3-phosphate
CC (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC Colocalized with SORT1 to tubular endosomal membrane structures called
CC endosome-to-TGN transport carriers (ETCs) which are budding from early
CC endosome vacuoles just before maturing into late endosome vacuoles.
CC Colocalized with F-actin at the leading edge of lamellipodia in a
CC KALRN-dependent manner. {ECO:0000250|UniProtKB:Q13596}.
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:Q13596}.
CC -!- MISCELLANEOUS: Binds phosphatidylinositol 3-phosphate (PtdIns-(3)P) and
CC phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2) in liposome-
CC based assays. Can bind PtdIns(3,4,5)P3 in protein:lipid overlay assays,
CC but not in liposome-based assays (By similarity).
CC {ECO:0000250|UniProtKB:Q13596}.
CC -!- SIMILARITY: Belongs to the sorting nexin 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; BC122759; AAI22760.1; -; mRNA.
DR RefSeq; NP_001039572.2; NM_001046107.3.
DR AlphaFoldDB; Q05B62; -.
DR BMRB; Q05B62; -.
DR SMR; Q05B62; -.
DR STRING; 9913.ENSBTAP00000002609; -.
DR PaxDb; Q05B62; -.
DR PRIDE; Q05B62; -.
DR GeneID; 512029; -.
DR KEGG; bta:512029; -.
DR CTD; 6642; -.
DR eggNOG; KOG2273; Eukaryota.
DR InParanoid; Q05B62; -.
DR OrthoDB; 947320at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0072673; P:lamellipodium morphogenesis; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR CDD; cd07281; PX_SNX1; 1.
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; IPR034901; PX_SNX1.
DR InterPro; IPR028660; SNX1.
DR InterPro; IPR005329; Sorting_nexin_N.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR10555:SF129; PTHR10555:SF129; 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; SSF103657; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell projection; Endosome; Golgi apparatus; Lipid-binding;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..522
FT /note="Sorting nexin-1"
FT /id="PRO_0000290185"
FT DOMAIN 143..272
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 302..522
FT /note="BAR"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..298
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000250|UniProtKB:Q13596"
FT COMPBIAS 95..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186
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 188
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 214
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 238
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 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13596"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13596"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV80"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13596"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV80"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13596"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13596"
FT MOD_RES 237
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13596"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13596"
SQ SEQUENCE 522 AA; 59056 MW; AE236FF0588063AA CRC64;
MASGGGGCSA SERLPPPFPG LEPESEGAVG GSEPEAGDSD TEGEDIFTGA AAVSKPQSPK
RIASLLPINS GSKENGIHEE QDQEPQDLFA DATVELSLDS TQNNQKKVPA KTLISLPPQE
ATNSSKPQPS YEELEEEEQE DQFDLTVGIT DPEKIGDGMN AYVAYKVTTQ TSLPMFRSKH
FAVKRRFSDF LGLYEKLSEK HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA
ALERYLQRIV NHPTMLQDPD VREFLEKEEL PRAVGTQTLS GAGLLKMFNK ATDAVSKMTI
NMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTAQFAKS LAMLGSSEDN
TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI RLLAIVRAAF DQRMKTWQRW
QDAQTTLQKK REAEARLLWA NKPDKLQQAK DEIVEWESRV TQYERDFERI STVVRKEVIR
FEKEKSRDFR NHVIQYLETL LHSQQQLAKY WEAFLPEAKA IS
