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SNX1_PONAB
ID   SNX1_PONAB              Reviewed;         522 AA.
AC   Q5RFP8; Q5RFP9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Sorting nexin-1;
GN   Name=SNX1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
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DR   EMBL; CR857103; CAH89408.1; -; mRNA.
DR   EMBL; CR857104; CAH89409.1; -; mRNA.
DR   RefSeq; NP_001127143.1; NM_001133671.1.
DR   AlphaFoldDB; Q5RFP8; -.
DR   BMRB; Q5RFP8; -.
DR   SMR; Q5RFP8; -.
DR   STRING; 9601.ENSPPYP00000007424; -.
DR   GeneID; 100174193; -.
DR   KEGG; pon:100174193; -.
DR   CTD; 6642; -.
DR   eggNOG; KOG2273; Eukaryota.
DR   HOGENOM; CLU_022783_2_0_1; -.
DR   InParanoid; Q5RFP8; -.
DR   TreeFam; TF313698; -.
DR   Proteomes; UP000001595; 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_0000236193"
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        57..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   CONFLICT        246
FT                   /note="I -> L (in Ref. 1; CAH89408)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        285
FT                   /note="P -> L (in Ref. 1; CAH89408)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   522 AA;  59082 MW;  F5C6E9EEA649B799 CRC64;
     MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA AVVSKHQSPK
     RATSLLPINN GSKENGIHEE QDQEPQDLFA DATVELSLDS TQNNQKKMPA KTLISLPPQE
     ATNSSKPQPT YEELEEEEQE DQFDLTVGIT DPEKIGDGMN AYVAYKVTTQ TSLPLFRSKQ
     FAVKRRFSDF LGLYEKLSEK HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA
     ALERYIQRIV NHPTMLQDPD VREFLEKEEL PRAVGTQTLS GAGLPKMFNK ATDAVSKMTI
     KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTAQFAKS LAMLGSSEDN
     TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI RLLAIVRAAF DQRMKTWQRW
     QDAQATLQKK REAEARLLWA NKPDKLQQAK DEILEWESRV TQYERDFERI STVVRKEVIR
     FEKEKSKDFK NHVIKYLETL LYSQQQLAKY WEAFLPEAKA IS
 
 
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