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Protein

Sorting nexin-1

Gene

Snx1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity. Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1). Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Involvement in retromer-independent endocytic trafficking of P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R. Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN. Required for endocytosis of DRD5 upon agonist stimulation but not for basal receptor trafficking (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861Phosphatidylinositol 3-phosphateBy similarity
Binding sitei188 – 1881Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei214 – 2141Phosphatidylinositol 3-phosphateBy similarity
Binding sitei238 – 2381Phosphatidylinositol 3-phosphateBy similarity

GO - Molecular functioni

  1. phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

  1. early endosome to Golgi transport Source: GO_Central
  2. endocytosis Source: GO_Central
  3. endosomal transport Source: RGD
  4. intracellular protein transport Source: InterPro
  5. lamellipodium morphogenesis Source: UniProtKB
  6. positive regulation of protein catabolic process Source: RGD
  7. receptor internalization Source: UniProtKB
  8. retrograde transport, endosome to Golgi Source: UniProtKB
  9. vesicle organization Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-1
Gene namesi
Name:Snx1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi68935. Snx1.

Subcellular locationi

Endosome membrane By similarity; Peripheral membrane protein; Cytoplasmic side. Golgi apparatustrans-Golgi network membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionlamellipodium By similarity
Note: Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles. Colocalized with F-actin at the leading edge of lamellipodia in a KALRN-dependent manner.By similarity

GO - Cellular componenti

  1. cytosol Source: RGD
  2. early endosome membrane Source: UniProtKB-SubCell
  3. endosome membrane Source: UniProtKB
  4. extrinsic component of membrane Source: GO_Central
  5. Golgi apparatus Source: UniProtKB-SubCell
  6. lamellipodium Source: UniProtKB-SubCell
  7. membrane Source: RGD
  8. retromer complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Sorting nexin-1PRO_0000213837Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei48 – 481PhosphothreonineBy similarity
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei237 – 2371N6-acetyllysineBy similarity
Modified residuei280 – 2801PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ99N27.
PRIDEiQ99N27.

PTM databases

PhosphoSiteiQ99N27.

Expressioni

Gene expression databases

GenevestigatoriQ99N27.

Interactioni

Subunit structurei

Predominantly forms heterodimers with BAR domain-containing sorting nexins SNX5, SNX6 and SNX32; can self-associate to form homodimers. The heterodimers are proposed to self-assemble into helical arrays on the membrane to stabilize and expand local membrane curvature underlying endosomal tubule formation. Thought to be a component of the originally described retromer complex (also called SNX-BAR retromer) which is a pentamer containing the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting subcomplex (VPS) and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. Interacts with SNX5, SNX6, SNX32, VPS26A, VPS29, VPS35, DRD5, DENND5A, KALRN, RHOG (GDP-bound form). The interaction with SNX2 is reported controversially. Interacts with DNAJC13; prevented by presence of HGS (By similarity). Interacts with HGS (PubMed:11110793).By similarity

Protein-protein interaction databases

IntActiQ99N27. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ99N27.
SMRiQ99N27. Positions 142-269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini143 – 272130PXPROSITE-ProRule annotationAdd
BLAST
Domaini302 – 522221BARAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni281 – 29818Membrane-binding amphipathic helixBy similarityAdd
BLAST

Domaini

The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of a N-terminal amphipatric helix (AH) in the membrane (By similarity).By similarity

Sequence similaritiesi

Belongs to the sorting nexin family.Curated
Contains 1 BAR domain.Curated
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5391.
GeneTreeiENSGT00780000121895.
HOGENOMiHOG000293327.
HOVERGENiHBG000618.
InParanoidiQ99N27.
KOiK17917.
OMAiEIAEWES.
OrthoDBiEOG7HHWSB.
PhylomeDBiQ99N27.
TreeFamiTF313698.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028660. SNX1.
IPR005329. Sorting_nexin_N.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF129. PTHR10555:SF129. 1 hit.
PfamiPF00787. PX. 1 hit.
PF03700. Sorting_nexin. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99N27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGGGGCSA SERLPPPFPG MDPESEGAAG GSEPEAGDSD TEGEDIFTGA
60 70 80 90 100
AAASKPQSPK KTTSLFPIKN GSKENGIHEE QDQEPQDLFA DATVELSLDS
110 120 130 140 150
TQNNQKTMPG KTLIPHPTQE ATNSPKPQPS YEELEEEEQE DQFDLTVGIT
160 170 180 190 200
DPEKIGDGMN AYVAYKVTTQ TSLPMFRSRQ FAVKRRFSDF LGLYEKLSEK
210 220 230 240 250
HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA ALERYLQRIV
260 270 280 290 300
NHPTMLQDPD VREFLEKEEL PRAVGTQALS GAGLLKMFNK ATDAVSKMTI
310 320 330 340 350
KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTALFAKS
360 370 380 390 400
LAMLGSSEDN TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI
410 420 430 440 450
RLLAIVRAAF DQRMKTWQRW QDAQATLQKK RESEARLLWA NKPDKLQQAK
460 470 480 490 500
DEITEWESRV TQYERDFERI STVVRKEVTR FEKEKSKDFK NHVIKYLETL
510 520
LHSQQQLAKY WEAFLPEARA IS
Length:522
Mass (Da):59,044
Last modified:May 31, 2001 - v1
Checksum:iF0F05664087E4D24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218916 mRNA. Translation: AAG59616.1.
BC092201 mRNA. Translation: AAH92201.1.
RefSeqiNP_445863.1. NM_053411.1.
UniGeneiRn.144614.

Genome annotation databases

EnsembliENSRNOT00000022960; ENSRNOP00000022960; ENSRNOG00000017029.
GeneIDi84471.
KEGGirno:84471.
UCSCiRGD:68935. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218916 mRNA. Translation: AAG59616.1.
BC092201 mRNA. Translation: AAH92201.1.
RefSeqiNP_445863.1. NM_053411.1.
UniGeneiRn.144614.

3D structure databases

ProteinModelPortaliQ99N27.
SMRiQ99N27. Positions 142-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99N27. 1 interaction.

PTM databases

PhosphoSiteiQ99N27.

Proteomic databases

PaxDbiQ99N27.
PRIDEiQ99N27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022960; ENSRNOP00000022960; ENSRNOG00000017029.
GeneIDi84471.
KEGGirno:84471.
UCSCiRGD:68935. rat.

Organism-specific databases

CTDi6642.
RGDi68935. Snx1.

Phylogenomic databases

eggNOGiCOG5391.
GeneTreeiENSGT00780000121895.
HOGENOMiHOG000293327.
HOVERGENiHBG000618.
InParanoidiQ99N27.
KOiK17917.
OMAiEIAEWES.
OrthoDBiEOG7HHWSB.
PhylomeDBiQ99N27.
TreeFamiTF313698.

Miscellaneous databases

NextBioi616956.
PROiQ99N27.

Gene expression databases

GenevestigatoriQ99N27.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028660. SNX1.
IPR005329. Sorting_nexin_N.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF129. PTHR10555:SF129. 1 hit.
PfamiPF00787. PX. 1 hit.
PF03700. Sorting_nexin. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor."
    Chin L.-S., Raynor M.C., Wei X., Chen H.-Q., Li L.
    J. Biol. Chem. 276:7069-7078(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HGS.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.

Entry informationi

Entry nameiSNX1_RAT
AccessioniPrimary (citable) accession number: Q99N27
Secondary accession number(s): Q56A25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2001
Last sequence update: May 31, 2001
Last modified: March 3, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds phosphatidylinositol 3-phosphate (PtdIns-3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2) in liposome-based assays. Can bind PtdIns(3,4,5)P3 in protein:lipid overlay assays, but not in liposome-based assays (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.