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Protein

Sorting nexin-5

Gene

Snx5

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 lipids. 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). Does not have in vitro vesicle-to-membrane remodeling activity. Involved in retrograde transport of lysosomal enzyme receptor IGF2R. May function as link between endosomal transport vesicles and dynactin. Plays a role in the internalization of EGFR after EGF stimulation. Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C and is retromer-independent. Together with PIP5K1C facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C-mediated E-cadherin degradation. Plays a role in macropinocytosis (By similarity).By similarity

GO - Molecular functioni

  • dynactin binding Source: UniProtKB
  • phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-5
Gene namesi
Name:Snx5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi1310190. Snx5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 404403Sorting nexin-5PRO_0000405693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei275 – 2751N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiB1H267.
PRIDEiB1H267.

Expressioni

Gene expression databases

ExpressionAtlasiB1H267. baseline and differential.
GenevisibleiB1H267. RN.

Interactioni

Subunit structurei

Forms heterodimers with BAR domain-containing sorting nexins SNX1 and SNX2; does not homodimerize. 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 descibed 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 SNX1, SNX2, VPS26A, VPS29, VPS35, DCTN1, DOCK1, MIB1, PIP5K1C. Interacts with HGS; increased by PIP5K1C kinase activity and by PtdIns(3P) and/or PtdIns(3,4)P2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008934.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 4112Combined sources
Beta strandi44 – 5310Combined sources
Beta strandi58 – 6710Combined sources
Helixi69 – 8113Combined sources
Helixi83 – 853Combined sources
Helixi100 – 11112Combined sources
Helixi112 – 1154Combined sources
Helixi118 – 15235Combined sources
Helixi156 – 1583Combined sources
Helixi160 – 1678Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HPBX-ray2.19A20-180[»]
3HPCX-ray1.47X20-180[»]
ProteinModelPortaliB1H267.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiB1H267.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 172148PXPROSITE-ProRule annotationAdd
BLAST
Domaini202 – 404203BARAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 467Phosphatidylinositol bisphosphate binding1 Publication
Regioni99 – 1057Phosphatidylinositol bisphosphate binding1 Publication
Regioni113 – 1164Phosphatidylinositol bisphosphate binding1 Publication
Regioni169 – 26193Interaction with DOCK1By similarityAdd
BLAST
Regioni183 – 20018Membrane-binding amphipathic helixBy similarityAdd
BLAST

Domaini

The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate.1 Publication
The BAR domain is able to sense membrane curvature upon dimerization. Membrane remodeling seems to implicate insertion of an 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

eggNOGiKOG1660. Eukaryota.
ENOG410XPZY. LUCA.
HOGENOMiHOG000231691.
HOVERGENiHBG000716.
InParanoidiB1H267.
OMAiHEDFIWL.
OrthoDBiEOG7X0VH4.
PhylomeDBiB1H267.
TreeFamiTF313698.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028654. SNX5.
IPR014637. SNX5/SNX6/SNX32.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF6. PTHR10555:SF6. 2 hits.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B1H267-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVPELLEQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH
60 70 80 90 100
TKTTLPTFQS PEFSVTRQHE DFVWLHDTLT ETTDYAGLII PPAPTKPDFD
110 120 130 140 150
GPREKMQKLG EGEGSMTKEE FAKMKQELEA EYLAVFKKTV SSHEVFLQRL
160 170 180 190 200
SSHPVLSKDR NFHVFLEYDQ DLSVRRKNTK EMFGGFFKSV VKSADEVLFS
210 220 230 240 250
GVKEVDDFFE QEKNFLINYY NRIKDSCAKA DKMTRSHKNV ADDYIHTAAC
260 270 280 290 300
LHSLALEEPT VIKKYLLKVA ELFEKLRKVE GRVSSDEDLK LTELLRYYML
310 320 330 340 350
NIEAAKDLLY RRTKALIDYE NSNKALDKAR LKSKDVKLAE THQQECCQKF
360 370 380 390 400
EQLSESAKEE LINFKRKRVA AFRKNLIEMS ELEIKHARNN VSLLQSCIDL

FKNN
Length:404
Mass (Da):46,793
Last modified:April 29, 2008 - v1
Checksum:i26264759D77ECBC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC160883 mRNA. Translation: AAI60883.1.
RefSeqiXP_006235181.1. XM_006235119.2.
UniGeneiRn.86151.

Genome annotation databases

EnsembliENSRNOT00000008934; ENSRNOP00000008934; ENSRNOG00000006077.
ENSRNOT00000074606; ENSRNOP00000066353; ENSRNOG00000006077.
GeneIDi296199.
UCSCiRGD:1310190. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC160883 mRNA. Translation: AAI60883.1.
RefSeqiXP_006235181.1. XM_006235119.2.
UniGeneiRn.86151.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HPBX-ray2.19A20-180[»]
3HPCX-ray1.47X20-180[»]
ProteinModelPortaliB1H267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008934.

Proteomic databases

PaxDbiB1H267.
PRIDEiB1H267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008934; ENSRNOP00000008934; ENSRNOG00000006077.
ENSRNOT00000074606; ENSRNOP00000066353; ENSRNOG00000006077.
GeneIDi296199.
UCSCiRGD:1310190. rat.

Organism-specific databases

CTDi27131.
RGDi1310190. Snx5.

Phylogenomic databases

eggNOGiKOG1660. Eukaryota.
ENOG410XPZY. LUCA.
HOGENOMiHOG000231691.
HOVERGENiHBG000716.
InParanoidiB1H267.
OMAiHEDFIWL.
OrthoDBiEOG7X0VH4.
PhylomeDBiB1H267.
TreeFamiTF313698.

Miscellaneous databases

EvolutionaryTraceiB1H267.
PROiB1H267.

Gene expression databases

ExpressionAtlasiB1H267. baseline and differential.
GenevisibleiB1H267. RN.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028654. SNX5.
IPR014637. SNX5/SNX6/SNX32.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF6. PTHR10555:SF6. 2 hits.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  2. "The phox domain of sorting nexin 5 lacks phosphatidylinositol 3-phosphate (PtdIns(3)P) specificity and preferentially binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)."
    Koharudin L.M., Furey W., Liu H., Liu Y.J., Gronenborn A.M.
    J. Biol. Chem. 284:23697-23707(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 20-180, STRUCTURE BY NMR OF 20-180, DOMAIN, PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE BINDING.

Entry informationi

Entry nameiSNX5_RAT
AccessioniPrimary (citable) accession number: B1H267
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: April 29, 2008
Last modified: May 11, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

The selectivity for particular phosphatidylinositol lipids is under debate. According to one report (PubMed:19553671), the rat protein binds exclusively to phosphatidylinositol 4,5-bisphosphate, while the human protein has been reported (PubMed:15561769) to bind to phosphatidylinositol 3,4-bisphosphate and also to phosphatidylinositol 3-phosphate.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.