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Protein

Sorting nexin-5

Gene

Snx5

Organism
Mus musculus (Mouse)
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 (By similarity). Plays a role in macropinocytosis (PubMed:18854019).By similarity1 Publication

GO - Molecular functioni

  1. dynactin binding Source: UniProtKB
  2. phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

  1. endocytosis Source: GO_Central
  2. intracellular protein transport Source: InterPro
  3. pinocytosis Source: UniProtKB
  4. retrograde transport, endosome to Golgi Source: MGI
  5. vesicle organization Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_342454. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-5
Gene namesi
Name:Snx5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1916428. Snx5.

Subcellular locationi

  1. Endosome By similarity
  2. Early endosome By similarity
  3. Early endosome membrane By similarity; Peripheral membrane protein; Cytoplasmic side
  4. Cell membrane By similarity; Peripheral membrane protein; Cytoplasmic side By similarity
  5. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side
  6. Cytoplasm
  7. Cell projectionphagocytic cup
  8. Cell projectionruffle

  9. Note: Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2) (By similarity). Detected on macropinosomes (PubMed:18854019). Targeted to membrane ruffles in response to EGFR stimulation (By similarity).By similarity1 Publication

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. early endosome membrane Source: UniProtKB-SubCell
  3. endosome Source: GO_Central
  4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  5. extrinsic component of endosome membrane Source: UniProtKB
  6. extrinsic component of membrane Source: GO_Central
  7. macropinocytic cup Source: UniProtKB
  8. phagocytic cup Source: UniProtKB-SubCell
  9. retromer complex Source: UniProtKB
  10. ruffle Source: UniProtKB-SubCell
  11. tubular endosome Source: UniProtKB
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 methioninei1 – 11RemovedBy similarity
Chaini2 – 404403Sorting nexin-5PRO_0000213845Add
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

MaxQBiQ9D8U8.
PaxDbiQ9D8U8.
PRIDEiQ9D8U8.

PTM databases

PhosphoSiteiQ9D8U8.

Expressioni

Tissue specificityi

Detected in macrophages (at protein level).1 Publication

Gene expression databases

BgeeiQ9D8U8.
CleanExiMM_SNX5.
ExpressionAtlasiQ9D8U8. baseline and differential.
GenevestigatoriQ9D8U8.

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

Protein-protein interaction databases

IntActiQ9D8U8. 1 interaction.
MINTiMINT-1751142.

Structurei

3D structure databases

ProteinModelPortaliQ9D8U8.
SMRiQ9D8U8. Positions 20-174.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity
Regioni99 – 1057Phosphatidylinositol bisphosphate bindingBy similarity
Regioni113 – 1164Phosphatidylinositol bisphosphate bindingBy similarity
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.By similarity
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

eggNOGiNOG255198.
GeneTreeiENSGT00780000121944.
HOGENOMiHOG000231691.
HOVERGENiHBG000716.
InParanoidiQ9D8U8.
KOiK17920.
OMAiIKDSCAK.
OrthoDBiEOG7X0VH4.
PhylomeDBiQ9D8U8.
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. 1 hit.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SMARTiSM00312. PX. 1 hit.
[Graphical view]
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.

Q9D8U8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVPELLEQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH
60 70 80 90 100
TKTTLSTFQS PEFSVTRQHE DFVWLHDTLT ETTDYAGLII PPAPTKPDFD
110 120 130 140 150
GPREKMQKLG EGEGSMTKEE FAKMKQELEA EYLAVFKKTV STHEVFLQRL
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):46,797
Last modified:June 1, 2001 - v1
Checksum:iC24D8C78F753FAFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007676 mRNA. Translation: BAB25180.1.
AK029463 mRNA. Translation: BAC26460.1.
AK031873 mRNA. Translation: BAC27587.1.
AK049129 mRNA. Translation: BAC33558.1.
AK159904 mRNA. Translation: BAE35468.1.
AK169786 mRNA. Translation: BAE41365.1.
BC002242 mRNA. Translation: AAH02242.1.
CCDSiCCDS16815.1.
RefSeqiNP_001186117.1. NM_001199188.1.
NP_077187.1. NM_024225.5.
UniGeneiMm.273379.

Genome annotation databases

EnsembliENSMUST00000028909; ENSMUSP00000028909; ENSMUSG00000027423.
ENSMUST00000110030; ENSMUSP00000105657; ENSMUSG00000027423.
GeneIDi69178.
KEGGimmu:69178.
UCSCiuc008mqq.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007676 mRNA. Translation: BAB25180.1.
AK029463 mRNA. Translation: BAC26460.1.
AK031873 mRNA. Translation: BAC27587.1.
AK049129 mRNA. Translation: BAC33558.1.
AK159904 mRNA. Translation: BAE35468.1.
AK169786 mRNA. Translation: BAE41365.1.
BC002242 mRNA. Translation: AAH02242.1.
CCDSiCCDS16815.1.
RefSeqiNP_001186117.1. NM_001199188.1.
NP_077187.1. NM_024225.5.
UniGeneiMm.273379.

3D structure databases

ProteinModelPortaliQ9D8U8.
SMRiQ9D8U8. Positions 20-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D8U8. 1 interaction.
MINTiMINT-1751142.

PTM databases

PhosphoSiteiQ9D8U8.

Proteomic databases

MaxQBiQ9D8U8.
PaxDbiQ9D8U8.
PRIDEiQ9D8U8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028909; ENSMUSP00000028909; ENSMUSG00000027423.
ENSMUST00000110030; ENSMUSP00000105657; ENSMUSG00000027423.
GeneIDi69178.
KEGGimmu:69178.
UCSCiuc008mqq.3. mouse.

Organism-specific databases

CTDi27131.
MGIiMGI:1916428. Snx5.

Phylogenomic databases

eggNOGiNOG255198.
GeneTreeiENSGT00780000121944.
HOGENOMiHOG000231691.
HOVERGENiHBG000716.
InParanoidiQ9D8U8.
KOiK17920.
OMAiIKDSCAK.
OrthoDBiEOG7X0VH4.
PhylomeDBiQ9D8U8.
TreeFamiTF313698.

Enzyme and pathway databases

ReactomeiREACT_342454. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

NextBioi328774.
PROiQ9D8U8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8U8.
CleanExiMM_SNX5.
ExpressionAtlasiQ9D8U8. baseline and differential.
GenevestigatoriQ9D8U8.

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. 1 hit.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Head, Medulla oblongata, Pancreas and Thymus.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "A role for SNX5 in the regulation of macropinocytosis."
    Lim J.P., Wang J.T., Kerr M.C., Teasdale R.D., Gleeson P.A.
    BMC Cell Biol. 9:58-58(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSNX5_MOUSE
AccessioniPrimary (citable) accession number: Q9D8U8
Secondary accession number(s): Q543N9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 104 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.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.