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Q8BVL3 (SNX17_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sorting nexin-17
Gene names
Name:Snx17
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)). Ref.3 Ref.4 Ref.5

Subunit structure

Monomer. Interacts with HRAS. Interacts with ITGB1 and ITGB5 (via NPxY motif). Interacts with KRIT1 (via N-terminus) By similarity. Interacts with the C-termini of P-selectin, PTC, LDLR, VLDLR, LRP1 and LRP8. Interacts with APP (via cytoplasmic YXNPXY motif). Interacts with KIF1B. Ref.3 Ref.4 Ref.5 Ref.6

Subcellular location

Cytoplasm. Early endosome. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity Ref.3 Ref.4 Ref.5.

Tissue specificity

Detected in brain neurons (at protein level). Broadly expressed, with highest levels in brain and placenta, and lowest levels in colon, intestine and liver. Ref.3 Ref.5

Domain

The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)). Required for association with endosomes By similarity.

The PTB-like F3 module within the FERM-like domain mediates cargo recognition via their NPxY sequences, while the F1 module (Ras-associating) is responsible for interaction with membrane-bound HRAS By similarity.

Sequence similarities

Belongs to the sorting nexin family.

Contains 1 PX (phox homology) domain.

Contains 1 Ras-associating domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Sorting nexin-17
PRO_0000236205

Regions

Domain1 – 109109PX
Domain115 – 20692Ras-associating
Region115 – 432318FERM-like By similarity
Region270 – 432163PTB-like F3 module By similarity

Sites

Binding site361Phosphatidylinositol 3-phosphate By similarity
Binding site381Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site621Phosphatidylinositol 3-phosphate By similarity
Binding site751Phosphatidylinositol 3-phosphate By similarity

Amino acid modifications

Modified residue4071Phosphoserine By similarity
Modified residue4091Phosphoserine Ref.7
Modified residue4151Phosphoserine By similarity
Modified residue4211Phosphoserine Ref.7
Modified residue4371Phosphoserine By similarity
Modified residue4401Phosphoserine By similarity

Experimental info

Sequence conflict1981K → E in BAC37004. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BVL3 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 3023B5FAEF38BB42

FASTA47052,797
        10         20         30         40         50         60 
MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE YGANVVPAFP 

        70         80         90        100        110        120 
PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS FLRRAQQETQ QVPTEEVSLE 

       130        140        150        160        170        180 
VLLSNGQKVL VTVLTSDQTE DVLEAVAAKL DLPDDLIGYF SLFLVREKED GAFSFVRKLQ 

       190        200        210        220        230        240 
EFELPYVSVT SLRSQEYKIV LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIEHGWILVT 

       250        260        270        280        290        300 
KEQHRQLKSL QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ 

       310        320        330        340        350        360 
LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGGTSSPSRG RGEVRLELAF EYLMSKDRLQ 

       370        380        390        400        410        420 
WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV GGTLRRSDSQ QAVKSPPLLE 

       430        440        450        460        470 
SPDASRESMV KLSSKLSAVS LRGIGSPSTD ASASAVHGNF AFEGIGDEDL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: Spleen 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].
Strain: FVB/N.
Tissue: Colon and Mammary tumor.
[3]"The PX-domain protein SNX17 interacts with members of the LDL receptor family and modulates endocytosis of the LDL receptor."
Stockinger W., Sailler B., Strasser V., Recheis B., Fasching D., Kahr L., Schneider W.J., Nimpf J.
EMBO J. 21:4259-4267(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LDLR; VLDLR; LRP1 AND LRP8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
[4]"Sorting nexin 17 facilitates LRP recycling in the early endosome."
van Kerkhof P., Lee J., McCormick L., Tetrault E., Lu W., Schoenfish M., Oorschot V., Strous G.J., Klumperman J., Bu G.
EMBO J. 24:2851-2861(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRP1, SUBCELLULAR LOCATION, FUNCTION.
[5]"Adaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes."
Lee J., Retamal C., Cuitino L., Caruano-Yzermans A., Shin J.E., van Kerkhof P., Marzolo M.P., Bu G.
J. Biol. Chem. 283:11501-11508(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APP, TISSUE SPECIFICITY.
[6]"Sorting nexin 17 interacts directly with kinesin superfamily KIF1Bbeta protein."
Seog D.H., Han J.
Korean J. Physiol. Pharmacol. 12:199-204(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIF1B.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK077650 mRNA. Translation: BAC36927.1.
AK077780 mRNA. Translation: BAC37004.1.
AK156299 mRNA. Translation: BAE33663.1.
BC026571 mRNA. Translation: AAH26571.1.
BC023732 mRNA. Translation: AAH23732.1.
CCDSCCDS19177.1.
RefSeqNP_710147.1. NM_153680.2.
UniGeneMm.6118.

3D structure databases

ProteinModelPortalQ8BVL3.
SMRQ8BVL3. Positions 1-109, 112-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000031029.

Proteomic databases

MaxQBQ8BVL3.
PaxDbQ8BVL3.
PRIDEQ8BVL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031029; ENSMUSP00000031029; ENSMUSG00000029146.
GeneID266781.
KEGGmmu:266781.
UCSCuc008wxm.1. mouse.

Organism-specific databases

CTD9784.
MGIMGI:2387801. Snx17.

Phylogenomic databases

eggNOGNOG290558.
GeneTreeENSGT00530000063147.
HOGENOMHOG000007722.
HOVERGENHBG061207.
InParanoidQ8BVL3.
KOK17929.
OMAKKIFTLT.
OrthoDBEOG70CR71.
PhylomeDBQ8BVL3.
TreeFamTF318398.

Gene expression databases

ArrayExpressQ8BVL3.
BgeeQ8BVL3.
CleanExMM_SNX17.
GenevestigatorQ8BVL3.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR019749. Band_41_domain.
IPR001683. Phox.
IPR000159. Ras-assoc.
IPR028666. SNX17.
[Graphical view]
PANTHERPTHR12431:SF16. PTHR12431:SF16. 1 hit.
PfamPF00787. PX. 1 hit.
[Graphical view]
SMARTSM00295. B41. 1 hit.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF64268. SSF64268. 1 hit.
PROSITEPS50195. PX. 1 hit.
PS50200. RA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio392194.
PROQ8BVL3.
SOURCESearch...

Entry information

Entry nameSNX17_MOUSE
AccessionPrimary (citable) accession number: Q8BVL3
Secondary accession number(s): Q8R0N8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 30, 2006
Last modified: July 9, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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