Sorting nexin-1 - Rattus norvegicus (Rat)

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Q99N27 (SNX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sorting nexin-1

Gene names

Name:

Snx1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in several stages of intracellular trafficking. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) By similarity.
Subunit structure	Self-assembles into a complex of approximately 300 kDa. Component of the retromer complex composed of VPS26 (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts with SNX6 By similarity. Interacts with HGS. Ref.1
Subcellular location	Endosome membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Golgi apparatus › trans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side 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) By similarity.
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.
Sequence similarities	Belongs to the sorting nexin family. Contains 1 BAR domain. Contains 1 PX (phox homology) domain.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endosome Golgi apparatus Membrane
Ligand	Lipid-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell communication Inferred from electronic annotation. Source: InterPro early endosome to Golgi transport Inferred from electronic annotation. Source: Compara endosomal transport Inferred from expression pattern Ref.1. Source: RGD intracellular protein transport Inferred from electronic annotation. Source: Compara positive regulation of protein catabolic process Inferred from mutant phenotype Ref.1. Source: RGD
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.1. Source: RGD early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	phosphatidylinositol binding Inferred from sequence or structural similarity. Source: UniProtKB protein transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 522

522

Sorting nexin-1

PRO_0000213837

Regions

Domain

143 – 272

130

Domain

302 – 522

221

BAR

Sites

Binding site

186

Phosphatidylinositol 3-phosphate By similarity

Binding site

188

Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygen By similarity

Binding site

214

Phosphatidylinositol 3-phosphate By similarity

Binding site

238

Phosphatidylinositol 3-phosphate By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

188

Phosphoserine By similarity

Modified residue

237

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q99N27 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F0F05664087E4D24
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FASTA

522

59,044

        10         20         30         40         50         60 
MASGGGGCSA SERLPPPFPG MDPESEGAAG GSEPEAGDSD TEGEDIFTGA AAASKPQSPK 

        70         80         90        100        110        120 
KTTSLFPIKN GSKENGIHEE QDQEPQDLFA DATVELSLDS TQNNQKTMPG KTLIPHPTQE 

       130        140        150        160        170        180 
ATNSPKPQPS YEELEEEEQE DQFDLTVGIT DPEKIGDGMN AYVAYKVTTQ TSLPMFRSRQ 

       190        200        210        220        230        240 
FAVKRRFSDF LGLYEKLSEK HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA 

       250        260        270        280        290        300 
ALERYLQRIV NHPTMLQDPD VREFLEKEEL PRAVGTQALS GAGLLKMFNK ATDAVSKMTI 

       310        320        330        340        350        360 
KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTALFAKS LAMLGSSEDN 

       370        380        390        400        410        420 
TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI RLLAIVRAAF DQRMKTWQRW 

       430        440        450        460        470        480 
QDAQATLQKK RESEARLLWA NKPDKLQQAK DEITEWESRV TQYERDFERI STVVRKEVTR 

       490        500        510        520 
FEKEKSKDFK NHVIKYLETL LHSQQQLAKY WEAFLPEARA IS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(2001) [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(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF218916 mRNA. Translation: AAG59616.1. BC092201 mRNA. Translation: AAH92201.1.
IPI	IPI00198369.
RefSeq	NP_445863.1. NM_053411.1.
UniGene	Rn.144614.
3D structure databases
ProteinModelPortal	Q99N27.
SMR	Q99N27. Positions 142-269.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99N27. 1 interaction.
PTM databases
PhosphoSite	Q99N27.
Proteomic databases
PaxDb	Q99N27.
PRIDE	Q99N27.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000022960; ENSRNOP00000022960; ENSRNOG00000017029.
GeneID	84471.
KEGG	rno:84471.
UCSC	RGD:68935. rat.
Organism-specific databases
CTD	6642.
RGD	68935. Snx1.
Phylogenomic databases
eggNOG	COG5391.
GeneTree	ENSGT00550000074512.
HOGENOM	HOG000293327.
HOVERGEN	HBG000618.
InParanoid	Q99N27.
OrthoDB	EOG418BNH.
Gene expression databases
ArrayExpress	Q99N27.
Genevestigator	Q99N27.
GermOnline	ENSRNOG00000017029. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.1520.10. 1 hit.
InterPro	IPR001683. Phox. IPR005329. Sorting_nexin_N. IPR015404. Vps5_C. [Graphical view]
Pfam	PF00787. PX. 1 hit. PF03700. Sorting_nexin. 1 hit. PF09325. Vps5. 1 hit. [Graphical view]
SMART	SM00312. PX. 1 hit. [Graphical view]
SUPFAM	SSF64268. PX. 1 hit.
PROSITE	PS51021. BAR. False negative. PS50195. PX. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	616956.

Entry information

Entry name

SNX1_RAT

Accession

Primary (citable) accession number: Q99N27
Secondary accession number(s): Q56A25

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents