Q6PHU5 (SORT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sortilin

Alternative name(s):
Neurotensin receptor 3
Short name=NTR3
Short name=mNTR3

Gene names

Name:

Sort1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	825 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15
Subunit structure	Interacts with the cytosolic adapter proteins GGA1 and GGA2. Interacts with numerous ligands including the receptor-associated protein LRPAP1/RAP, NTS and GM2A. Forms a complex with NGFR which binds specifically to the precursor forms of NGFB (proNGFB) and BDNF (proBDNF). Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; may regulate their anterograde axonal transport and signaling By similarity. Interacts with LPL, PSAP and SLC2A4. Interacts with NRADD and NGFR. Interaction with NRADD protects against degradation in the lysosome. Ref.7 Ref.9 Ref.12
Subcellular location	Membrane; Single-pass type I membrane protein Potential. Endoplasmic reticulum membrane; Single-pass type I membrane protein Potential. Endosome membrane; Single-pass type I membrane protein Potential. Golgi apparatus › Golgi stack membrane; Single-pass type I membrane protein Potential. Lysosome membrane; Single-pass type I membrane protein Potential. Nucleus membrane; Single-pass type I membrane protein Potential. Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane; Single-pass type I membrane protein Potential. Note: Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. Interaction with NRADD promotes localization at the cell membrane in neurons; this promotes interaction with NGFR. Also found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes is enhanced by insulin. Ref.1 Ref.5 Ref.9 Ref.12
Tissue specificity	Expressed in the brain, particularly the piriform cortex, the cerebral cortex and the hippocampus. Ref.6
Developmental stage	Expressed in the ectoderm at E7.5 and within the germ cell layers at E8.5. Expressed within the neural epithelium and the neural tube at E9.5 and subsequently expressed in the nervous system throughout development. Expression in the proliferative zones of the central nervous system declines between E14.5 and E16.5, while expression remains high in the cerebral cortex and the neural retina. Expressed in the pituitary and the sensory epithelia throughout development. Ref.6
Induction	During adipocyte differentiation. Ref.5 Ref.12
Domain	The N-terminal propeptide may facilitate precursor transport within the Golgi stack. Intrachain binding of the N-terminal propeptide and the extracellular domain may also inhibit premature ligand binding By similarity. The extracellular domain may be shed following protease cleavage in some cell types By similarity.
Post-translational modification	The N-terminal propeptide is cleaved by furin and possibly other homologous proteases By similarity.
Sequence similarities	Belongs to the VPS10-related sortilin family. SORT1 subfamily. Contains 9 BNR repeats.

Ontologies

Keywords
Biological process	Differentiation Endocytosis Osteogenesis Transport
Cellular component	Cell membrane Endoplasmic reticulum Endosome Golgi apparatus Lysosome Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW glucose import Inferred from mutant phenotype Ref.12. Source: BHF-UCL myotube differentiation Inferred from mutant phenotype. Source: BHF-UCL ossification Inferred from electronic annotation. Source: UniProtKB-KW response to insulin stimulus Inferred from mutant phenotype Ref.12. Source: BHF-UCL vesicle organization Inferred from mutant phenotype Ref.12. Source: BHF-UCL
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay Ref.12. Source: BHF-UCL nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.12. Source: BHF-UCL trans-Golgi network transport vesicle Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6PHU5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q6PHU5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     748-748: Q → QDSRPQGHSLSQNPAPPPLGYTENTHFLSPTQKQ

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Propeptide	32 – 75	44	Removed in mature form By similarity		PRO_0000045155
	Chain	76 – 825	750	Sortilin		PRO_0000045156
Regions
	Topological domain	32 – 754	723	Extracellular Potential
	Transmembrane	755 – 775	21	Helical; Potential
	Topological domain	776 – 825	50	Cytoplasmic Potential
	Repeat	143 – 154	12	BNR 1
	Repeat	196 – 207	12	BNR 2
	Repeat	238 – 249	12	BNR 3
	Repeat	285 – 296	12	BNR 4
	Repeat	326 – 337	12	BNR 5
	Repeat	375 – 386	12	BNR 6
	Repeat	426 – 437	12	BNR 7
	Repeat	504 – 515	12	BNR 8
	Repeat	546 – 557	12	BNR 9
	Region	48 – 59	12	Intrachain binding of the propeptide and the extracellular domain By similarity
	Region	610 – 754	145	Interactions with LRPAP1 and NGFB By similarity
	Region	777 – 825	49	Golgi to endosome transport and interactions with GGA1 and GGA2 By similarity
	Motif	785 – 790	6	Endocytosis signal Potential
	Compositional bias	38 – 44	7	Poly-Pro
Amino acid modifications
	Modified residue	819	1	Phosphoserine Ref.13
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	160	1	N-linked (GlcNAc...) Potential
	Glycosylation	272	1	N-linked (GlcNAc...) Potential
	Glycosylation	404	1	N-linked (GlcNAc...) Potential
	Glycosylation	580	1	N-linked (GlcNAc...) Potential
	Glycosylation	682	1	N-linked (GlcNAc...) Potential
	Disulfide bond	84 ↔ 554		By similarity
	Disulfide bond	255 ↔ 275		By similarity
	Disulfide bond	446 ↔ 456		By similarity
	Disulfide bond	610 ↔ 649		By similarity
	Disulfide bond	632 ↔ 664		By similarity
	Disulfide bond	666 ↔ 721		By similarity
	Disulfide bond	673 ↔ 686		By similarity
	Disulfide bond	700 ↔ 738		By similarity
Natural variations
	Alternative sequence	748	1	Q → QDSRPQGHSLSQNPAPPPLG YTENTHFLSPTQKQ in isoform 2.		VSP_016650
Experimental info
	Sequence conflict	315	1	V → E in AAF22639. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 9A7A73C6FE1C8201	FASTA	825	91,200
	10 20 30 40 50 60 MERPRGAADG LLRWPLGLLL LLQLLPPAAV GQDRLDAPPP PAPPLLRWAG PVGVSWGLRA 70 80 90 100 110 120 AAPGGPVPRA GRWRRGAPAE DQDCGRLPDF IAKLTNNTHQ HVFDDLSGSV SLSWVGDSTG 130 140 150 160 170 180 VILVLTTFQV PLVIVSFGQS KLYRSEDYGK NFKDITNLIN NTFIRTEFGM AIGPENSGKV 190 200 210 220 230 240 ILTAEVSGGS RGGRVFRSSD FAKNFVQTDL PFHPLTQMMY SPQNSDYLLA LSTENGLWVS 250 260 270 280 290 300 KNFGEKWEEI HKAVCLAKWG PNNIIFFTTH VNGSCKADLG ALELWRTSDL GKTFKTIGVK 310 320 330 340 350 360 IYSFGLGGRF LFASVMADKD TTRRIHVSTD QGDTWSMAQL PSVGQEQFYS ILAANEDMVF 370 380 390 400 410 420 MHVDEPGDTG FGTIFTSDDR GIVYSKSLDR HLYTTTGGET DFTNVTSLRG VYITSTLSED 430 440 450 460 470 480 NSIQSMITFD QGGRWEHLRK PENSKCDATA KNKNECSLHI HASYSISQKL NVPMAPLSEP 490 500 510 520 530 540 NAVGIVIAHG SVGDAISVMV PDVYISDDGG YSWAKMLEGP HYYTILDSGG IIVAIEHSNR 550 560 570 580 590 600 PINVIKFSTD EGQCWQSYVF TQEPIYFTGL ASEPGARSMN ISIWGFTESF ITRQWVSYTV 610 620 630 640 650 660 DFKDILERNC EEDDYTTWLA HSTDPGDYKD GCILGYKEQF LRLRKSSVCQ NGRDYVVAKQ 670 680 690 700 710 720 PSVCPCSLED FLCDFGYFRP ENASECVEQP ELKGHELEFC LYGKEEHLTT NGYRKIPGDK 730 740 750 760 770 780 CQGGMNPARE VKDLKKKCTS NFLNPTKQNS KSNSVPIILA IVGLMLVTVV AGVLIVKKYV 790 800 810 820 CGGRFLVHRY SVLQQHAEAD GVEALDSTSH AKSGYHDDSD EDLLE
	Isoform 2 [UniParc]. Checksum: B4AC632F993E8E14	FASTA	858	94,813
	10 20 30 40 50 60 MERPRGAADG LLRWPLGLLL LLQLLPPAAV GQDRLDAPPP PAPPLLRWAG PVGVSWGLRA 70 80 90 100 110 120 AAPGGPVPRA GRWRRGAPAE DQDCGRLPDF IAKLTNNTHQ HVFDDLSGSV SLSWVGDSTG 130 140 150 160 170 180 VILVLTTFQV PLVIVSFGQS KLYRSEDYGK NFKDITNLIN NTFIRTEFGM AIGPENSGKV 190 200 210 220 230 240 ILTAEVSGGS RGGRVFRSSD FAKNFVQTDL PFHPLTQMMY SPQNSDYLLA LSTENGLWVS 250 260 270 280 290 300 KNFGEKWEEI HKAVCLAKWG PNNIIFFTTH VNGSCKADLG ALELWRTSDL GKTFKTIGVK 310 320 330 340 350 360 IYSFGLGGRF LFASVMADKD TTRRIHVSTD QGDTWSMAQL PSVGQEQFYS ILAANEDMVF 370 380 390 400 410 420 MHVDEPGDTG FGTIFTSDDR GIVYSKSLDR HLYTTTGGET DFTNVTSLRG VYITSTLSED 430 440 450 460 470 480 NSIQSMITFD QGGRWEHLRK PENSKCDATA KNKNECSLHI HASYSISQKL NVPMAPLSEP 490 500 510 520 530 540 NAVGIVIAHG SVGDAISVMV PDVYISDDGG YSWAKMLEGP HYYTILDSGG IIVAIEHSNR 550 560 570 580 590 600 PINVIKFSTD EGQCWQSYVF TQEPIYFTGL ASEPGARSMN ISIWGFTESF ITRQWVSYTV 610 620 630 640 650 660 DFKDILERNC EEDDYTTWLA HSTDPGDYKD GCILGYKEQF LRLRKSSVCQ NGRDYVVAKQ 670 680 690 700 710 720 PSVCPCSLED FLCDFGYFRP ENASECVEQP ELKGHELEFC LYGKEEHLTT NGYRKIPGDK 730 740 750 760 770 780 CQGGMNPARE VKDLKKKCTS NFLNPTKQDS RPQGHSLSQN PAPPPLGYTE NTHFLSPTQK 790 800 810 820 830 840 QNSKSNSVPI ILAIVGLMLV TVVAGVLIVK KYVCGGRFLV HRYSVLQQHA EADGVEALDS 850 TSHAKSGYHD DSDEDLLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pharmacological properties of the mouse neurotensin receptor 3. Maintenance of cell surface receptor during internalization of neurotensin." Navarro V., Martin S., Sarret P., Nielsen M.S., Petersen C.M., Vincent J.-P., Mazella J. FEBS Lett. 495:100-105(2001) [PubMed: 11322955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS A NEUROTENSIN RECEPTOR, SUBCELLULAR LOCATION, GLYCOSYLATION. Strain: BALB/c. Tissue: Brain.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6. Tissue: Brain.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Brain and Salivary gland.
[5]	"Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes." Morris N.J., Ross S.A., Lane W.S., Moestrup S.K., Petersen C.M., Keller S.R., Lienhard G.E. J. Biol. Chem. 273:3582-3587(1998) [PubMed: 9452485] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION.
[6]	"Expression of the 100-kDa neurotensin receptor sortilin during mouse embryonal development." Hermans-Borgmeyer I., Hermey G., Nykjaer A., Schaller C. Brain Res. Mol. Brain Res. 65:216-219(1999) [PubMed: 10064893] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]	"Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase." Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M. J. Biol. Chem. 274:8832-8836(1999) [PubMed: 10085125] [Abstract] Cited for: INTERACTION WITH LPL.
[8]	"Characterization of insulin-responsive GLUT4 storage vesicles isolated from 3T3-L1 adipocytes." Hashiramoto M., James D.E. Mol. Cell. Biol. 20:416-427(2000) [PubMed: 10594043] [Abstract] Cited for: FUNCTION.
[9]	"Study of the mouse sortilin gene: effects of its transient silencing by RNA interference in TM4 Sertoli cells." Zeng J., Hassan A.J., Morales C.R. Mol. Reprod. Dev. 68:469-475(2004) [PubMed: 15236332] [Abstract] Cited for: FUNCTION, INTERACTION WITH PSAP, SUBCELLULAR LOCATION.
[10]	"The trafficking of prosaposin (SGP-1) and GM2AP to the lysosomes of TM4 Sertoli cells is mediated by sortilin and monomeric adaptor proteins." Hassan A.J., Zeng J., Ni X., Morales C.R. Mol. Reprod. Dev. 68:476-483(2004) [PubMed: 15236333] [Abstract] Cited for: FUNCTION.
[11]	"Neurotensin receptor-3/sortilin mediates neurotensin-induced cytokine/chemokine expression in a murine microglial cell line." Dicou E., Vincent J.-P., Mazella J. J. Neurosci. Res. 78:92-99(2004) [PubMed: 15372498] [Abstract] Cited for: FUNCTION.
[12]	"Sortilin is essential and sufficient for the formation of Glut4 storage vesicles in 3T3-L1 adipocytes." Shi J., Kandror K.V. Dev. Cell 9:99-108(2005) [PubMed: 15992544] [Abstract] Cited for: FUNCTION, INTERACTION WITH SLC2A4, SUBCELLULAR LOCATION, INDUCTION.
[13]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819, MASS SPECTROMETRY. Tissue: Liver.
[14]	"NRH2 is a trafficking switch to regulate sortilin localization and permit proneurotrophin-induced cell death." Kim T., Hempstead B.L. EMBO J. 28:1612-1623(2009) [PubMed: 19407813] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NGFR AND NRADD.
[15]	"Sortilin associates with Trk receptors to enhance anterograde transport and neurotrophin signaling." Vaegter C.B., Jansen P., Fjorback A.W., Glerup S., Skeldal S., Kjolby M., Richner M., Erdmann B., Nyengaard J.R., Tessarollo L., Lewin G.R., Willnow T.E., Chao M.V., Nykjaer A. Nat. Neurosci. 14:54-61(2011) [PubMed: 21102451] [Abstract] Cited for: FUNCTION IN NTRK1 SIGNALING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF175279 mRNA. Translation: AAF22639.1. AK147442 mRNA. Translation: BAE27915.1. AL671899 Genomic DNA. Translation: CAM19473.1. BC034129 mRNA. Translation: AAH34129.1. BC056343 mRNA. Translation: AAH56343.1.
IPI	IPI00420955. IPI00650038.
RefSeq	NP_064356.2. NM_019972.2.
UniGene	Mm.157119.
3D structure databases
ProteinModelPortal	Q6PHU5.
SMR	Q6PHU5. Positions 86-747.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46095N.
STRING	Q6PHU5.
PTM databases
PhosphoSite	Q6PHU5.
Proteomic databases
PRIDE	Q6PHU5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000090564; ENSMUSP00000088052; ENSMUSG00000068747. ENSMUST00000102632; ENSMUSP00000099692; ENSMUSG00000068747.
GeneID	20661.
KEGG	mmu:20661.
UCSC	uc008qyr.1. mouse. uc008qys.1. mouse.
Organism-specific databases
CTD	6272.
MGI	MGI:1338015. Sort1.
Phylogenomic databases
GeneTree	ENSGT00510000046443.
HOVERGEN	HBG080235.
OMA	LTQMMYS.
OrthoDB	EOG4QVCBD.
PhylomeDB	Q6PHU5.
Gene expression databases
ArrayExpress	Q6PHU5.
Bgee	Q6PHU5.
CleanEx	MM_SORT1.
Genevestigator	Q6PHU5.
GermOnline	ENSMUSG00000068747. Mus musculus.
Family and domain databases
InterPro	IPR002860. BNR_rpt. IPR006581. VPS10. [Graphical view]
KO	K12388.
Pfam	PF02012. BNR. 5 hits. [Graphical view]
SMART	SM00602. VPS10. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	299105.
SOURCE	Search...

Entry information

Entry name

SORT_MOUSE

Accession

Primary (citable) accession number: Q6PHU5
Secondary accession number(s): A2AEE8 , Q3UHE2, Q8K043, Q9QXW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program