Full text data of SNX3
SNX3
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Sorting nexin-3 (Protein SDP3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Sorting nexin-3 (Protein SDP3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O60493
ID SNX3_HUMAN Reviewed; 162 AA.
AC O60493; A8K0B1; E1P5E4; E1P5E5; O60718; Q4TT29; Q4TT31; Q5JXJ7;
read moreAC Q5JXJ8; Q96AP9; Q9C0J5; Q9NU45;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Sorting nexin-3;
DE AltName: Full=Protein SDP3;
GN Name=SNX3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9819414;
RA Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.;
RT "Identification of a family of sorting nexin molecules and
RT characterization of their association with receptors.";
RL Mol. Cell. Biol. 18:7278-7287(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, PHOSPHOINOSITIDE-BINDING, DOMAIN PX, AND MUTAGENESIS OF
RP 69-ARG--TYR-71 AND TYR-71.
RX PubMed=11433298; DOI=10.1038/35083051;
RA Xu Y., Hortsman H., Seet L., Wong S.H., Hong W.;
RT "SNX3 regulates endosomal function through its PX-domain-mediated
RT interaction with PtdIns(3)P.";
RL Nat. Cell Biol. 3:658-666(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Hayama A., Uchida S., Sasaki S., Marumo F.;
RT "Homo sapiens sorting nexin 3A (SNX 3A) mRNA.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Colon, Pancreas, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP CHROMOSOMAL TRANSLOCATION, AND INVOLVEMENT IN MCOPS8.
RX PubMed=12471201; DOI=10.1136/jmg.39.12.893;
RA Vervoort V.S., Viljoen D., Smart R., Suthers G., DuPont B.R.,
RA Abbott A., Schwartz C.E.;
RT "Sorting nexin 3 (SNX3) is disrupted in a patient with a translocation
RT t(6;13)(q21;q12) and microcephaly, microphthalmia, ectrodactyly,
RT prognathism (MMEP) phenotype.";
RL J. Med. Genet. 39:893-899(2002).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP FUNCTION.
RX PubMed=18767904; DOI=10.1371/journal.pbio.0060214;
RA Pons V., Luyet P.P., Morel E., Abrami L., van der Goot F.G.,
RA Parton R.G., Gruenberg J.;
RT "Hrs and SNX3 functions in sorting and membrane invagination within
RT multivesicular bodies.";
RL PLoS Biol. 6:E214-E214(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 24-155.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the PX domain of human sorting nexin 3.";
RL Submitted (MAR-2013) to the PDB data bank.
CC -!- FUNCTION: Phosphoinositide-binding protein required for
CC multivesicular body formation. Specifically binds
CC phosphatidylinositol 3-phosphate (PtdIns(P3)). Plays a role in
CC protein transport between cellular compartments. Promotes
CC stability and cell surface expression of epithelial sodium channel
CC (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in
CC EGFR degradation.
CC -!- SUBUNIT: Interacts with USP10 and SCNN1A (By similarity).
CC -!- INTERACTION:
CC P46108:CRK; NbExp=2; IntAct=EBI-727209, EBI-886;
CC -!- SUBCELLULAR LOCATION: Early endosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60493-1; Sequence=Displayed;
CC Name=2; Synonyms=SNX 3A;
CC IsoId=O60493-2; Sequence=VSP_006190;
CC Name=3;
CC IsoId=O60493-3; Sequence=VSP_012928;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=O60493-4; Sequence=VSP_014694;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The PX domain mediates specific binding to
CC phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC Deubiquitinated by USP10 (By similarity).
CC -!- DISEASE: Microphthalmia, syndromic, 8 (MCOPS8) [MIM:601349]: A
CC very rare congenital syndrome characterized by microcephaly,
CC microphthalmia, ectrodactyly of the lower limbs and prognathism.
CC Intellectual deficit has been reported. Microphthalmia is a
CC disorder of eye formation, ranging from small size of a single eye
CC to complete bilateral absence of ocular tissues (anophthalmia). In
CC many cases, microphthalmia/anophthalmia occurs in association with
CC syndromes that include non-ocular abnormalities. Note=The gene
CC represented in this entry may be involved in disease pathogenesis.
CC A chromosomal aberration involving SNX3 has been found in patients
CC with syndromic microphthalmia. Translocation t(6;13)(q21;q12).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR EMBL; AF034546; AAC16040.1; -; mRNA.
DR EMBL; AF062483; AAC16018.1; -; mRNA.
DR EMBL; AB047360; BAB32649.1; -; mRNA.
DR EMBL; AK289476; BAF82165.1; -; mRNA.
DR EMBL; BT007114; AAP35778.1; -; mRNA.
DR EMBL; CR456898; CAG33179.1; -; mRNA.
DR EMBL; AL078596; CAI20817.1; -; Genomic_DNA.
DR EMBL; Z98742; CAI20817.1; JOINED; Genomic_DNA.
DR EMBL; AL078596; CAI20818.1; -; Genomic_DNA.
DR EMBL; Z98742; CAI20818.1; JOINED; Genomic_DNA.
DR EMBL; AL078596; CAI20819.1; -; Genomic_DNA.
DR EMBL; Z98742; CAI20819.1; JOINED; Genomic_DNA.
DR EMBL; Z98742; CAI95646.1; -; Genomic_DNA.
DR EMBL; AL078596; CAI95646.1; JOINED; Genomic_DNA.
DR EMBL; Z98742; CAI95647.1; -; Genomic_DNA.
DR EMBL; AL078596; CAI95647.1; JOINED; Genomic_DNA.
DR EMBL; Z98742; CAI95648.1; -; Genomic_DNA.
DR EMBL; AL078596; CAI95648.1; JOINED; Genomic_DNA.
DR EMBL; CH471051; EAW48378.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48379.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48381.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48382.1; -; Genomic_DNA.
DR EMBL; BC008444; AAH08444.1; -; mRNA.
DR EMBL; BC014580; AAH14580.1; -; mRNA.
DR EMBL; BC015179; AAH15179.1; -; mRNA.
DR EMBL; BC016863; AAH16863.1; -; mRNA.
DR RefSeq; NP_003786.1; NM_003795.4.
DR RefSeq; NP_690040.1; NM_152827.2.
DR RefSeq; XP_005267249.1; XM_005267192.1.
DR UniGene; Hs.12102; -.
DR PDB; 2YPS; X-ray; 2.60 A; A/B/C/D=24-155.
DR PDBsum; 2YPS; -.
DR ProteinModelPortal; O60493; -.
DR SMR; O60493; 24-148.
DR IntAct; O60493; 9.
DR MINT; MINT-1421811; -.
DR PhosphoSite; O60493; -.
DR REPRODUCTION-2DPAGE; IPI00815770; -.
DR UCD-2DPAGE; O60493; -.
DR PaxDb; O60493; -.
DR PRIDE; O60493; -.
DR DNASU; 8724; -.
DR Ensembl; ENST00000230085; ENSP00000230085; ENSG00000112335.
DR Ensembl; ENST00000349379; ENSP00000296991; ENSG00000112335.
DR Ensembl; ENST00000368979; ENSP00000357975; ENSG00000112335.
DR Ensembl; ENST00000368982; ENSP00000357978; ENSG00000112335.
DR Ensembl; ENST00000426155; ENSP00000401779; ENSG00000112335.
DR GeneID; 8724; -.
DR KEGG; hsa:8724; -.
DR UCSC; uc003psh.3; human.
DR CTD; 8724; -.
DR GeneCards; GC06M108578; -.
DR H-InvDB; HIX0006117; -.
DR HGNC; HGNC:11174; SNX3.
DR HPA; HPA028638; -.
DR MIM; 601349; phenotype.
DR MIM; 605930; gene.
DR neXtProt; NX_O60493; -.
DR Orphanet; 3434; MMEP syndrome.
DR PharmGKB; PA36013; -.
DR eggNOG; COG5391; -.
DR HOVERGEN; HBG055338; -.
DR InParanoid; O60493; -.
DR OMA; TPSKIRQ; -.
DR OrthoDB; EOG7GJ6G1; -.
DR PhylomeDB; O60493; -.
DR Reactome; REACT_111102; Signal Transduction.
DR GeneWiki; SNX3; -.
DR GenomeRNAi; 8724; -.
DR NextBio; 32723; -.
DR PRO; PR:O60493; -.
DR Bgee; O60493; -.
DR CleanEx; HS_SNX3; -.
DR Genevestigator; O60493; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Chromosomal rearrangement; Complete proteome;
KW Direct protein sequencing; Endosome; Lipid-binding; Microphthalmia;
KW Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 162 Sorting nexin-3.
FT /FTId=PRO_0000213840.
FT DOMAIN 27 151 PX.
FT BINDING 70 70 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 72 72 Phosphatidylinositol 3-phosphate; via
FT amide nitrogen and carbonyl oxygen (By
FT similarity).
FT BINDING 95 95 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 118 118 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 72 72 Phosphoserine.
FT VAR_SEQ 33 54 Missing (in isoform 4).
FT /FTId=VSP_014694.
FT VAR_SEQ 55 86 Missing (in isoform 2).
FT /FTId=VSP_006190.
FT VAR_SEQ 87 162 VVVPPLPGKAFLRQLPFRGDDGIFDDNFIEERKQGLEQFIN
FT KVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA -> PC
FT LRMTSEARSHGRTWCAQNDEKLFCD (in isoform 3).
FT /FTId=VSP_012928.
FT MUTAGEN 69 71 RRY->AAA: Abolishes binding to
FT phosphatidylinositol 3-phosphate.
FT MUTAGEN 71 71 Y->A: Abolishes binding to
FT phosphatidylinositol 3-phosphate.
FT CONFLICT 100 101 QL -> HF (in Ref. 2; AAC16018).
FT CONFLICT 151 151 D -> V (in Ref. 4; BAF82165).
FT STRAND 29 34
FT HELIX 44 46
FT STRAND 49 55
FT STRAND 63 69
FT HELIX 71 84
FT HELIX 114 131
FT HELIX 133 136
FT HELIX 139 146
SQ SEQUENCE 162 AA; 18762 MW; 983D422FCA6E07BC CRC64;
MAETVADTRR LITKPQNLND AYGPPSNFLE IDVSNPQTVG VGRGRFTTYE IRVKTNLPIF
KLKESTVRRR YSDFEWLRSE LERESKVVVP PLPGKAFLRQ LPFRGDDGIF DDNFIEERKQ
GLEQFINKVA GHPLAQNERC LHMFLQDEII DKSYTPSKIR HA
//
ID SNX3_HUMAN Reviewed; 162 AA.
AC O60493; A8K0B1; E1P5E4; E1P5E5; O60718; Q4TT29; Q4TT31; Q5JXJ7;
read moreAC Q5JXJ8; Q96AP9; Q9C0J5; Q9NU45;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Sorting nexin-3;
DE AltName: Full=Protein SDP3;
GN Name=SNX3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9819414;
RA Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.;
RT "Identification of a family of sorting nexin molecules and
RT characterization of their association with receptors.";
RL Mol. Cell. Biol. 18:7278-7287(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, PHOSPHOINOSITIDE-BINDING, DOMAIN PX, AND MUTAGENESIS OF
RP 69-ARG--TYR-71 AND TYR-71.
RX PubMed=11433298; DOI=10.1038/35083051;
RA Xu Y., Hortsman H., Seet L., Wong S.H., Hong W.;
RT "SNX3 regulates endosomal function through its PX-domain-mediated
RT interaction with PtdIns(3)P.";
RL Nat. Cell Biol. 3:658-666(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Hayama A., Uchida S., Sasaki S., Marumo F.;
RT "Homo sapiens sorting nexin 3A (SNX 3A) mRNA.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Colon, Pancreas, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP CHROMOSOMAL TRANSLOCATION, AND INVOLVEMENT IN MCOPS8.
RX PubMed=12471201; DOI=10.1136/jmg.39.12.893;
RA Vervoort V.S., Viljoen D., Smart R., Suthers G., DuPont B.R.,
RA Abbott A., Schwartz C.E.;
RT "Sorting nexin 3 (SNX3) is disrupted in a patient with a translocation
RT t(6;13)(q21;q12) and microcephaly, microphthalmia, ectrodactyly,
RT prognathism (MMEP) phenotype.";
RL J. Med. Genet. 39:893-899(2002).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
RP FUNCTION.
RX PubMed=18767904; DOI=10.1371/journal.pbio.0060214;
RA Pons V., Luyet P.P., Morel E., Abrami L., van der Goot F.G.,
RA Parton R.G., Gruenberg J.;
RT "Hrs and SNX3 functions in sorting and membrane invagination within
RT multivesicular bodies.";
RL PLoS Biol. 6:E214-E214(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 24-155.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the PX domain of human sorting nexin 3.";
RL Submitted (MAR-2013) to the PDB data bank.
CC -!- FUNCTION: Phosphoinositide-binding protein required for
CC multivesicular body formation. Specifically binds
CC phosphatidylinositol 3-phosphate (PtdIns(P3)). Plays a role in
CC protein transport between cellular compartments. Promotes
CC stability and cell surface expression of epithelial sodium channel
CC (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in
CC EGFR degradation.
CC -!- SUBUNIT: Interacts with USP10 and SCNN1A (By similarity).
CC -!- INTERACTION:
CC P46108:CRK; NbExp=2; IntAct=EBI-727209, EBI-886;
CC -!- SUBCELLULAR LOCATION: Early endosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60493-1; Sequence=Displayed;
CC Name=2; Synonyms=SNX 3A;
CC IsoId=O60493-2; Sequence=VSP_006190;
CC Name=3;
CC IsoId=O60493-3; Sequence=VSP_012928;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=O60493-4; Sequence=VSP_014694;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The PX domain mediates specific binding to
CC phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC Deubiquitinated by USP10 (By similarity).
CC -!- DISEASE: Microphthalmia, syndromic, 8 (MCOPS8) [MIM:601349]: A
CC very rare congenital syndrome characterized by microcephaly,
CC microphthalmia, ectrodactyly of the lower limbs and prognathism.
CC Intellectual deficit has been reported. Microphthalmia is a
CC disorder of eye formation, ranging from small size of a single eye
CC to complete bilateral absence of ocular tissues (anophthalmia). In
CC many cases, microphthalmia/anophthalmia occurs in association with
CC syndromes that include non-ocular abnormalities. Note=The gene
CC represented in this entry may be involved in disease pathogenesis.
CC A chromosomal aberration involving SNX3 has been found in patients
CC with syndromic microphthalmia. Translocation t(6;13)(q21;q12).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR EMBL; AF034546; AAC16040.1; -; mRNA.
DR EMBL; AF062483; AAC16018.1; -; mRNA.
DR EMBL; AB047360; BAB32649.1; -; mRNA.
DR EMBL; AK289476; BAF82165.1; -; mRNA.
DR EMBL; BT007114; AAP35778.1; -; mRNA.
DR EMBL; CR456898; CAG33179.1; -; mRNA.
DR EMBL; AL078596; CAI20817.1; -; Genomic_DNA.
DR EMBL; Z98742; CAI20817.1; JOINED; Genomic_DNA.
DR EMBL; AL078596; CAI20818.1; -; Genomic_DNA.
DR EMBL; Z98742; CAI20818.1; JOINED; Genomic_DNA.
DR EMBL; AL078596; CAI20819.1; -; Genomic_DNA.
DR EMBL; Z98742; CAI20819.1; JOINED; Genomic_DNA.
DR EMBL; Z98742; CAI95646.1; -; Genomic_DNA.
DR EMBL; AL078596; CAI95646.1; JOINED; Genomic_DNA.
DR EMBL; Z98742; CAI95647.1; -; Genomic_DNA.
DR EMBL; AL078596; CAI95647.1; JOINED; Genomic_DNA.
DR EMBL; Z98742; CAI95648.1; -; Genomic_DNA.
DR EMBL; AL078596; CAI95648.1; JOINED; Genomic_DNA.
DR EMBL; CH471051; EAW48378.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48379.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48381.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48382.1; -; Genomic_DNA.
DR EMBL; BC008444; AAH08444.1; -; mRNA.
DR EMBL; BC014580; AAH14580.1; -; mRNA.
DR EMBL; BC015179; AAH15179.1; -; mRNA.
DR EMBL; BC016863; AAH16863.1; -; mRNA.
DR RefSeq; NP_003786.1; NM_003795.4.
DR RefSeq; NP_690040.1; NM_152827.2.
DR RefSeq; XP_005267249.1; XM_005267192.1.
DR UniGene; Hs.12102; -.
DR PDB; 2YPS; X-ray; 2.60 A; A/B/C/D=24-155.
DR PDBsum; 2YPS; -.
DR ProteinModelPortal; O60493; -.
DR SMR; O60493; 24-148.
DR IntAct; O60493; 9.
DR MINT; MINT-1421811; -.
DR PhosphoSite; O60493; -.
DR REPRODUCTION-2DPAGE; IPI00815770; -.
DR UCD-2DPAGE; O60493; -.
DR PaxDb; O60493; -.
DR PRIDE; O60493; -.
DR DNASU; 8724; -.
DR Ensembl; ENST00000230085; ENSP00000230085; ENSG00000112335.
DR Ensembl; ENST00000349379; ENSP00000296991; ENSG00000112335.
DR Ensembl; ENST00000368979; ENSP00000357975; ENSG00000112335.
DR Ensembl; ENST00000368982; ENSP00000357978; ENSG00000112335.
DR Ensembl; ENST00000426155; ENSP00000401779; ENSG00000112335.
DR GeneID; 8724; -.
DR KEGG; hsa:8724; -.
DR UCSC; uc003psh.3; human.
DR CTD; 8724; -.
DR GeneCards; GC06M108578; -.
DR H-InvDB; HIX0006117; -.
DR HGNC; HGNC:11174; SNX3.
DR HPA; HPA028638; -.
DR MIM; 601349; phenotype.
DR MIM; 605930; gene.
DR neXtProt; NX_O60493; -.
DR Orphanet; 3434; MMEP syndrome.
DR PharmGKB; PA36013; -.
DR eggNOG; COG5391; -.
DR HOVERGEN; HBG055338; -.
DR InParanoid; O60493; -.
DR OMA; TPSKIRQ; -.
DR OrthoDB; EOG7GJ6G1; -.
DR PhylomeDB; O60493; -.
DR Reactome; REACT_111102; Signal Transduction.
DR GeneWiki; SNX3; -.
DR GenomeRNAi; 8724; -.
DR NextBio; 32723; -.
DR PRO; PR:O60493; -.
DR Bgee; O60493; -.
DR CleanEx; HS_SNX3; -.
DR Genevestigator; O60493; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Chromosomal rearrangement; Complete proteome;
KW Direct protein sequencing; Endosome; Lipid-binding; Microphthalmia;
KW Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 162 Sorting nexin-3.
FT /FTId=PRO_0000213840.
FT DOMAIN 27 151 PX.
FT BINDING 70 70 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 72 72 Phosphatidylinositol 3-phosphate; via
FT amide nitrogen and carbonyl oxygen (By
FT similarity).
FT BINDING 95 95 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT BINDING 118 118 Phosphatidylinositol 3-phosphate (By
FT similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 72 72 Phosphoserine.
FT VAR_SEQ 33 54 Missing (in isoform 4).
FT /FTId=VSP_014694.
FT VAR_SEQ 55 86 Missing (in isoform 2).
FT /FTId=VSP_006190.
FT VAR_SEQ 87 162 VVVPPLPGKAFLRQLPFRGDDGIFDDNFIEERKQGLEQFIN
FT KVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA -> PC
FT LRMTSEARSHGRTWCAQNDEKLFCD (in isoform 3).
FT /FTId=VSP_012928.
FT MUTAGEN 69 71 RRY->AAA: Abolishes binding to
FT phosphatidylinositol 3-phosphate.
FT MUTAGEN 71 71 Y->A: Abolishes binding to
FT phosphatidylinositol 3-phosphate.
FT CONFLICT 100 101 QL -> HF (in Ref. 2; AAC16018).
FT CONFLICT 151 151 D -> V (in Ref. 4; BAF82165).
FT STRAND 29 34
FT HELIX 44 46
FT STRAND 49 55
FT STRAND 63 69
FT HELIX 71 84
FT HELIX 114 131
FT HELIX 133 136
FT HELIX 139 146
SQ SEQUENCE 162 AA; 18762 MW; 983D422FCA6E07BC CRC64;
MAETVADTRR LITKPQNLND AYGPPSNFLE IDVSNPQTVG VGRGRFTTYE IRVKTNLPIF
KLKESTVRRR YSDFEWLRSE LERESKVVVP PLPGKAFLRQ LPFRGDDGIF DDNFIEERKQ
GLEQFINKVA GHPLAQNERC LHMFLQDEII DKSYTPSKIR HA
//
MIM
601349
*RECORD*
*FIELD* NO
601349
*FIELD* TI
%601349 MICROPHTHALMIA, SYNDROMIC 8; MCOPS8
;;MICROCEPHALY, MICROPHTHALMIA, ECTRODACTYLY OF LOWER LIMBS, AND PROGNATHISM;
read moreMMEP
*FIELD* TX
CLINICAL FEATURES
Viljoen and Smart (1993) described a woman with mental retardation,
borderline microcephaly, microphthalmia, prognathism, cleft lip and
palate, ectrodactyly of the feet, and premature aging of the skin. Her
karyotype showed a de novo translocation 46,XX,t(6;13)(q21;q12).
Suthers and Morris (1996) reported a mentally retarded man with
borderline microcephaly, microphthalmia, microcornea, prognathism, wide
gap between his upper central incisors, ventricular septal defect,
split-feet, cryptorchidism, and normal karyotype. They proposed that
their patient and that of Viljoen and Smart (1993) represented a
distinct syndrome which could be related to mutation in a gene located
on either 6q21 or 13q12.
Van den Ende et al. (1996) described the association of congenital heart
defects and split-feet in 4 infants who had the additional
manifestations of short palpebral fissures and micrognathia; see 601348.
It is possible that the various facial abnormalities reflect age-related
differences.
CYTOGENETICS
In the patient with MMEP and translocation 46,XX,t(6;13)(q21;q12)
reported by Viljoen and Smart (1993), Vervoort et al. (2002) localized
the breakpoint on chromosome 6q21 close to marker D6S1250. Cloning of
the breakpoint fragment allowed localization of the der(13) breakpoint
close to a marker in the region 13q11-q12. Sequencing of the chromosome
13 breakpoint confirmed that the translocation was balanced, with no
missing or duplicated material. No gene on chromosome 13 appeared to be
disrupted, whereas the SNX3 gene on 6q21 was. Mutation screening of
another sporadic case of MMEP failed to detect any point mutations or
deletions in the SNX3 coding sequence. Because of the possibility of
positional effect, Vervoort et al. (2002) suggested that another
candidate gene in the vicinity of the chromosome 6 breakpoint may have
been responsible for MMEP in the original patient or, just as likely,
the MMEP phenotype in the 2 patients resulted from different genetic
causes.
*FIELD* RF
1. Suthers, G.; Morris, L.: A second case of microcephaly, microphthalmia,
ectrodactyly (split-foot) and prognathism (MMEP). Clin. Dysmorph. 5:
77-79, 1996.
2. Van den Ende, J. J.; Van der Burgt, C. J. A. M.; Jansweijer, M.
C. E.; Hamel, B. C. J.; Brunner, H. G.: Ectrodactyly of lower limbs,
congenital heart defect and characteristic facies in four unrelated
Dutch patients: a new association. Clin. Dysmorph. 5: 1-7, 1996.
3. Vervoort, V. S.; Viljoen, D.; Smart, R.; Suthers, G.; DuPont, B.
R.; Abbott, A.; Schwartz, C. E.: Sorting nexin 3 (SNX3) is disrupted
in a patient with a translocation t(6;13)(q21;q12) and microcephaly,
microphthalmia, ectrodactyly, prognathism (MMEP) phenotype. J. Med.
Genet. 39: 893-899, 2002.
4. Viljoen, D. L.; Smart, R.: Split-foot anomaly, microphthalmia,
cleft-lip and cleft-palate, and mental retardation associated with
a chromosome 6;13 translocation. Clin. Dysmorph. 2: 274-277, 1993.
*FIELD* CS
Neuro:
Mental retardation
Head:
Borderline microcephaly
Eyes:
Microphthalmia;
Microcornea;
Short palpebral fissures
Mandible:
Prognathism
Mouth:
Cleft lip/palate
Limbs:
Ectrodactyly of feet
Skin:
Premature skin aging
Teeth:
Wide gap between upper central incisors
GU:
Cryptorchidism
Lab:
De novo translocation 46,XX,t(6,13)(q21,q12)
Inheritance:
? Autosomal dominant
*FIELD* CD
John F. Jackson: 10/3/1997
*FIELD* ED
joanna: 05/19/2011
*FIELD* CN
Marla J. F. O'Neill - updated: 6/1/2006
Victor A. McKusick - updated: 7/8/2003
*FIELD* CD
Iosif W. Lurie: 7/20/1996
*FIELD* ED
carol: 10/30/2009
carol: 6/1/2006
tkritzer: 7/15/2003
tkritzer: 7/9/2003
tkritzer: 7/8/2003
carol: 7/22/1996
*RECORD*
*FIELD* NO
601349
*FIELD* TI
%601349 MICROPHTHALMIA, SYNDROMIC 8; MCOPS8
;;MICROCEPHALY, MICROPHTHALMIA, ECTRODACTYLY OF LOWER LIMBS, AND PROGNATHISM;
read moreMMEP
*FIELD* TX
CLINICAL FEATURES
Viljoen and Smart (1993) described a woman with mental retardation,
borderline microcephaly, microphthalmia, prognathism, cleft lip and
palate, ectrodactyly of the feet, and premature aging of the skin. Her
karyotype showed a de novo translocation 46,XX,t(6;13)(q21;q12).
Suthers and Morris (1996) reported a mentally retarded man with
borderline microcephaly, microphthalmia, microcornea, prognathism, wide
gap between his upper central incisors, ventricular septal defect,
split-feet, cryptorchidism, and normal karyotype. They proposed that
their patient and that of Viljoen and Smart (1993) represented a
distinct syndrome which could be related to mutation in a gene located
on either 6q21 or 13q12.
Van den Ende et al. (1996) described the association of congenital heart
defects and split-feet in 4 infants who had the additional
manifestations of short palpebral fissures and micrognathia; see 601348.
It is possible that the various facial abnormalities reflect age-related
differences.
CYTOGENETICS
In the patient with MMEP and translocation 46,XX,t(6;13)(q21;q12)
reported by Viljoen and Smart (1993), Vervoort et al. (2002) localized
the breakpoint on chromosome 6q21 close to marker D6S1250. Cloning of
the breakpoint fragment allowed localization of the der(13) breakpoint
close to a marker in the region 13q11-q12. Sequencing of the chromosome
13 breakpoint confirmed that the translocation was balanced, with no
missing or duplicated material. No gene on chromosome 13 appeared to be
disrupted, whereas the SNX3 gene on 6q21 was. Mutation screening of
another sporadic case of MMEP failed to detect any point mutations or
deletions in the SNX3 coding sequence. Because of the possibility of
positional effect, Vervoort et al. (2002) suggested that another
candidate gene in the vicinity of the chromosome 6 breakpoint may have
been responsible for MMEP in the original patient or, just as likely,
the MMEP phenotype in the 2 patients resulted from different genetic
causes.
*FIELD* RF
1. Suthers, G.; Morris, L.: A second case of microcephaly, microphthalmia,
ectrodactyly (split-foot) and prognathism (MMEP). Clin. Dysmorph. 5:
77-79, 1996.
2. Van den Ende, J. J.; Van der Burgt, C. J. A. M.; Jansweijer, M.
C. E.; Hamel, B. C. J.; Brunner, H. G.: Ectrodactyly of lower limbs,
congenital heart defect and characteristic facies in four unrelated
Dutch patients: a new association. Clin. Dysmorph. 5: 1-7, 1996.
3. Vervoort, V. S.; Viljoen, D.; Smart, R.; Suthers, G.; DuPont, B.
R.; Abbott, A.; Schwartz, C. E.: Sorting nexin 3 (SNX3) is disrupted
in a patient with a translocation t(6;13)(q21;q12) and microcephaly,
microphthalmia, ectrodactyly, prognathism (MMEP) phenotype. J. Med.
Genet. 39: 893-899, 2002.
4. Viljoen, D. L.; Smart, R.: Split-foot anomaly, microphthalmia,
cleft-lip and cleft-palate, and mental retardation associated with
a chromosome 6;13 translocation. Clin. Dysmorph. 2: 274-277, 1993.
*FIELD* CS
Neuro:
Mental retardation
Head:
Borderline microcephaly
Eyes:
Microphthalmia;
Microcornea;
Short palpebral fissures
Mandible:
Prognathism
Mouth:
Cleft lip/palate
Limbs:
Ectrodactyly of feet
Skin:
Premature skin aging
Teeth:
Wide gap between upper central incisors
GU:
Cryptorchidism
Lab:
De novo translocation 46,XX,t(6,13)(q21,q12)
Inheritance:
? Autosomal dominant
*FIELD* CD
John F. Jackson: 10/3/1997
*FIELD* ED
joanna: 05/19/2011
*FIELD* CN
Marla J. F. O'Neill - updated: 6/1/2006
Victor A. McKusick - updated: 7/8/2003
*FIELD* CD
Iosif W. Lurie: 7/20/1996
*FIELD* ED
carol: 10/30/2009
carol: 6/1/2006
tkritzer: 7/15/2003
tkritzer: 7/9/2003
tkritzer: 7/8/2003
carol: 7/22/1996
MIM
605930
*RECORD*
*FIELD* NO
605930
*FIELD* TI
*605930 SORTING NEXIN 3; SNX3
*FIELD* TX
DESCRIPTION
SNX3 is a member of the sorting nexin family of molecules that contain
read morean approximately 100-amino acid region termed the phox homology (PX)
domain (Haft et al., 1998).
CLONING
By database searching with the sequence of sorting nexin-1 (SNX1;
601272), Haft et al. (1998) obtained several human EST clones,
determined their nucleotide sequences, and constructed full-length cDNAS
corresponding to an isoform of SNX1 (SNX1A), SNX2 (605929), SNX3, and
SNX4 (605931). The SNX3 cDNA encodes a deduced 162-amino acid protein.
Northern blot analysis detected an approximately 1.9-kb SNX3 transcript
in all tissues tested, with highest expression in peripheral leukocytes,
spleen, heart, and skeletal muscle, and low expression in kidney.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SNX3
gene to chromosome 6 (TMAP stSG46058).
GENE FUNCTION
By Western blot analysis, Haft et al. (1998) showed that SNX3 is found
mainly in the cytosol, whereas SNX1, SNX1A, SNX2, and SNX4 are
associated predominantly with membranes. Coimmunoprecipitation studies
detected no association of SNX3 with any receptors studied. Because SNX3
is the human ortholog of yeast Grd19p, Haft et al. (1998) suggested that
SNX3 may associate with late-Golgi resident proteins rather than cell
surface receptors. Based on the functions of their yeast homologs, Haft
et al. (1998) suggested that mammalian sorting nexins function in
intracellular trafficking of proteins to various organelles.
MOLECULAR GENETICS
Viljoen and Smart (1993) described a t(6;13)(q21;q12) translocation in a
patient with microcephaly, microphthalmia, ectrodactyly, and prognathism
(MCOPS8; 601349). Using FISH analysis, Vervoort et al. (2002) localized
the breakpoint on chromosome 6q21 close to marker D6S1250. Cloning of
the breakpoint fragment allowed localization of the der(13) breakpoint
close to a marker in the region 13q11-q12. Sequencing of the chromosome
13 breakpoint confirmed that the translocation was balanced, with no
missing or duplicated material. No gene on chromosome 13 appeared to be
disrupted, whereas the SNX3 gene on 6q21 was. Mutation screening of
another sporadic case of MMEP failed to detect any point mutations or
deletions in the SNX3 coding sequence. Because of the possibility of
positional effect, Vervoort et al. (2002) suggested that another
candidate gene in the vicinity of the chromosome 6 breakpoint may have
been responsible for MMEP in the original patient or, just as likely,
the MMEP phenotype in the 2 patients resulted from different genetic
causes.
*FIELD* RF
1. Haft, C. R.; de la Luz Sierra, M.; Barr, V. A.; Haft, D. H.; Taylor,
S. I.: Identification of a family of sorting nexin molecules and
characterization of their association with receptors. Molec. Cell.
Biol. 18: 7278-7287, 1998.
2. Vervoort, V. S.; Viljoen, D.; Smart, R.; Suthers, G.; DuPont, B.
R.; Abbott, A.; Schwartz, C. E.: Sorting nexin 3 (SNX3) is disrupted
in a patient with a translocation t(6;13)(q21;q12) and microcephaly,
microphthalmia, ectrodactyly, prognathism (MMEP) phenotype. J. Med.
Genet. 39: 893-899, 2002.
3. Viljoen, D. L.; Smart, R.: Split-foot anomaly, microphthalmia,
cleft-lip and cleft-palate, and mental retardation associated with
a chromosome 6;13 translocation. Clin. Dysmorph. 2: 274-277, 1993.
*FIELD* CN
Victor A. McKusick - updated: 6/30/2003
*FIELD* CD
Carol A. Bocchini: 5/14/2001
*FIELD* ED
carol: 10/30/2009
carol: 10/19/2009
tkritzer: 7/15/2003
tkritzer: 7/7/2003
terry: 6/30/2003
mcapotos: 5/16/2001
carol: 5/15/2001
*RECORD*
*FIELD* NO
605930
*FIELD* TI
*605930 SORTING NEXIN 3; SNX3
*FIELD* TX
DESCRIPTION
SNX3 is a member of the sorting nexin family of molecules that contain
read morean approximately 100-amino acid region termed the phox homology (PX)
domain (Haft et al., 1998).
CLONING
By database searching with the sequence of sorting nexin-1 (SNX1;
601272), Haft et al. (1998) obtained several human EST clones,
determined their nucleotide sequences, and constructed full-length cDNAS
corresponding to an isoform of SNX1 (SNX1A), SNX2 (605929), SNX3, and
SNX4 (605931). The SNX3 cDNA encodes a deduced 162-amino acid protein.
Northern blot analysis detected an approximately 1.9-kb SNX3 transcript
in all tissues tested, with highest expression in peripheral leukocytes,
spleen, heart, and skeletal muscle, and low expression in kidney.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SNX3
gene to chromosome 6 (TMAP stSG46058).
GENE FUNCTION
By Western blot analysis, Haft et al. (1998) showed that SNX3 is found
mainly in the cytosol, whereas SNX1, SNX1A, SNX2, and SNX4 are
associated predominantly with membranes. Coimmunoprecipitation studies
detected no association of SNX3 with any receptors studied. Because SNX3
is the human ortholog of yeast Grd19p, Haft et al. (1998) suggested that
SNX3 may associate with late-Golgi resident proteins rather than cell
surface receptors. Based on the functions of their yeast homologs, Haft
et al. (1998) suggested that mammalian sorting nexins function in
intracellular trafficking of proteins to various organelles.
MOLECULAR GENETICS
Viljoen and Smart (1993) described a t(6;13)(q21;q12) translocation in a
patient with microcephaly, microphthalmia, ectrodactyly, and prognathism
(MCOPS8; 601349). Using FISH analysis, Vervoort et al. (2002) localized
the breakpoint on chromosome 6q21 close to marker D6S1250. Cloning of
the breakpoint fragment allowed localization of the der(13) breakpoint
close to a marker in the region 13q11-q12. Sequencing of the chromosome
13 breakpoint confirmed that the translocation was balanced, with no
missing or duplicated material. No gene on chromosome 13 appeared to be
disrupted, whereas the SNX3 gene on 6q21 was. Mutation screening of
another sporadic case of MMEP failed to detect any point mutations or
deletions in the SNX3 coding sequence. Because of the possibility of
positional effect, Vervoort et al. (2002) suggested that another
candidate gene in the vicinity of the chromosome 6 breakpoint may have
been responsible for MMEP in the original patient or, just as likely,
the MMEP phenotype in the 2 patients resulted from different genetic
causes.
*FIELD* RF
1. Haft, C. R.; de la Luz Sierra, M.; Barr, V. A.; Haft, D. H.; Taylor,
S. I.: Identification of a family of sorting nexin molecules and
characterization of their association with receptors. Molec. Cell.
Biol. 18: 7278-7287, 1998.
2. Vervoort, V. S.; Viljoen, D.; Smart, R.; Suthers, G.; DuPont, B.
R.; Abbott, A.; Schwartz, C. E.: Sorting nexin 3 (SNX3) is disrupted
in a patient with a translocation t(6;13)(q21;q12) and microcephaly,
microphthalmia, ectrodactyly, prognathism (MMEP) phenotype. J. Med.
Genet. 39: 893-899, 2002.
3. Viljoen, D. L.; Smart, R.: Split-foot anomaly, microphthalmia,
cleft-lip and cleft-palate, and mental retardation associated with
a chromosome 6;13 translocation. Clin. Dysmorph. 2: 274-277, 1993.
*FIELD* CN
Victor A. McKusick - updated: 6/30/2003
*FIELD* CD
Carol A. Bocchini: 5/14/2001
*FIELD* ED
carol: 10/30/2009
carol: 10/19/2009
tkritzer: 7/15/2003
tkritzer: 7/7/2003
terry: 6/30/2003
mcapotos: 5/16/2001
carol: 5/15/2001