Full text data of SNX5
SNX5
[Confidence: low (only semi-automatic identification from reviews)]
Sorting nexin-5
Sorting nexin-5
UniProt
Q9Y5X3
ID SNX5_HUMAN Reviewed; 404 AA.
AC Q9Y5X3; B7ZKN3; D3DW26; Q52LC4; Q9BWP0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Sorting nexin-5;
GN Name=SNX5;
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], AND SUBCELLULAR LOCATION.
RX PubMed=11485546; DOI=10.1042/0264-6021:3580007;
RA Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.;
RT "A large family of endosome-localized proteins related to sorting
RT nexin 1.";
RL Biochem. J. 358:7-16(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovarian carcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [6]
RP SUBCELLULAR LOCATION, AND PHOSPHATIDYLINOSITOL 3,4-BISPHOSPHATE
RP BINDING.
RX PubMed=15561769; DOI=10.1242/jcs.01561;
RA Merino-Trigo A., Kerr M.C., Houghton F., Lindberg A., Mitchell C.,
RA Teasdale R.D., Gleeson P.A.;
RT "Sorting nexin 5 is localized to a subdomain of the early endosomes
RT and is recruited to the plasma membrane following EGF stimulation.";
RL J. Cell Sci. 117:6413-6424(2004).
RN [7]
RP INTERACTION WITH SNX1, AND SUBCELLULAR LOCATION.
RX PubMed=16968745; DOI=10.1242/jcs.03167;
RA Kerr M.C., Lindsay M.R., Luetterforst R., Hamilton N., Simpson F.,
RA Parton R.G., Gleeson P.A., Teasdale R.D.;
RT "Visualisation of macropinosome maturation by the recruitment of
RT sorting nexins.";
RL J. Cell Sci. 119:3967-3980(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18854019; DOI=10.1186/1471-2121-9-58;
RA Lim J.P., Wang J.T., Kerr M.C., Teasdale R.D., Gleeson P.A.;
RT "A role for SNX5 in the regulation of macropinocytosis.";
RL BMC Cell Biol. 9:58-58(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21048941; DOI=10.1371/journal.pone.0013763;
RA Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S.,
RA Teasdale R.D.;
RT "The SNX-PX-BAR family in macropinocytosis: the regulation of
RT macropinosome formation by SNX-PX-BAR proteins.";
RL PLoS ONE 5:E13763-E13763(2010).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 257-265 IN COMPLEX WITH HLA
RP CLASS I HISTOCOMPATIBILITY COMPLEX.
RX PubMed=15226359; DOI=10.1084/jem.20031680;
RA Zernich D., Purcell A.W., Macdonald W.A., Kjer-Nielsen L., Ely L.K.,
RA Laham N., Crockford T., Mifsud N.A., Bharadwaj M., Chang L.,
RA Tait B.D., Holdsworth R., Brooks A.G., Bottomley S.P., Beddoe T.,
RA Peh C.A., Rossjohn J., McCluskey J.;
RT "Natural HLA class I polymorphism controls the pathway of antigen
RT presentation and susceptibility to viral evasion.";
RL J. Exp. Med. 200:13-24(2004).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. Plays a role in macropinocytosis. Plays a role in the
CC internalization of EGFR after EGF stimulation.
CC -!- SUBUNIT: Interacts with SNX1; this promotes location at the
CC endosome membrane.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasmic vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell
CC projection, phagocytic cup. Cell projection, ruffle.
CC Note=Recruited to the plasma membrane after EGF stimulation, which
CC leads to increased levels of phosphatidylinositol 3,4-bisphosphate
CC (PdtIns(3,4)P2). Detected on macropinosomes. Targeted to membrane
CC ruffles in response to EGFR stimulation.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched
CC in phosphatidylinositol 3,4-bisphosphate and/or
CC phosphatidylinositol 4,5-bisphosphate (By similarity).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC -!- CAUTION: The selectivity for particular phosphatidylinositol
CC lipids is under debate. According to one report (PubMed:19553671),
CC the rat protein binds exclusively to phosphatidylinositol 4,5-
CC bisphosphate, while the human protein has been reported
CC (PubMed:15561769) to bind to phosphatidylinositol 3,4-bisphosphate
CC and also to phosphatidylinositol 3-phosphate.
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DR EMBL; AF121855; AAD27828.1; -; mRNA.
DR EMBL; AK001793; BAA91914.1; -; mRNA.
DR EMBL; AL121585; CAC00471.1; -; Genomic_DNA.
DR EMBL; BC000100; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471133; EAX10264.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10265.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10266.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10268.1; -; Genomic_DNA.
DR EMBL; BC093623; AAH93623.1; -; mRNA.
DR EMBL; BC093980; AAH93980.1; -; mRNA.
DR EMBL; BC143274; AAI43275.1; -; mRNA.
DR RefSeq; NP_055241.1; NM_014426.3.
DR RefSeq; NP_689413.1; NM_152227.2.
DR UniGene; Hs.316890; -.
DR PDB; 1SYS; X-ray; 2.40 A; C=257-265.
DR PDBsum; 1SYS; -.
DR ProteinModelPortal; Q9Y5X3; -.
DR SMR; Q9Y5X3; 20-174.
DR IntAct; Q9Y5X3; 17.
DR MINT; MINT-2823978; -.
DR STRING; 9606.ENSP00000366988; -.
DR PhosphoSite; Q9Y5X3; -.
DR DMDM; 10720289; -.
DR PaxDb; Q9Y5X3; -.
DR PRIDE; Q9Y5X3; -.
DR DNASU; 27131; -.
DR Ensembl; ENST00000377759; ENSP00000366988; ENSG00000089006.
DR Ensembl; ENST00000377768; ENSP00000366998; ENSG00000089006.
DR GeneID; 27131; -.
DR KEGG; hsa:27131; -.
DR UCSC; uc002wqc.3; human.
DR CTD; 27131; -.
DR GeneCards; GC20M017870; -.
DR HGNC; HGNC:14969; SNX5.
DR HPA; CAB020679; -.
DR MIM; 605937; gene.
DR neXtProt; NX_Q9Y5X3; -.
DR PharmGKB; PA37945; -.
DR eggNOG; NOG255198; -.
DR HOVERGEN; HBG000716; -.
DR InParanoid; Q9Y5X3; -.
DR OMA; IKDSCAK; -.
DR OrthoDB; EOG7X0VH4; -.
DR PhylomeDB; Q9Y5X3; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; SNX5; human.
DR EvolutionaryTrace; Q9Y5X3; -.
DR GeneWiki; SNX5; -.
DR GenomeRNAi; 27131; -.
DR NextBio; 49854; -.
DR PRO; PR:Q9Y5X3; -.
DR ArrayExpress; Q9Y5X3; -.
DR Bgee; Q9Y5X3; -.
DR CleanEx; HS_SNX5; -.
DR Genevestigator; Q9Y5X3; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic to cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0031313; C:extrinsic to endosome membrane; IDA:UniProtKB.
DR GO; GO:0070685; C:macropinocytic cup; IDA:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006907; P:pinocytosis; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
DR InterPro; IPR014637; SNX5/SNX6/SNX32.
DR InterPro; IPR015404; Vps5_C.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 1.
DR PIRSF; PIRSF036924; Snx5_Snx6; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS51021; BAR; FALSE_NEG.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cell projection;
KW Complete proteome; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
KW Endosome; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 404 Sorting nexin-5.
FT /FTId=PRO_0000213844.
FT DOMAIN 25 172 PX.
FT DOMAIN 202 404 BAR.
FT REGION 40 46 Phosphatidylinositol bisphosphate binding
FT (By similarity).
FT REGION 99 105 Phosphatidylinositol bisphosphate binding
FT (By similarity).
FT REGION 113 116 Phosphatidylinositol bisphosphate binding
FT (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 275 275 N6-acetyllysine.
FT CONFLICT 279 279 V -> L (in Ref. 2).
SQ SEQUENCE 404 AA; 46816 MW; 87A85620AF827EC6 CRC64;
MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH TKTTLPTFQS
PEFSVTRQHE DFVWLHDTLI ETTDYAGLII PPAPTKPDFD GPREKMQKLG EGEGSMTKEE
FAKMKQELEA EYLAVFKKTV SSHEVFLQRL SSHPVLSKDR NFHVFLEYDQ DLSVRRKNTK
EMFGGFFKSV VKSADEVLFT GVKEVDDFFE QEKNFLINYY NRIKDSCVKA DKMTRSHKNV
ADDYIHTAAC LHSLALEEPT VIKKYLLKVA ELFEKLRKVE GRVSSDEDLK LTELLRYYML
NIEAAKDLLY RRTKALIDYE NSNKALDKAR LKSKDVKLAE AHQQECCQKF EQLSESAKEE
LINFKRKRVA AFRKNLIEMS ELEIKHARNN VSLLQSCIDL FKNN
//
ID SNX5_HUMAN Reviewed; 404 AA.
AC Q9Y5X3; B7ZKN3; D3DW26; Q52LC4; Q9BWP0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Sorting nexin-5;
GN Name=SNX5;
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], AND SUBCELLULAR LOCATION.
RX PubMed=11485546; DOI=10.1042/0264-6021:3580007;
RA Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.;
RT "A large family of endosome-localized proteins related to sorting
RT nexin 1.";
RL Biochem. J. 358:7-16(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovarian carcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [6]
RP SUBCELLULAR LOCATION, AND PHOSPHATIDYLINOSITOL 3,4-BISPHOSPHATE
RP BINDING.
RX PubMed=15561769; DOI=10.1242/jcs.01561;
RA Merino-Trigo A., Kerr M.C., Houghton F., Lindberg A., Mitchell C.,
RA Teasdale R.D., Gleeson P.A.;
RT "Sorting nexin 5 is localized to a subdomain of the early endosomes
RT and is recruited to the plasma membrane following EGF stimulation.";
RL J. Cell Sci. 117:6413-6424(2004).
RN [7]
RP INTERACTION WITH SNX1, AND SUBCELLULAR LOCATION.
RX PubMed=16968745; DOI=10.1242/jcs.03167;
RA Kerr M.C., Lindsay M.R., Luetterforst R., Hamilton N., Simpson F.,
RA Parton R.G., Gleeson P.A., Teasdale R.D.;
RT "Visualisation of macropinosome maturation by the recruitment of
RT sorting nexins.";
RL J. Cell Sci. 119:3967-3980(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18854019; DOI=10.1186/1471-2121-9-58;
RA Lim J.P., Wang J.T., Kerr M.C., Teasdale R.D., Gleeson P.A.;
RT "A role for SNX5 in the regulation of macropinocytosis.";
RL BMC Cell Biol. 9:58-58(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21048941; DOI=10.1371/journal.pone.0013763;
RA Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S.,
RA Teasdale R.D.;
RT "The SNX-PX-BAR family in macropinocytosis: the regulation of
RT macropinosome formation by SNX-PX-BAR proteins.";
RL PLoS ONE 5:E13763-E13763(2010).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 257-265 IN COMPLEX WITH HLA
RP CLASS I HISTOCOMPATIBILITY COMPLEX.
RX PubMed=15226359; DOI=10.1084/jem.20031680;
RA Zernich D., Purcell A.W., Macdonald W.A., Kjer-Nielsen L., Ely L.K.,
RA Laham N., Crockford T., Mifsud N.A., Bharadwaj M., Chang L.,
RA Tait B.D., Holdsworth R., Brooks A.G., Bottomley S.P., Beddoe T.,
RA Peh C.A., Rossjohn J., McCluskey J.;
RT "Natural HLA class I polymorphism controls the pathway of antigen
RT presentation and susceptibility to viral evasion.";
RL J. Exp. Med. 200:13-24(2004).
CC -!- FUNCTION: May be involved in several stages of intracellular
CC trafficking. Plays a role in macropinocytosis. Plays a role in the
CC internalization of EGFR after EGF stimulation.
CC -!- SUBUNIT: Interacts with SNX1; this promotes location at the
CC endosome membrane.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasmic vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell
CC projection, phagocytic cup. Cell projection, ruffle.
CC Note=Recruited to the plasma membrane after EGF stimulation, which
CC leads to increased levels of phosphatidylinositol 3,4-bisphosphate
CC (PdtIns(3,4)P2). Detected on macropinosomes. Targeted to membrane
CC ruffles in response to EGFR stimulation.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched
CC in phosphatidylinositol 3,4-bisphosphate and/or
CC phosphatidylinositol 4,5-bisphosphate (By similarity).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC -!- CAUTION: The selectivity for particular phosphatidylinositol
CC lipids is under debate. According to one report (PubMed:19553671),
CC the rat protein binds exclusively to phosphatidylinositol 4,5-
CC bisphosphate, while the human protein has been reported
CC (PubMed:15561769) to bind to phosphatidylinositol 3,4-bisphosphate
CC and also to phosphatidylinositol 3-phosphate.
CC -----------------------------------------------------------------------
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DR EMBL; AF121855; AAD27828.1; -; mRNA.
DR EMBL; AK001793; BAA91914.1; -; mRNA.
DR EMBL; AL121585; CAC00471.1; -; Genomic_DNA.
DR EMBL; BC000100; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471133; EAX10264.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10265.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10266.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10268.1; -; Genomic_DNA.
DR EMBL; BC093623; AAH93623.1; -; mRNA.
DR EMBL; BC093980; AAH93980.1; -; mRNA.
DR EMBL; BC143274; AAI43275.1; -; mRNA.
DR RefSeq; NP_055241.1; NM_014426.3.
DR RefSeq; NP_689413.1; NM_152227.2.
DR UniGene; Hs.316890; -.
DR PDB; 1SYS; X-ray; 2.40 A; C=257-265.
DR PDBsum; 1SYS; -.
DR ProteinModelPortal; Q9Y5X3; -.
DR SMR; Q9Y5X3; 20-174.
DR IntAct; Q9Y5X3; 17.
DR MINT; MINT-2823978; -.
DR STRING; 9606.ENSP00000366988; -.
DR PhosphoSite; Q9Y5X3; -.
DR DMDM; 10720289; -.
DR PaxDb; Q9Y5X3; -.
DR PRIDE; Q9Y5X3; -.
DR DNASU; 27131; -.
DR Ensembl; ENST00000377759; ENSP00000366988; ENSG00000089006.
DR Ensembl; ENST00000377768; ENSP00000366998; ENSG00000089006.
DR GeneID; 27131; -.
DR KEGG; hsa:27131; -.
DR UCSC; uc002wqc.3; human.
DR CTD; 27131; -.
DR GeneCards; GC20M017870; -.
DR HGNC; HGNC:14969; SNX5.
DR HPA; CAB020679; -.
DR MIM; 605937; gene.
DR neXtProt; NX_Q9Y5X3; -.
DR PharmGKB; PA37945; -.
DR eggNOG; NOG255198; -.
DR HOVERGEN; HBG000716; -.
DR InParanoid; Q9Y5X3; -.
DR OMA; IKDSCAK; -.
DR OrthoDB; EOG7X0VH4; -.
DR PhylomeDB; Q9Y5X3; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; SNX5; human.
DR EvolutionaryTrace; Q9Y5X3; -.
DR GeneWiki; SNX5; -.
DR GenomeRNAi; 27131; -.
DR NextBio; 49854; -.
DR PRO; PR:Q9Y5X3; -.
DR ArrayExpress; Q9Y5X3; -.
DR Bgee; Q9Y5X3; -.
DR CleanEx; HS_SNX5; -.
DR Genevestigator; Q9Y5X3; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic to cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0031313; C:extrinsic to endosome membrane; IDA:UniProtKB.
DR GO; GO:0070685; C:macropinocytic cup; IDA:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006907; P:pinocytosis; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; Phox.
DR InterPro; IPR014637; SNX5/SNX6/SNX32.
DR InterPro; IPR015404; Vps5_C.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 1.
DR PIRSF; PIRSF036924; Snx5_Snx6; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS51021; BAR; FALSE_NEG.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cell projection;
KW Complete proteome; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
KW Endosome; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 404 Sorting nexin-5.
FT /FTId=PRO_0000213844.
FT DOMAIN 25 172 PX.
FT DOMAIN 202 404 BAR.
FT REGION 40 46 Phosphatidylinositol bisphosphate binding
FT (By similarity).
FT REGION 99 105 Phosphatidylinositol bisphosphate binding
FT (By similarity).
FT REGION 113 116 Phosphatidylinositol bisphosphate binding
FT (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 275 275 N6-acetyllysine.
FT CONFLICT 279 279 V -> L (in Ref. 2).
SQ SEQUENCE 404 AA; 46816 MW; 87A85620AF827EC6 CRC64;
MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH TKTTLPTFQS
PEFSVTRQHE DFVWLHDTLI ETTDYAGLII PPAPTKPDFD GPREKMQKLG EGEGSMTKEE
FAKMKQELEA EYLAVFKKTV SSHEVFLQRL SSHPVLSKDR NFHVFLEYDQ DLSVRRKNTK
EMFGGFFKSV VKSADEVLFT GVKEVDDFFE QEKNFLINYY NRIKDSCVKA DKMTRSHKNV
ADDYIHTAAC LHSLALEEPT VIKKYLLKVA ELFEKLRKVE GRVSSDEDLK LTELLRYYML
NIEAAKDLLY RRTKALIDYE NSNKALDKAR LKSKDVKLAE AHQQECCQKF EQLSESAKEE
LINFKRKRVA AFRKNLIEMS ELEIKHARNN VSLLQSCIDL FKNN
//
MIM
605937
*RECORD*
*FIELD* NO
605937
*FIELD* TI
*605937 SORTING NEXIN 5; SNX5
*FIELD* TX
DESCRIPTION
SNX5 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 (Otsuki et al., 1999).
CLONING
Using a yeast 2-hybrid screen with a fragment of FANCA (607139) as bait,
Otsuki et al. (1999) identified SNX5 as a putative FANCA-binding
protein. Northern blot analysis detected 2 SNX5 transcripts of 2.2 and
1.6 kb, which were present in varying amounts among the tissues and cell
lines tested. The highest levels were found in skeletal muscle and
kidney as well as in a T-cell leukemia, a colon adenocarcinoma, and a
lung carcinoma cell line, and the lowest levels were found in brain,
placenta, lung, and liver.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SNX5
gene to chromosome 20 (TMAP stSG9992).
GENE FUNCTION
Otsuki et al. (1999) confirmed the interaction between FANCA and SNX5 by
immunoprecipitation studies. Deletion mutant analysis indicated that the
PX domain is not required for binding to FANCA, but that a central
region of SNX5 is essential. Otsuki et al. (1999) found that
overexpression of SNX5 increased FANCA protein levels, leading them to
suggest that FANCA may affect SNX5 traffic with cell surface receptors.
The cell surface receptor CED1 (107770) mediates apoptotic cell
recognition by phagocytic cells, enabling cell corpse clearance in C.
elegans. Chen et al. (2010) found that the C. elegans intracellular
protein sorting complex, retromer, was required for cell corpse
clearance by mediating the recycling of CED1. The mammalian retromer
complex contains sorting nexins 1 and 2 (601272, 605929) (C. elegans
homolog snx1) and 5 and 6 (606098) (C. elegans homolog snx6). Retromer
was recruited to the surfaces of phagosomes containing cell corpses, and
its loss of function caused defective cell corpse removal. The retromer
probably acted through direct interaction with CED1 in the cell corpse
recognition pathway. In the absence of retromer function, CED1
associated with lysosomes and failed to recycle from phagosomes and
cytosol to the plasma membrane. Thus, Chen et al. (2010) concluded that
retromer is an essential mediator of apoptotic cell clearance by
regulating phagocytic receptor(s) during cell corpse engulfment.
*FIELD* RF
1. Chen, D.; Xiao, H.; Zhang, K.; Wang, B.; Gao, Z.; Jian, Y.; Qi,
X.; Sun, J.; Miao, L.; Yang, C.: Retromer is required for apoptotic
cell clearance by phagocytic receptor recycling. Science 327: 1261-1264,
2010.
2. Otsuki, T.; Kajigaya, S.; Ozawa, K.; Liu, J. M.: SNX5, a new member
of the sorting nexin family, binds to the Fanconi anemia complementation
group A protein. Biochem. Biophys. Res. Commun. 265: 630-635, 1999.
*FIELD* CN
Ada Hamosh - updated: 4/22/2010
*FIELD* CD
Carol A. Bocchini: 5/15/2001
*FIELD* ED
alopez: 04/26/2010
terry: 4/22/2010
carol: 10/19/2009
ckniffin: 1/24/2003
carol: 5/15/2001
*RECORD*
*FIELD* NO
605937
*FIELD* TI
*605937 SORTING NEXIN 5; SNX5
*FIELD* TX
DESCRIPTION
SNX5 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 (Otsuki et al., 1999).
CLONING
Using a yeast 2-hybrid screen with a fragment of FANCA (607139) as bait,
Otsuki et al. (1999) identified SNX5 as a putative FANCA-binding
protein. Northern blot analysis detected 2 SNX5 transcripts of 2.2 and
1.6 kb, which were present in varying amounts among the tissues and cell
lines tested. The highest levels were found in skeletal muscle and
kidney as well as in a T-cell leukemia, a colon adenocarcinoma, and a
lung carcinoma cell line, and the lowest levels were found in brain,
placenta, lung, and liver.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SNX5
gene to chromosome 20 (TMAP stSG9992).
GENE FUNCTION
Otsuki et al. (1999) confirmed the interaction between FANCA and SNX5 by
immunoprecipitation studies. Deletion mutant analysis indicated that the
PX domain is not required for binding to FANCA, but that a central
region of SNX5 is essential. Otsuki et al. (1999) found that
overexpression of SNX5 increased FANCA protein levels, leading them to
suggest that FANCA may affect SNX5 traffic with cell surface receptors.
The cell surface receptor CED1 (107770) mediates apoptotic cell
recognition by phagocytic cells, enabling cell corpse clearance in C.
elegans. Chen et al. (2010) found that the C. elegans intracellular
protein sorting complex, retromer, was required for cell corpse
clearance by mediating the recycling of CED1. The mammalian retromer
complex contains sorting nexins 1 and 2 (601272, 605929) (C. elegans
homolog snx1) and 5 and 6 (606098) (C. elegans homolog snx6). Retromer
was recruited to the surfaces of phagosomes containing cell corpses, and
its loss of function caused defective cell corpse removal. The retromer
probably acted through direct interaction with CED1 in the cell corpse
recognition pathway. In the absence of retromer function, CED1
associated with lysosomes and failed to recycle from phagosomes and
cytosol to the plasma membrane. Thus, Chen et al. (2010) concluded that
retromer is an essential mediator of apoptotic cell clearance by
regulating phagocytic receptor(s) during cell corpse engulfment.
*FIELD* RF
1. Chen, D.; Xiao, H.; Zhang, K.; Wang, B.; Gao, Z.; Jian, Y.; Qi,
X.; Sun, J.; Miao, L.; Yang, C.: Retromer is required for apoptotic
cell clearance by phagocytic receptor recycling. Science 327: 1261-1264,
2010.
2. Otsuki, T.; Kajigaya, S.; Ozawa, K.; Liu, J. M.: SNX5, a new member
of the sorting nexin family, binds to the Fanconi anemia complementation
group A protein. Biochem. Biophys. Res. Commun. 265: 630-635, 1999.
*FIELD* CN
Ada Hamosh - updated: 4/22/2010
*FIELD* CD
Carol A. Bocchini: 5/15/2001
*FIELD* ED
alopez: 04/26/2010
terry: 4/22/2010
carol: 10/19/2009
ckniffin: 1/24/2003
carol: 5/15/2001