SNX27_HUMAN
ID SNX27_HUMAN Reviewed; 541 AA.
AC Q96L92; Q32Q36; Q4AEJ5; Q5VWB0; Q5VWB1; Q5VWB2; Q6IPP6; Q86UB1; Q96D79;
AC Q9H3K8;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Sorting nexin-27;
GN Name=SNX27; Synonyms=KIAA0488; ORFNames=My014;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=15466885; DOI=10.1242/jcs.01379;
RA Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA Marin P., Dumuis A., Bockaert J.;
RT "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a
RT receptor splice variant: roles in receptor targeting.";
RL J. Cell Sci. 117:5367-5379(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 175-541 (ISOFORM 1).
RC TISSUE=Eye, Lung, Placenta, and Uterus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-528 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-528 (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Lin Q., Li Y., Dai J.L., Ying K.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17644068; DOI=10.1016/j.bbrc.2007.06.183;
RA MacNeil A.J., Pohajdak B.;
RT "Polarization of endosomal SNX27 in migrating and tumor-engaged natural
RT killer cells.";
RL Biochem. Biophys. Res. Commun. 361:146-150(2007).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH CYTIP.
RX PubMed=17577583; DOI=10.1016/j.bbrc.2007.05.162;
RA MacNeil A.J., Mansour M., Pohajdak B.;
RT "Sorting nexin 27 interacts with the Cytohesin associated scaffolding
RT protein (CASP) in lymphocytes.";
RL Biochem. Biophys. Res. Commun. 359:848-853(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP DGKZ.
RX PubMed=17351151; DOI=10.1074/mcp.m700047-mcp200;
RA Rincon E., Santos T., Avila-Flores A., Albar J.P., Lalioti V., Lei C.,
RA Hong W., Merida I.;
RT "Proteomics identification of sorting nexin 27 as a diacylglycerol kinase
RT zeta-associated protein: new diacylglycerol kinase roles in endocytic
RT recycling.";
RL Mol. Cell. Proteomics 6:1073-1087(2007).
RN [9]
RP INTERACTION WITH MCC.
RX PubMed=19555689; DOI=10.1016/j.febslet.2009.06.034;
RA Arnaud C., Sebbagh M., Nola S., Audebert S., Bidaut G., Hermant A.,
RA Gayet O., Dusetti N.J., Ollendorff V., Santoni M.J., Borg J.P., Lecine P.;
RT "MCC, a new interacting protein for Scrib, is required for cell migration
RT in epithelial cells.";
RL FEBS Lett. 583:2326-2332(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ADRB2, AND MUTAGENESIS OF
RP HIS-114.
RX PubMed=20733053; DOI=10.1083/jcb.201004060;
RA Lauffer B.E., Melero C., Temkin P., Lei C., Hong W., Kortemme T.,
RA von Zastrow M.;
RT "SNX27 mediates PDZ-directed sorting from endosomes to the plasma
RT membrane.";
RL J. Cell Biol. 190:565-574(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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., Buerckstuemmer T.,
RA 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 [13]
RP FUNCTION, AND INTERACTION WITH ARHGEF7.
RX PubMed=21926430; DOI=10.1074/jbc.m111.260802;
RA Valdes J.L., Tang J., McDermott M.I., Kuo J.C., Zimmerman S.P.,
RA Wincovitch S.M., Waterman C.M., Milgram S.L., Playford M.P.;
RT "Sorting nexin 27 protein regulates trafficking of a p21-activated kinase
RT (PAK) interacting exchange factor (beta-Pix)-G protein-coupled receptor
RT kinase interacting protein (GIT) complex via a PDZ domain interaction.";
RL J. Biol. Chem. 286:39403-39416(2011).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND
RP PHOSPHATIDYLINOSITOL-3-PHOSPHATE-BINDING.
RX PubMed=21303929; DOI=10.1242/jcs.072447;
RA Rincon E., Saez de Guinoa J., Gharbi S.I., Sorzano C.O., Carrasco Y.R.,
RA Merida I.;
RT "Translocation dynamics of sorting nexin 27 in activated T cells.";
RL J. Cell Sci. 124:776-788(2011).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL-3-PHOSPHATE-BINDING,
RP TISSUE SPECIFICITY, AND INTERACTION WITH GRIN2C.
RX PubMed=21300787; DOI=10.1128/mcb.01044-10;
RA Cai L., Loo L.S., Atlashkin V., Hanson B.J., Hong W.;
RT "Deficiency of sorting nexin 27 (SNX27) leads to growth retardation and
RT elevated levels of N-methyl-D-aspartate receptor 2C (NR2C).";
RL Mol. Cell. Biol. 31:1734-1747(2011).
RN [16]
RP FUNCTION, AND INTERACTION WITH ADRB2.
RX PubMed=21602791; DOI=10.1038/ncb2252;
RA Temkin P., Lauffer B., Jager S., Cimermancic P., Krogan N.J.,
RA von Zastrow M.;
RT "SNX27 mediates retromer tubule entry and endosome-to-plasma membrane
RT trafficking of signalling receptors.";
RL Nat. Cell Biol. 13:715-721(2011).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABCC4.
RX PubMed=22411990; DOI=10.1074/jbc.m111.337931;
RA Hayashi H., Naoi S., Nakagawa T., Nishikawa T., Fukuda H., Imajoh-Ohmi S.,
RA Kondo A., Kubo K., Yabuki T., Hattori A., Hirouchi M., Sugiyama Y.;
RT "Sorting nexin 27 interacts with multidrug resistance-associated protein 4
RT (MRP4) and mediates internalization of MRP4.";
RL J. Biol. Chem. 287:15054-15065(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP FUNCTION, AND INTERACTION WITH SLC2A1; VPS26A AND SNX1.
RX PubMed=23563491; DOI=10.1038/ncb2721;
RA Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J., Heesom K.J.,
RA Tavare J.M., Cullen P.J.;
RT "A global analysis of SNX27-retromer assembly and cargo specificity reveals
RT a function in glucose and metal ion transport.";
RL Nat. Cell Biol. 15:461-471(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 156-265.
RG Structural genomics consortium (SGC);
RT "Crystal structure of PX domain of human sorting nexin SNX27.";
RL Submitted (APR-2013) to the PDB data bank.
CC -!- FUNCTION: Involved in the retrograde transport from endosome to plasma
CC membrane, a trafficking pathway that promotes the recycling of
CC internalized transmembrane proteins. Following internalization,
CC endocytosed transmembrane proteins are delivered to early endosomes and
CC recycled to the plasma membrane instead of being degraded in lysosomes.
CC SNX27 specifically binds and directs sorting of a subset of
CC transmembrane proteins containing a PDZ-binding motif at the C-
CC terminus: following interaction with target transmembrane proteins,
CC associates with the retromer complex, preventing entry into the
CC lysosomal pathway, and promotes retromer-tubule based plasma membrane
CC recycling. SNX27 also binds with the WASH complex. Interacts with
CC membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May
CC participate in establishment of natural killer cell polarity. Recruits
CC CYTIP to early endosomes. {ECO:0000269|PubMed:17351151,
CC ECO:0000269|PubMed:20733053, ECO:0000269|PubMed:21300787,
CC ECO:0000269|PubMed:21303929, ECO:0000269|PubMed:21602791,
CC ECO:0000269|PubMed:21926430, ECO:0000269|PubMed:22411990,
CC ECO:0000269|PubMed:23563491}.
CC -!- SUBUNIT: Core component of the SNX27-retromer, a multiprotein complex
CC composed of SNX27, the WASH complex and the retromer complex. Interacts
CC (via PDZ domain) with a number of target transmembrane proteins (via
CC PDZ-binding motif): ABCC4, ADRB2, ARHGEF7, GRIA1, GRIA2, GRIN1, GRIN2A
CC GRIN2C, KCNJ6, KCNJ9 and SLC2A1/GLUT1. Interacts (via the FERM-like
CC regions) with the WASH complex. Interacts with SNX1. Interacts with
CC CYTIP. Isoform 1 and isoform 2 directly interact with DGKZ. Isoform 1
CC and isoform 2 interact with HT4R isoform 5-HTA(A). Interacts with MCC.
CC {ECO:0000269|PubMed:17351151, ECO:0000269|PubMed:17577583,
CC ECO:0000269|PubMed:19555689, ECO:0000269|PubMed:20733053,
CC ECO:0000269|PubMed:21300787, ECO:0000269|PubMed:21602791,
CC ECO:0000269|PubMed:21926430, ECO:0000269|PubMed:22411990,
CC ECO:0000269|PubMed:23563491}.
CC -!- INTERACTION:
CC Q96L92; Q9BYF1: ACE2; NbExp=2; IntAct=EBI-2514865, EBI-7730807;
CC Q96L92; P0DTC2: S; Xeno; NbExp=16; IntAct=EBI-2514865, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC protein. Cytoplasm, cytosol. Note=Localizes to immunological synapse in
CC T-cells. In T-cells, recruited from the cytosol to sorting endosomes by
CC phosphoinositide-3-kinase products.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SNX27a;
CC IsoId=Q96L92-1; Sequence=Displayed;
CC Name=2; Synonyms=SNX27b;
CC IsoId=Q96L92-3; Sequence=VSP_030539;
CC Name=3;
CC IsoId=Q96L92-2; Sequence=VSP_030537, VSP_030538, VSP_030539;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in cells of
CC hematopoietic origin (at protein level). {ECO:0000269|PubMed:17351151,
CC ECO:0000269|PubMed:17577583, ECO:0000269|PubMed:21300787}.
CC -!- DOMAIN: The PDZ domain mediates binding to a subset of proteins
CC containing a PDZ-binding motif at the C-terminus: the specificity for
CC PDZ-binding motif is provided by the 2 residues located upstream of the
CC canonical PDZ-binding motif (By similarity). The PDZ domain also
CC mediates binding to the retromer complex via direct interaction with
CC VPS26 (VPS26A or VPS26B) (PubMed:23563491). {ECO:0000250,
CC ECO:0000269|PubMed:23563491}.
CC -!- DOMAIN: The PX domain mediates binding to phosphatidylinositol 3-
CC phosphate (PtdIns(3P)) and localization to early endosome membranes.
CC {ECO:0000269|PubMed:20733053}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG43127.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH12184.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY044866; AAK97797.1; -; mRNA.
DR EMBL; AL391335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012184; AAH12184.1; ALT_INIT; mRNA.
DR EMBL; BC051817; AAH51817.1; -; mRNA.
DR EMBL; BC071825; AAH71825.1; -; mRNA.
DR EMBL; BC100998; AAI00999.1; -; mRNA.
DR EMBL; BC100999; AAI01000.1; -; mRNA.
DR EMBL; BC101000; AAI01001.1; -; mRNA.
DR EMBL; BC101822; AAI01823.1; -; mRNA.
DR EMBL; BC101824; AAI01825.1; -; mRNA.
DR EMBL; BC107862; AAI07863.1; -; mRNA.
DR EMBL; AB007957; BAE16986.1; -; mRNA.
DR EMBL; AF060509; AAG43127.1; ALT_INIT; mRNA.
DR CCDS; CCDS1001.1; -. [Q96L92-3]
DR CCDS; CCDS81377.1; -. [Q96L92-1]
DR RefSeq; NP_001317652.1; NM_001330723.1. [Q96L92-1]
DR RefSeq; NP_112180.4; NM_030918.5. [Q96L92-3]
DR PDB; 4HAS; X-ray; 1.74 A; A/B=156-265.
DR PDB; 5ZN9; X-ray; 1.78 A; A/B=156-265.
DR PDB; 6SAK; X-ray; 2.00 A; C/D=40-135.
DR PDB; 7CT1; X-ray; 1.95 A; A=273-526.
DR PDB; 7E0B; X-ray; 1.29 A; A=40-135.
DR PDBsum; 4HAS; -.
DR PDBsum; 5ZN9; -.
DR PDBsum; 6SAK; -.
DR PDBsum; 7CT1; -.
DR PDBsum; 7E0B; -.
DR AlphaFoldDB; Q96L92; -.
DR SMR; Q96L92; -.
DR BioGRID; 123546; 144.
DR IntAct; Q96L92; 80.
DR MINT; Q96L92; -.
DR STRING; 9606.ENSP00000357836; -.
DR TCDB; 9.A.3.1.1; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
DR GlyGen; Q96L92; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96L92; -.
DR PhosphoSitePlus; Q96L92; -.
DR BioMuta; SNX27; -.
DR DMDM; 166214988; -.
DR EPD; Q96L92; -.
DR jPOST; Q96L92; -.
DR MassIVE; Q96L92; -.
DR MaxQB; Q96L92; -.
DR PaxDb; Q96L92; -.
DR PeptideAtlas; Q96L92; -.
DR PRIDE; Q96L92; -.
DR ProteomicsDB; 77161; -. [Q96L92-1]
DR ProteomicsDB; 77162; -. [Q96L92-2]
DR ProteomicsDB; 77163; -. [Q96L92-3]
DR Antibodypedia; 46991; 290 antibodies from 25 providers.
DR DNASU; 81609; -.
DR Ensembl; ENST00000368843.8; ENSP00000357836.3; ENSG00000143376.14. [Q96L92-3]
DR Ensembl; ENST00000458013.7; ENSP00000400333.2; ENSG00000143376.14. [Q96L92-1]
DR GeneID; 81609; -.
DR KEGG; hsa:81609; -.
DR MANE-Select; ENST00000458013.7; ENSP00000400333.2; NM_001330723.2; NP_001317652.1.
DR UCSC; uc001eyn.2; human. [Q96L92-1]
DR CTD; 81609; -.
DR DisGeNET; 81609; -.
DR GeneCards; SNX27; -.
DR HGNC; HGNC:20073; SNX27.
DR HPA; ENSG00000143376; Low tissue specificity.
DR MalaCards; SNX27; -.
DR MIM; 611541; gene.
DR neXtProt; NX_Q96L92; -.
DR OpenTargets; ENSG00000143376; -.
DR PharmGKB; PA134969143; -.
DR VEuPathDB; HostDB:ENSG00000143376; -.
DR eggNOG; KOG3784; Eukaryota.
DR GeneTree; ENSGT00950000183212; -.
DR HOGENOM; CLU_028138_0_0_1; -.
DR InParanoid; Q96L92; -.
DR OMA; NCSKDNM; -.
DR OrthoDB; 395943at2759; -.
DR PhylomeDB; Q96L92; -.
DR TreeFam; TF318398; -.
DR PathwayCommons; Q96L92; -.
DR SignaLink; Q96L92; -.
DR BioGRID-ORCS; 81609; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; SNX27; human.
DR GeneWiki; SNX27; -.
DR GenomeRNAi; 81609; -.
DR Pharos; Q96L92; Tbio.
DR PRO; PR:Q96L92; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96L92; protein.
DR Bgee; ENSG00000143376; Expressed in medial globus pallidus and 213 other tissues.
DR ExpressionAtlas; Q96L92; baseline and differential.
DR Genevisible; Q96L92; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IC:ParkinsonsUK-UCL.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:0001770; P:establishment of natural killer cell polarity; TAS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13338; FERM-like_C_SNX27; 1.
DR CDD; cd01777; FERM_F1_SNX27; 1.
DR CDD; cd06886; PX_SNX27; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR037831; SNX17/27/31.
DR InterPro; IPR028667; SNX27.
DR InterPro; IPR037827; SNX27_FERM-like_dom.
DR InterPro; IPR037833; SNX27_PX.
DR InterPro; IPR037835; SNX27_RA.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12431; PTHR12431; 1.
DR PANTHER; PTHR12431:SF17; PTHR12431:SF17; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Endosome; Lipid-binding;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..541
FT /note="Sorting nexin-27"
FT /id="PRO_0000315356"
FT DOMAIN 43..136
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 161..269
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 273..362
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..362
FT /note="FERM-like region F1"
FT REGION 373..421
FT /note="FERM-like region F2"
FT REGION 425..525
FT /note="FERM-like region F3"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15466885"
FT /id="VSP_030537"
FT VAR_SEQ 94..104
FT /note="GVRKGDRILEV -> MGLSFSLFPLR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15466885"
FT /id="VSP_030538"
FT VAR_SEQ 527..541
FT /note="NIFQMARSQQRDVAT -> EY (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15466885,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9455484,
FT ECO:0000303|Ref.5"
FT /id="VSP_030539"
FT VARIANT 459
FT /note="E -> K (in dbSNP:rs11204871)"
FT /id="VAR_059851"
FT MUTAGEN 114
FT /note="H->A: Abolishes interaction with ADRB2, sorting and
FT recycling of ADRB2."
FT /evidence="ECO:0000269|PubMed:20733053"
FT CONFLICT 467
FT /note="I -> V (in Ref. 3; AAI07863)"
FT /evidence="ECO:0000305"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:6SAK"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:6SAK"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6SAK"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6SAK"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:6SAK"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:6SAK"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6SAK"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:6SAK"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:6SAK"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:4HAS"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:4HAS"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4HAS"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:4HAS"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:4HAS"
FT HELIX 229..246
FT /evidence="ECO:0007829|PDB:4HAS"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:4HAS"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:4HAS"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:7CT1"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:7CT1"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 374..389
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 411..418
FT /evidence="ECO:0007829|PDB:7CT1"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 462..469
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:7CT1"
FT TURN 481..484
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:7CT1"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:7CT1"
FT HELIX 507..526
FT /evidence="ECO:0007829|PDB:7CT1"
SQ SEQUENCE 541 AA; 61265 MW; 1AA2265E463CB8DA CRC64;
MADEDGEGIH PSAPHRNGGG GGGGGSGLHC AGNGGGGGGG PRVVRIVKSE SGYGFNVRGQ
VSEGGQLRSI NGELYAPLQH VSAVLPGGAA DRAGVRKGDR ILEVNHVNVE GATHKQVVDL
IRAGEKELIL TVLSVPPHEA DNLDPSDDSL GQSFYDYTEK QAVPISVPRY KHVEQNGEKF
VVYNVYMAGR QLCSKRYREF AILHQNLKRE FANFTFPRLP GKWPFSLSEQ QLDARRRGLE
EYLEKVCSIR VIGESDIMQE FLSESDENYN GVSDVELRVA LPDGTTVTVR VKKNSTTDQV
YQAIAAKVGM DSTTVNYFAL FEVISHSFVR KLAPNEFPHK LYIQNYTSAV PGTCLTIRKW
LFTTEEEILL NDNDLAVTYF FHQAVDDVKK GYIKAEEKSY QLQKLYEQRK MVMYLNMLRT
CEGYNEIIFP HCACDSRRKG HVITAISITH FKLHACTEEG QLENQVIAFE WDEMQRWDTD
EEGMAFCFEY ARGEKKPRWV KIFTPYFNYM HECFERVFCE LKWRKENIFQ MARSQQRDVA
T
