SNX4_HUMAN
ID SNX4_HUMAN Reviewed; 450 AA.
AC O95219; B3KMH0; B4DQV4; D3DNA3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Sorting nexin-4 {ECO:0000303|PubMed:9819414};
GN Name=SNX4 {ECO:0000303|PubMed:9819414, ECO:0000312|HGNC:HGNC:11175};
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 1), AND FUNCTION.
RX PubMed=9819414; DOI=10.1128/mcb.18.12.7278;
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 characterization
RT of their association with receptors.";
RL Mol. Cell. Biol. 18:7278-7287(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BIN1.
RX PubMed=12668730; DOI=10.1242/jcs.00403;
RA Leprince C., Le Scolan E., Meunier B., Fraisier V., Brandon N.,
RA De Gunzburg J., Camonis J.;
RT "Sorting nexin 4 and amphiphysin 2, a new partnership between endocytosis
RT and intracellular trafficking.";
RL J. Cell Sci. 116:1937-1948(2003).
RN [7]
RP FUNCTION, INTERACTION WITH WWC1/KIBRA, MUTAGENESIS OF LYS-132, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17994011; DOI=10.1038/ncb1656;
RA Traer C.J., Rutherford A.C., Palmer K.J., Wassmer T., Oakley J., Attar N.,
RA Carlton J.G., Kremerskothen J., Stephens D.J., Cullen P.J.;
RT "SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport
RT into the endocytic recycling compartment.";
RL Nat. Cell Biol. 9:1370-1380(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SNX7 AND SNX30.
RX PubMed=32513819; DOI=10.1242/jcs.246306;
RA Anton Z., Betin V.M.S., Simonetti B., Traer C.J., Attar N., Cullen P.J.,
RA Lane J.D.;
RT "A heterodimeric SNX4--SNX7 SNX-BAR autophagy complex coordinates ATG9A
RT trafficking for efficient autophagosome assembly.";
RL J. Cell Sci. 133:0-0(2020).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=33468622; DOI=10.1242/jcs.250670;
RA Ravussin A., Brech A., Tooze S.A., Stenmark H.;
RT "The phosphatidylinositol 3-phosphate-binding protein SNX4 controls ATG9A
RT recycling and autophagy.";
RL J. Cell Sci. 134:0-0(2021).
CC -!- FUNCTION: Involved in the regulation of endocytosis and in several
CC stages of intracellular trafficking (PubMed:12668730, PubMed:17994011,
CC PubMed:32513819, PubMed:33468622). Plays a role in recycling
CC endocytosed transferrin receptor and prevent its degradation
CC (PubMed:17994011). Involved in autophagosome assembly by regulating
CC trafficking and recycling of phospholipid scramblase ATG9A
CC (PubMed:32513819, PubMed:33468622). {ECO:0000269|PubMed:12668730,
CC ECO:0000269|PubMed:17994011, ECO:0000269|PubMed:32513819,
CC ECO:0000269|PubMed:33468622}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with SNX7 or SNX30
CC (PubMed:32513819). Interacts with WWC1/KIBRA (PubMed:17994011).
CC Identified in a complex with WWC1/KIBRA and dynein components DYNLL1
CC and DYNC1I2 (PubMed:17994011). Interacts with BIN1 (PubMed:12668730).
CC {ECO:0000269|PubMed:12668730, ECO:0000269|PubMed:17994011,
CC ECO:0000269|PubMed:32513819}.
CC -!- INTERACTION:
CC O95219; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-724909, EBI-714543;
CC O95219; O00499: BIN1; NbExp=4; IntAct=EBI-724909, EBI-719094;
CC O95219; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-724909, EBI-12831978;
CC O95219; P43360: MAGEA6; NbExp=3; IntAct=EBI-724909, EBI-1045155;
CC O95219; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-724909, EBI-2623095;
CC O95219; Q5VWJ9: SNX30; NbExp=3; IntAct=EBI-724909, EBI-8099676;
CC O95219; Q9UNH6: SNX7; NbExp=2; IntAct=EBI-724909, EBI-751422;
CC O95219; Q9UNH6-3: SNX7; NbExp=4; IntAct=EBI-724909, EBI-12424584;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:17994011, ECO:0000269|PubMed:32513819,
CC ECO:0000269|PubMed:33468622}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17994011}; Cytoplasmic side
CC {ECO:0000269|PubMed:17994011}. Note=Also detected on a juxtanuclear
CC endocytic recycling compartment (ERC). {ECO:0000269|PubMed:17994011}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95219-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95219-2; Sequence=VSP_056665;
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization.
CC {ECO:0000250|UniProtKB:Q96L94}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF065485; AAC83149.1; -; mRNA.
DR EMBL; AK001835; BAG50982.1; -; mRNA.
DR EMBL; AK298972; BAG61066.1; -; mRNA.
DR EMBL; AC080096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79390.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79391.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79393.1; -; Genomic_DNA.
DR EMBL; BC018762; AAH18762.1; -; mRNA.
DR CCDS; CCDS3032.1; -. [O95219-1]
DR RefSeq; NP_003785.1; NM_003794.3. [O95219-1]
DR AlphaFoldDB; O95219; -.
DR SMR; O95219; -.
DR BioGRID; 114262; 49.
DR CORUM; O95219; -.
DR DIP; DIP-36719N; -.
DR IntAct; O95219; 34.
DR MINT; O95219; -.
DR STRING; 9606.ENSP00000251775; -.
DR iPTMnet; O95219; -.
DR MetOSite; O95219; -.
DR PhosphoSitePlus; O95219; -.
DR BioMuta; SNX4; -.
DR DOSAC-COBS-2DPAGE; O95219; -.
DR EPD; O95219; -.
DR jPOST; O95219; -.
DR MassIVE; O95219; -.
DR MaxQB; O95219; -.
DR PaxDb; O95219; -.
DR PeptideAtlas; O95219; -.
DR PRIDE; O95219; -.
DR ProteomicsDB; 4904; -.
DR ProteomicsDB; 50724; -. [O95219-1]
DR Antibodypedia; 1370; 272 antibodies from 32 providers.
DR DNASU; 8723; -.
DR Ensembl; ENST00000251775.9; ENSP00000251775.4; ENSG00000114520.11. [O95219-1]
DR GeneID; 8723; -.
DR KEGG; hsa:8723; -.
DR MANE-Select; ENST00000251775.9; ENSP00000251775.4; NM_003794.4; NP_003785.1.
DR UCSC; uc003eib.5; human. [O95219-1]
DR CTD; 8723; -.
DR GeneCards; SNX4; -.
DR HGNC; HGNC:11175; SNX4.
DR HPA; ENSG00000114520; Low tissue specificity.
DR MIM; 605931; gene.
DR neXtProt; NX_O95219; -.
DR OpenTargets; ENSG00000114520; -.
DR PharmGKB; PA36014; -.
DR VEuPathDB; HostDB:ENSG00000114520; -.
DR eggNOG; KOG2273; Eukaryota.
DR GeneTree; ENSGT00930000151029; -.
DR HOGENOM; CLU_057138_0_0_1; -.
DR InParanoid; O95219; -.
DR OMA; QKSGHYL; -.
DR OrthoDB; 632390at2759; -.
DR PhylomeDB; O95219; -.
DR TreeFam; TF328543; -.
DR PathwayCommons; O95219; -.
DR SignaLink; O95219; -.
DR BioGRID-ORCS; 8723; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; SNX4; human.
DR GeneWiki; SNX4; -.
DR GenomeRNAi; 8723; -.
DR Pharos; O95219; Tbio.
DR PRO; PR:O95219; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O95219; protein.
DR Bgee; ENSG00000114520; Expressed in secondary oocyte and 211 other tissues.
DR ExpressionAtlas; O95219; baseline and differential.
DR Genevisible; O95219; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:UniProtKB.
DR GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
DR GO; GO:1990460; F:leptin receptor binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IMP:UniProtKB.
DR GO; GO:1990459; F:transferrin receptor binding; IDA:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR CDD; cd07622; BAR_SNX4; 1.
DR CDD; cd06864; PX_SNX4; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR034902; PX_SNX4.
DR InterPro; IPR034783; SNX4.
DR InterPro; IPR037430; SNX4_BAR.
DR PANTHER; PTHR46596; PTHR46596; 1.
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 Acetylation; Alternative splicing; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..450
FT /note="Sorting nexin-4"
FT /id="PRO_0000213842"
FT DOMAIN 61..187
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q3UR97"
FT BINDING 108
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q96L94"
FT BINDING 132
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q96L94"
FT BINDING 154
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T1"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..145
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056665"
FT MUTAGEN 132
FT /note="K->A: Abolishes phosphatidylinositol phosphate
FT binding. Abolishes endosomal location."
FT /evidence="ECO:0000269|PubMed:17994011"
SQ SEQUENCE 450 AA; 51909 MW; 3D5B52AC52A07686 CRC64;
MEQAPPDPER QLQPAPLEPL GSPDAGLGAA VGKEAEGAGE ESSGVDTMTH NNFWLKKIEI
SVSEAEKRTG RNAMNMQETY TAYLIETRSV EHTDGQSVLT DSLWRRYSEF ELLRSYLLVY
YPHIVVPPLP EKRAEFVWHK LSADNMDPDF VERRRIGLEN FLLRIASHPI LCRDKIFYLF
LTQEGNWKET VNETGFQLKA DSRLKALNAT FRVKNPDKRF TDLKHYSDEL QSVISHLLRV
RARVADRLYG VYKVHGNYGR VFSEWSAIEK EMGDGLQSAG HHMDVYASSI DDILEDEEHY
ADQLKEYLFY AEALRAVCRK HELMQYDLEM AAQDLASKKQ QCEELVTGTV RTFSLKGMTT
KLFGQETPEQ REARIKVLEE QINEGEQQLK SKNLEGREFV KNAWADIERF KEQKNRDLKE
ALISYAVMQI SMCKKGIQVW TNAKECFSKM
