ZFY16_HUMAN
ID ZFY16_HUMAN Reviewed; 1539 AA.
AC Q7Z3T8; O15023; Q5H9U2; Q7LAU7; Q86T69; Q8N5L3; Q8NEK3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Zinc finger FYVE domain-containing protein 16;
DE AltName: Full=Endofin;
DE AltName: Full=Endosome-associated FYVE domain protein;
GN Name=ZFYVE16; Synonyms=KIAA0305;
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), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DOMAIN, MUTAGENESIS OF CYS-753, AND VARIANTS THR-192;
RP THR-598 AND GLY-1055.
RX PubMed=11546807; DOI=10.1074/jbc.m105917200;
RA Seet L.-F., Hong W.;
RT "Endofin, an endosomal FYVE domain protein.";
RL J. Biol. Chem. 276:42445-42454(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS THR-192;
RP THR-598 AND GLY-1055.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS THR-192;
RP THR-598 AND GLY-1055.
RC TISSUE=Cervix, Spinal cord, and Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS THR-192
RP AND THR-598.
RC TISSUE=Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939 AND SER-946, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH TOM1.
RX PubMed=14613930; DOI=10.1074/jbc.m311228200;
RA Seet L.-F., Liu N., Hanson B.J., Hong W.;
RT "Endofin recruits TOM1 to endosomes.";
RL J. Biol. Chem. 279:4670-4679(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446; SER-815; SER-845;
RP SER-939 AND SER-946, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939 AND SER-946, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939 AND SER-946, AND
RP IDENTIFICATION BY 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 [14]
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 [15]
RP X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) OF 733-820 IN COMPLEX WITH ZINC.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the FYVE domain of endofin (ZFYVE16) at 1.1A
RT resolution.";
RL Submitted (AUG-2011) to the PDB data bank.
RN [16]
RP VARIANT VAL-380.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: May be involved in regulating membrane trafficking in the
CC endosomal pathway. Overexpression induces endosome aggregation.
CC Required to target TOM1 to endosomes. {ECO:0000269|PubMed:11546807,
CC ECO:0000269|PubMed:14613930}.
CC -!- SUBUNIT: Interacts with the C-terminus of TOM1. Does not interact with
CC TOM1L1 or TOM1L2. {ECO:0000269|PubMed:14613930, ECO:0000269|Ref.15}.
CC -!- INTERACTION:
CC Q7Z3T8; Q15075: EEA1; NbExp=4; IntAct=EBI-298055, EBI-298113;
CC Q7Z3T8; O60784: TOM1; NbExp=5; IntAct=EBI-298055, EBI-74634;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11546807}. Early
CC endosome membrane {ECO:0000269|PubMed:11546807}; Peripheral membrane
CC protein {ECO:0000269|PubMed:11546807}. Note=Localized to early
CC endosomes. Membrane-associated, probably via its association with
CC phosphatidylinositol 3-phosphate (PI3P).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z3T8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z3T8-3; Sequence=VSP_011019, VSP_011020;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney,
CC placenta and lung. Expressed at intermediate level in heart, brain,
CC skeletal muscle, spleen and liver. Weakly expressed in colon, thymus
CC and peripheral blood lymphocytes. {ECO:0000269|PubMed:11546807}.
CC -!- DOMAIN: The FYVE-type zinc finger is necessary and sufficient for its
CC localization into early endosomes and mediates the association with
CC PI3P. {ECO:0000269|PubMed:11546807}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20764.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF434817; AAL30772.1; -; mRNA.
DR EMBL; AB002303; BAA20764.2; ALT_INIT; mRNA.
DR EMBL; AL833087; CAD89968.1; -; mRNA.
DR EMBL; BX537424; CAD97666.1; -; mRNA.
DR EMBL; CR933621; CAI45932.1; -; mRNA.
DR EMBL; AC008771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030808; AAH30808.1; -; mRNA.
DR CCDS; CCDS4050.1; -. [Q7Z3T8-1]
DR RefSeq; NP_001271166.1; NM_001284237.1.
DR RefSeq; XP_005248689.1; XM_005248632.4. [Q7Z3T8-1]
DR RefSeq; XP_011542055.1; XM_011543753.2.
DR RefSeq; XP_016865580.1; XM_017010091.1. [Q7Z3T8-1]
DR RefSeq; XP_016865581.1; XM_017010092.1. [Q7Z3T8-1]
DR PDB; 3T7L; X-ray; 1.09 A; A=733-820.
DR PDB; 5MK0; X-ray; 1.76 A; B/D=1-22.
DR PDBsum; 3T7L; -.
DR PDBsum; 5MK0; -.
DR AlphaFoldDB; Q7Z3T8; -.
DR SMR; Q7Z3T8; -.
DR BioGRID; 115111; 55.
DR IntAct; Q7Z3T8; 20.
DR MINT; Q7Z3T8; -.
DR STRING; 9606.ENSP00000337159; -.
DR TCDB; 8.A.136.1.13; the beta-arrestin (arrb) family.
DR GlyGen; Q7Z3T8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z3T8; -.
DR PhosphoSitePlus; Q7Z3T8; -.
DR BioMuta; ZFYVE16; -.
DR DMDM; 296453075; -.
DR EPD; Q7Z3T8; -.
DR jPOST; Q7Z3T8; -.
DR MassIVE; Q7Z3T8; -.
DR MaxQB; Q7Z3T8; -.
DR PaxDb; Q7Z3T8; -.
DR PeptideAtlas; Q7Z3T8; -.
DR PRIDE; Q7Z3T8; -.
DR ProteomicsDB; 69083; -. [Q7Z3T8-1]
DR ProteomicsDB; 69084; -. [Q7Z3T8-3]
DR Antibodypedia; 24618; 164 antibodies from 25 providers.
DR DNASU; 9765; -.
DR Ensembl; ENST00000338008.9; ENSP00000337159.5; ENSG00000039319.17. [Q7Z3T8-1]
DR Ensembl; ENST00000505560.5; ENSP00000426848.1; ENSG00000039319.17. [Q7Z3T8-1]
DR Ensembl; ENST00000510158.5; ENSP00000423663.1; ENSG00000039319.17. [Q7Z3T8-1]
DR GeneID; 9765; -.
DR KEGG; hsa:9765; -.
DR MANE-Select; ENST00000505560.5; ENSP00000426848.1; NM_001284236.3; NP_001271165.2.
DR UCSC; uc003kgq.6; human. [Q7Z3T8-1]
DR CTD; 9765; -.
DR DisGeNET; 9765; -.
DR GeneCards; ZFYVE16; -.
DR HGNC; HGNC:20756; ZFYVE16.
DR HPA; ENSG00000039319; Low tissue specificity.
DR MIM; 608880; gene.
DR neXtProt; NX_Q7Z3T8; -.
DR OpenTargets; ENSG00000039319; -.
DR PharmGKB; PA134873366; -.
DR VEuPathDB; HostDB:ENSG00000039319; -.
DR eggNOG; KOG1841; Eukaryota.
DR GeneTree; ENSGT00940000163574; -.
DR HOGENOM; CLU_004326_0_0_1; -.
DR InParanoid; Q7Z3T8; -.
DR OMA; ECTIVQP; -.
DR OrthoDB; 278124at2759; -.
DR PhylomeDB; Q7Z3T8; -.
DR TreeFam; TF324904; -.
DR PathwayCommons; Q7Z3T8; -.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR SignaLink; Q7Z3T8; -.
DR BioGRID-ORCS; 9765; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; ZFYVE16; human.
DR GeneWiki; ZFYVE16; -.
DR GenomeRNAi; 9765; -.
DR Pharos; Q7Z3T8; Tbio.
DR PRO; PR:Q7Z3T8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q7Z3T8; protein.
DR Bgee; ENSG00000039319; Expressed in corpus callosum and 207 other tissues.
DR ExpressionAtlas; Q7Z3T8; baseline and differential.
DR Genevisible; Q7Z3T8; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0006622; P:protein targeting to lysosome; IMP:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; TAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0016050; P:vesicle organization; NAS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR022557; DUF3480.
DR InterPro; IPR035438; SARA/endofin.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR017165; Znf_FYVE_endofin.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46319:SF1; PTHR46319:SF1; 1.
DR Pfam; PF11979; DUF3480; 1.
DR Pfam; PF01363; FYVE; 1.
DR PIRSF; PIRSF037289; SARA/endofin; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Endosome; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1539
FT /note="Zinc finger FYVE domain-containing protein 16"
FT /id="PRO_0000098716"
FT ZN_FING 747..805
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 469..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 753
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 756
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 769
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 772
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 777
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 780
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 797
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 800
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U44"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U44"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 807..809
FT /note="AQA -> GEC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011019"
FT VAR_SEQ 810..1539
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011020"
FT VARIANT 35
FT /note="A -> E (in dbSNP:rs6893297)"
FT /id="VAR_057492"
FT VARIANT 192
FT /note="I -> T (in dbSNP:rs2544600)"
FT /evidence="ECO:0000269|PubMed:11546807,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9205841"
FT /id="VAR_019489"
FT VARIANT 380
FT /note="A -> V (in dbSNP:rs752702732)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069368"
FT VARIANT 598
FT /note="I -> T (in dbSNP:rs259028)"
FT /evidence="ECO:0000269|PubMed:11546807,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9205841"
FT /id="VAR_019490"
FT VARIANT 1055
FT /note="S -> G (in dbSNP:rs249038)"
FT /evidence="ECO:0000269|PubMed:11546807,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:9205841"
FT /id="VAR_019491"
FT VARIANT 1519
FT /note="T -> N (in dbSNP:rs16877836)"
FT /id="VAR_057493"
FT MUTAGEN 753
FT /note="C->S: Abolishes localization to endosomes and
FT association with PI3P."
FT /evidence="ECO:0000269|PubMed:11546807"
FT CONFLICT 82
FT /note="E -> K (in Ref. 5; AAH30808)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="P -> L (in Ref. 3; CAI45932)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="C -> S (in Ref. 3; CAD97666)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="T -> A (in Ref. 3; CAD89968)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="T -> I (in Ref. 3; CAD89968)"
FT /evidence="ECO:0000305"
FT CONFLICT 934
FT /note="N -> D (in Ref. 3; CAD89968)"
FT /evidence="ECO:0000305"
FT CONFLICT 1217
FT /note="L -> F (in Ref. 3; CAI45932)"
FT /evidence="ECO:0000305"
FT CONFLICT 1308
FT /note="A -> T (in Ref. 3; CAD97666)"
FT /evidence="ECO:0000305"
FT HELIX 3..20
FT /evidence="ECO:0007829|PDB:5MK0"
FT TURN 737..739
FT /evidence="ECO:0007829|PDB:3T7L"
FT HELIX 747..749
FT /evidence="ECO:0007829|PDB:3T7L"
FT TURN 754..756
FT /evidence="ECO:0007829|PDB:3T7L"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:3T7L"
FT TURN 770..772
FT /evidence="ECO:0007829|PDB:3T7L"
FT HELIX 778..780
FT /evidence="ECO:0007829|PDB:3T7L"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:3T7L"
FT TURN 788..790
FT /evidence="ECO:0007829|PDB:3T7L"
FT STRAND 791..796
FT /evidence="ECO:0007829|PDB:3T7L"
FT HELIX 798..807
FT /evidence="ECO:0007829|PDB:3T7L"
SQ SEQUENCE 1539 AA; 168903 MW; D9C2F8DDE12D69E2 CRC64;
MDSYFKAAVS DLDKLLDDFE QNPDEQDYLQ DVQNAYDSNH CSVSSELASS QRTSLLPKDQ
ECVNSCASSE TSYGTNESSL NEKTLKGLTS IQNEKNVTGL DLLSSVDGGT SDEIQPLYMG
RCSKPICDLI SDMGNLVHAT NSEEDIKKLL PDDFKSNADS LIGLDLSSVS DTPCVSSTDH
DSDTVREQQN DISSELQNRE IGGIKELGIK VDTTLSDSYN YSGTENLKDK KIFNQLESIV
DFNMSSALTR QSSKMFHAKD KLQHKSQPCG LLKDVGLVKE EVDVAVITAA ECLKEEGKTS
ALTCSLPKNE DLCLNDSNSR DENFKLPDFS FQEDKTVIKQ SAQEDSKSLD LKDNDVIQDS
SSALHVSSKD VPSSLSCLPA SGSMCGSLIE SKARGDFLPQ HEHKDNIQDA VTIHEEIQNS
VVLGGEPFKE NDLLKQEKCK SILLQSLIEG MEDRKIDPDQ TVIRAESLDG GDTSSTVVES
QEGLSGTHVP ESSDCCEGFI NTFSSNDMDG QDLDYFNIDE GAKSGPLISD AELDAFLTEQ
YLQTTNIKSF EENVNDSKSQ MNQIDMKGLD DGNINNIYFN AEAGAIGESH GINIICEIVD
KQNTIENGLS LGEKSTIPVQ QGLPTSKSEI TNQLSVSDIN SQSVGGARPK QLFSLPSRTR
SSKDLNKPDV PDTIESEPST ADTVVPITCA IDSTADPQVS FNSNYIDIES NSEGGSSFVT
ANEDSVPENT CKEGLVLGQK QPTWVPDSEA PNCMNCQVKF TFTKRRHHCR ACGKVFCGVC
CNRKCKLQYL EKEARVCVVC YETISKAQAF ERMMSPTGSN LKSNHSDECT TVQPPQENQT
SSIPSPATLP VSALKQPGVE GLCSKEQKRV WFADGILPNG EVADTTKLSS GSKRCSEDFS
PLSPDVPMTV NTVDHSHSTT VEKPNNETGD ITRNEIIQSP ISQVPSVEKL SMNTGNEGLP
TSGSFTLDDD VFAETEEPSS PTGVLVNSNL PIASISDYRL LCDINKYVCN KISLLPNDED
SLPPLLVASG EKGSVPVVEE HPSHEQIILL LEGESFHPVT FVLNANLLVN VKFIFYSSDK
YWYFSTNGLH GLGQAEIIIL LLCLPNEDTI PKDIFRLFIT IYKDALKGKY IENLDNITFT
ESFLSSKDHG GFLFITPTFQ KLDDLSLPSN PFLCGILIQK LEIPWAKVFP MRLMLRLGAE
YKAYPAPLTS IRGRKPLFGE IGHTIMNLLV DLRNYQYTLH NIDQLLIHME MGKSCIKIPR
KKYSDVMKVL NSSNEHVISI GASFSTEADS HLVCIQNDGI YETQANSATG HPRKVTGASF
VVFNGALKTS SGFLAKSSIV EDGLMVQITP ETMNGLRLAL REQKDFKITC GKVDAVDLRE
YVDICWVDAE EKGNKGVISS VDGISLQGFP SEKIKLEADF ETDEKIVKCT EVFYFLKDQD
LSILSTSYQF AKEIAMACSA ALCPHLKTLK SNGMNKIGLR VSIDTDMVEF QAGSEGQLLP
QHYLNDLDSA LIPVIHGGTS NSSLPLEIEL VFFIIEHLF
