ZFYV1_HUMAN
ID ZFYV1_HUMAN Reviewed; 777 AA.
AC Q9HBF4; J3KNL9; Q8WYX7; Q96K57; Q9BXP9; Q9HCI3;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger FYVE domain-containing protein 1;
DE AltName: Full=Double FYVE-containing protein 1;
DE AltName: Full=SR3;
DE AltName: Full=Tandem FYVE fingers-1;
GN Name=ZFYVE1; Synonyms=DFCP1, KIAA1589, TAFF1, ZNFN2A1; ORFNames=PP10436;
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), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Bone marrow stroma;
RX PubMed=11024279; DOI=10.1016/s0378-1119(00)00303-6;
RA Derubeis A.R., Young M.F., Jia L., Robey P.G., Fisher L.W.;
RT "Double FYVE-containing protein 1 (DFCP1): isolation, cloning and
RT characterization of a novel FYVE finger protein from a human bone marrow
RT cDNA library.";
RL Gene 255:195-203(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-770.
RX PubMed=11739631; DOI=10.1242/jcs.114.22.3991;
RA Ridley S.H., Ktistakis N., Davidson K., Anderson K.E., Manifava M.,
RA Ellson C.D., Lipp P., Bootman M., Coadwell J., Nazarian A.,
RA Erdjument-Bromage H., Tempst P., Cooper M.A., Thuring J.W.J.F., Lim Z.-Y.,
RA Holmes A.B., Stephens L.R., Hawkins P.T.;
RT "FENS-1 and DFCP1 are FYVE domain-containing proteins with distinct
RT functions in the endosomal and Golgi compartments.";
RL J. Cell Sci. 114:3991-4000(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF THR-616; LYS-617; HIS-619; ARG-621; CYS-654; SER-733;
RP LYS-734; HIS-736; ARG-738 AND CYS-770, AND TISSUE SPECIFICITY.
RX PubMed=11256955; DOI=10.1042/0264-6021:3550113;
RA Cheung P.C.F., Trinkle-Mulcahy L., Cohen P., Lucocq J.M.;
RT "Characterization of a novel phosphatidylinositol 3-phosphate-binding
RT protein containing two FYVE fingers in tandem that is targeted to the
RT Golgi.";
RL Biochem. J. 355:113-121(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
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 (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Eye, and Melanoma;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-777 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=22178386; DOI=10.1016/j.bbamcr.2011.11.015;
RA Tomar D., Singh R., Singh A.K., Pandya C.D., Singh R.;
RT "TRIM13 regulates ER stress induced autophagy and clonogenic ability of the
RT cells.";
RL Biochim. Biophys. Acta 1823:316-326(2012).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=25876663; DOI=10.2220/biomedres.36.121;
RA Nanao T., Koike M., Yamaguchi J., Sasaki M., Uchiyama Y.;
RT "Cellular localization and tissue distribution of endogenous DFCP1
RT protein.";
RL Biomed. Res. 36:121-133(2015).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-654 AND CYS-770, AND
RP INTERACTION WITH RAB18.
RX PubMed=31293035; DOI=10.1002/cbin.11199;
RA Gao G., Sheng Y., Yang H., Chua B.T., Xu L.;
RT "DFCP1 associates with lipid droplets.";
RL Cell Biol. Int. 0:0-0(2019).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB18; BSCL2 AND ZW10, AND
RP MUTAGENESIS OF TRP-543; CYS-654 AND CYS-770.
RX PubMed=30970241; DOI=10.1016/j.celrep.2019.03.025;
RA Li D., Zhao Y.G., Li D., Zhao H., Huang J., Miao G., Feng D., Liu P.,
RA Li D., Zhang H.;
RT "The ER-Localized Protein DFCP1 Modulates ER-Lipid Droplet Contact
RT Formation.";
RL Cell Rep. 27:343-358(2019).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=33499712; DOI=10.1080/15548627.2021.1874133;
RA Kojima W., Yamano K., Kosako H., Imai K., Kikuchi R., Tanaka K.,
RA Matsuda N.;
RT "Mammalian BCAS3 and C16orf70 associate with the phagophore assembly site
RT in response to selective and non-selective autophagy.";
RL Autophagy 1:1-26(2021).
CC -!- FUNCTION: Plays a role in the formation of lipid droplets (LDs) which
CC are storage organelles at the center of lipid and energy homeostasis
CC (PubMed:30970241). Regulates the morphology, size and distribution of
CC LDs (PubMed:31293035, PubMed:30970241). Mediates the formation of
CC endoplasmic reticulum-lipid droplets (ER-LD) contacts by forming a
CC complex with RAB18 and ZW10 (PubMed:30970241). Binds to
CC phosphatidylinositol 3-phosphate (PtdIns3P) through FYVE-type zinc
CC finger (PubMed:11739631, PubMed:11256955).
CC {ECO:0000269|PubMed:11256955, ECO:0000269|PubMed:11739631,
CC ECO:0000269|PubMed:30970241, ECO:0000269|PubMed:31293035}.
CC -!- SUBUNIT: Interacts with RAB18 (in GTP-bound form) (PubMed:31293035,
CC PubMed:30970241). Interacts with BSCL2 in a RAB18-dependent manner
CC (PubMed:30970241). Interacts with ZW10 (PubMed:30970241).
CC {ECO:0000269|PubMed:30970241, ECO:0000269|PubMed:31293035}.
CC -!- INTERACTION:
CC Q9HBF4; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-4401611, EBI-746778;
CC Q9HBF4; P62136: PPP1CA; NbExp=2; IntAct=EBI-4401611, EBI-357253;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack
CC {ECO:0000269|PubMed:11256955}. Golgi apparatus
CC {ECO:0000269|PubMed:11024279, ECO:0000269|PubMed:11739631,
CC ECO:0000269|PubMed:25876663}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:11024279, ECO:0000269|PubMed:22178386,
CC ECO:0000269|PubMed:25876663, ECO:0000269|PubMed:30970241}. Lipid
CC droplet {ECO:0000269|PubMed:30970241, ECO:0000269|PubMed:31293035}.
CC Preautophagosomal structure {ECO:0000269|PubMed:25876663,
CC ECO:0000269|PubMed:31293035, ECO:0000269|PubMed:33499712}.
CC Mitochondrion {ECO:0000269|PubMed:25876663}. Note=Resides predominantly
CC in the cisternal stacks of the Golgi (PubMed:11256955). Colocalizes
CC with TRIM13 on the perinuclear endoplasmic reticulum (PubMed:22178386).
CC During starvation conditions, localizes to omegasomes which are
CC endoplasmic reticulum connected strutures at the origin of
CC preautophagosomal structures (PubMed:31293035, PubMed:25876663).
CC Localizes to lipid droplets in the presence of oleic acid
CC (PubMed:31293035, PubMed:30970241). {ECO:0000269|PubMed:11256955,
CC ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:30970241,
CC ECO:0000269|PubMed:31293035}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HBF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HBF4-2; Sequence=VSP_008007;
CC Name=3;
CC IsoId=Q9HBF4-3; Sequence=VSP_056770;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Highly expressed in heart. Also
CC detected in the testis. {ECO:0000269|PubMed:11024279,
CC ECO:0000269|PubMed:11256955}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in all tissues examined,
CC including, brain, placenta, lung, liver, skeletal muscle, pancreas and
CC kidney. Highly expressed in heart. {ECO:0000269|PubMed:11024279,
CC ECO:0000269|PubMed:11256955}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL55826.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB13415.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55085.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF251025; AAG23748.1; -; mRNA.
DR EMBL; AJ310569; CAC83950.1; -; mRNA.
DR EMBL; AF311602; AAK27339.1; -; mRNA.
DR EMBL; AB046809; BAB13415.1; ALT_INIT; mRNA.
DR EMBL; AK027399; BAB55085.1; ALT_TERM; mRNA.
DR EMBL; AL442663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81084.1; -; Genomic_DNA.
DR EMBL; BC053520; AAH53520.1; -; mRNA.
DR EMBL; BC014902; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF318319; AAL55826.1; ALT_FRAME; mRNA.
DR CCDS; CCDS41969.1; -. [Q9HBF4-2]
DR CCDS; CCDS61498.1; -. [Q9HBF4-3]
DR CCDS; CCDS9811.1; -. [Q9HBF4-1]
DR RefSeq; NP_001268663.1; NM_001281734.1. [Q9HBF4-3]
DR RefSeq; NP_001268664.1; NM_001281735.1. [Q9HBF4-2]
DR RefSeq; NP_067083.1; NM_021260.3. [Q9HBF4-1]
DR RefSeq; NP_848535.1; NM_178441.2. [Q9HBF4-2]
DR RefSeq; XP_016876862.1; XM_017021373.1. [Q9HBF4-2]
DR AlphaFoldDB; Q9HBF4; -.
DR BioGRID; 119749; 51.
DR IntAct; Q9HBF4; 15.
DR MINT; Q9HBF4; -.
DR STRING; 9606.ENSP00000450742; -.
DR iPTMnet; Q9HBF4; -.
DR PhosphoSitePlus; Q9HBF4; -.
DR BioMuta; ZFYVE1; -.
DR DMDM; 34098716; -.
DR EPD; Q9HBF4; -.
DR jPOST; Q9HBF4; -.
DR MassIVE; Q9HBF4; -.
DR MaxQB; Q9HBF4; -.
DR PaxDb; Q9HBF4; -.
DR PeptideAtlas; Q9HBF4; -.
DR PRIDE; Q9HBF4; -.
DR ProteomicsDB; 81536; -. [Q9HBF4-1]
DR ProteomicsDB; 81537; -. [Q9HBF4-2]
DR Antibodypedia; 143; 187 antibodies from 22 providers.
DR DNASU; 53349; -.
DR Ensembl; ENST00000318876.9; ENSP00000326921.5; ENSG00000165861.14. [Q9HBF4-3]
DR Ensembl; ENST00000394207.6; ENSP00000377757.2; ENSG00000165861.14. [Q9HBF4-2]
DR Ensembl; ENST00000555072.1; ENSP00000452232.1; ENSG00000165861.14. [Q9HBF4-2]
DR Ensembl; ENST00000556143.6; ENSP00000450742.1; ENSG00000165861.14. [Q9HBF4-1]
DR GeneID; 53349; -.
DR KEGG; hsa:53349; -.
DR MANE-Select; ENST00000556143.6; ENSP00000450742.1; NM_021260.4; NP_067083.1.
DR UCSC; uc001xnl.5; human. [Q9HBF4-1]
DR CTD; 53349; -.
DR DisGeNET; 53349; -.
DR GeneCards; ZFYVE1; -.
DR HGNC; HGNC:13180; ZFYVE1.
DR HPA; ENSG00000165861; Low tissue specificity.
DR MIM; 605471; gene.
DR neXtProt; NX_Q9HBF4; -.
DR OpenTargets; ENSG00000165861; -.
DR PharmGKB; PA37752; -.
DR VEuPathDB; HostDB:ENSG00000165861; -.
DR eggNOG; KOG1818; Eukaryota.
DR GeneTree; ENSGT00390000016097; -.
DR HOGENOM; CLU_020922_0_0_1; -.
DR InParanoid; Q9HBF4; -.
DR OrthoDB; 198211at2759; -.
DR PhylomeDB; Q9HBF4; -.
DR TreeFam; TF323237; -.
DR PathwayCommons; Q9HBF4; -.
DR SignaLink; Q9HBF4; -.
DR SIGNOR; Q9HBF4; -.
DR BioGRID-ORCS; 53349; 13 hits in 1087 CRISPR screens.
DR ChiTaRS; ZFYVE1; human.
DR GeneWiki; ZFYVE1; -.
DR GenomeRNAi; 53349; -.
DR Pharos; Q9HBF4; Tbio.
DR PRO; PR:Q9HBF4; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9HBF4; protein.
DR Bgee; ENSG00000165861; Expressed in tibialis anterior and 192 other tissues.
DR ExpressionAtlas; Q9HBF4; baseline and differential.
DR Genevisible; Q9HBF4; HS.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0097629; C:extrinsic component of omegasome membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:1990462; C:omegasome; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IDA:ParkinsonsUK-UCL.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR042427; ZFYV1.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46624; PTHR46624; 1.
DR Pfam; PF01363; FYVE; 2.
DR SMART; SM00064; FYVE; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS50178; ZF_FYVE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Golgi apparatus;
KW Lipid droplet; Metal-binding; Mitochondrion; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..777
FT /note="Zinc finger FYVE domain-containing protein 1"
FT /id="PRO_0000098713"
FT ZN_FING 598..659
FT /note="FYVE-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT ZN_FING 715..775
FT /note="FYVE-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 416..777
FT /note="Required for localization in the lipid droplets"
FT /evidence="ECO:0000269|PubMed:30970241,
FT ECO:0000269|PubMed:31293035"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 623
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 628
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 631
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 654
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 737
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 740
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 745
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 748
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 770
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT VAR_SEQ 1..415
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11256955"
FT /id="VSP_008007"
FT VAR_SEQ 507..520
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056770"
FT MUTAGEN 543
FT /note="W->A: Disrupts its localization to lipid droplets."
FT /evidence="ECO:0000269|PubMed:30970241"
FT MUTAGEN 616
FT /note="T->R: Partially restore PtdIns3P binding; when
FT associated with R-733."
FT /evidence="ECO:0000269|PubMed:11256955"
FT MUTAGEN 617
FT /note="K->A: Drastically reduce PtdIns3P binding; when
FT associated with A-619 and A-621. Abolishes PtdIns3P
FT binding; when associated with A-734; A-736 and A-738."
FT /evidence="ECO:0000269|PubMed:11256955"
FT MUTAGEN 619
FT /note="H->A: Drastically reduce PtdIns3P binding; when
FT associated with A-617 and A-621. Abolishes PtdIns3P
FT binding; when associated with A-734; A-736 and A-738."
FT /evidence="ECO:0000269|PubMed:11256955"
FT MUTAGEN 621
FT /note="R->A: Drastically reduce PtdIns3P binding; when
FT associated with A-617 and A-619. Abolishes PtdIns3P
FT binding; when associated with A-734; A-736 and A-738."
FT /evidence="ECO:0000269|PubMed:11256955"
FT MUTAGEN 654
FT /note="C->S: Abolishes PtdIns3P binding but has no effect
FT on its localization to lipid droplets or its interaction
FT with RAB18; when associated with S-770."
FT /evidence="ECO:0000269|PubMed:11256955,
FT ECO:0000269|PubMed:30970241, ECO:0000269|PubMed:31293035"
FT MUTAGEN 733
FT /note="S->R: Partially restored PtdIns3P binding; when
FT associated with R-616."
FT /evidence="ECO:0000269|PubMed:11256955"
FT MUTAGEN 734
FT /note="K->A: Drastically reduce PtdIns3P binding; when
FT associated with A-736 and A-738. Abolishes PtdIns3P
FT binding; when associated with A-617; A-619 and A-621."
FT /evidence="ECO:0000269|PubMed:11256955"
FT MUTAGEN 736
FT /note="H->A: Drastically reduce PtdIns3P binding; when
FT associated with A-734 and A-738. Abolishes PtdIns3P
FT binding; when associated with A-617; A-619 and A-621."
FT /evidence="ECO:0000269|PubMed:11256955"
FT MUTAGEN 738
FT /note="R->A: Drastically reduce PtdIns3P binding; when
FT associated with A-734 and A-736. Abolishes PtdIns3P
FT binding; when associated with A-617; A-619 and A-621."
FT /evidence="ECO:0000269|PubMed:11256955"
FT MUTAGEN 770
FT /note="C->S: Abolishes PtdIns3P binding but has no effect
FT on its localization to lipid droplets or its interaction
FT with RAB18; when associated with S-654."
FT /evidence="ECO:0000269|PubMed:11256955,
FT ECO:0000269|PubMed:11739631, ECO:0000269|PubMed:30970241,
FT ECO:0000269|PubMed:31293035"
FT CONFLICT 120
FT /note="V -> M (in Ref. 8; BC014902)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 87176 MW; 11B5E561066CBCD5 CRC64;
MSAQTSPAEK GLNPGLMCQE SYACSGTDEA IFECDECCSL QCLRCEEELH RQERLRNHER
IRLKPGHVPY CDLCKGLSGH LPGVRQRAIV RCQTCKINLC LECQKRTHSG GNKRRHPVTV
YNVSNLQESL EAEEMDEETK RKKMTEKVVS FLLVDENEEI QVTNEEDFIR KLDCKPDQHL
KVVSIFGNTG DGKSHTLNHT FFYGREVFKT SPTQESCTVG VWAAYDPVHK VAVIDTEGLL
GATVNLSQRT RLLLKVLAIS DLVIYRTHAD RLHNDLFKFL GDASEAYLKH FTKELKATTA
RCGLDVPLST LGPAVIIFHE TVHTQLLGSD HPSEVPEKLI QDRFRKLGRF PEAFSSIHYK
GTRTYNPPTD FSGLRRALEQ LLENNTTRSP RHPGVIFKAL KALSDRFSGE IPDDQMAHSS
FFPDEYFTCS SLCLSCGVGC KKSMNHGKEG VPHEAKSRCR YSHQYDNRVY TCKACYERGE
EVSVVPKTSA STDSPWMGLA KYAWSGYVIE CPNCGVVYRS RQYWFGNQDP VDTVVRTEIV
HVWPGTDGFL KDNNNAAQRL LDGMNFMAQS VSELSLGPTK AVTSWLTDQI APAYWRPNSQ
ILSCNKCATS FKDNDTKHHC RACGEGFCDS CSSKTRPVPE RGWGPAPVRV CDNCYEARNV
QLAVTEAQVD DEGGTLIARK VGEAVQNTLG AVVTAIDIPL GLVKDAARPA YWVPDHEILH
CHNCRKEFSI KLSKHHCRAC GQGFCDECSH DRRAVPSRGW DHPVRVCFNC NKKPGDL
