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 24-JAN-2024, entry version 179. 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; GN 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). RN [15] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SARS-COV-2 RP NON-STRUCTURAL PROTEIN 6 (MICROBIAL INFECTION). RX PubMed=35551511; DOI=10.1038/s41586-022-04835-6; RA Ricciardi S., Guarino A.M., Giaquinto L., Polishchuk E.V., Santoro M., RA Di Tullio G., Wilson C., Panariello F., Soares V.C., Dias S.S.G., RA Santos J.C., Souza T.M.L., Fusco G., Viscardi M., Brandi S., Bozza P.T., RA Polishchuk R.S., Venditti R., De Matteis M.A.; RT "The role of NSP6 in the biogenesis of the SARS-CoV-2 replication RT organelle."; RL Nature 606:761-768(2022). 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 -!- FUNCTION: (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2 CC infection, mediates through binding with non-structural protein 6 CC (nsp6) the replication organelle-lipid droplet association required to CC sustain viral replication. {ECO:0000269|PubMed:35551511}. 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 -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS- CC CoV-2 non-structural protein 6 (nsp6); the interaction is independent CC of PtdIns3P-binding and leads to endoplasmic reticulum (ER) and double CC membrane vesicles (DMVs) binding to lipid droplets. CC {ECO:0000269|PubMed:35551511}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 55. DR IntAct; Q9HBF4; 15. DR MINT; Q9HBF4; -. DR STRING; 9606.ENSP00000450742; -. DR GlyGen; Q9HBF4; 3 sites, 1 O-linked glycan (3 sites). 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; 9606-ENSP00000450742; -. DR PeptideAtlas; Q9HBF4; -. DR ProteomicsDB; 81536; -. [Q9HBF4-1] DR ProteomicsDB; 81537; -. [Q9HBF4-2] DR Pumba; Q9HBF4; -. DR Antibodypedia; 143; 228 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 AGR; HGNC:13180; -. 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; 277036at2759; -. DR PhylomeDB; Q9HBF4; -. DR TreeFam; TF323237; -. DR PathwayCommons; Q9HBF4; -. DR SignaLink; Q9HBF4; -. DR SIGNOR; Q9HBF4; -. DR BioGRID-ORCS; 53349; 13 hits in 1165 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 194 other cell types or tissues. DR ExpressionAtlas; Q9HBF4; baseline and differential. DR GO; GO:0005776; C:autophagosome; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. 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 GO; GO:0044829; P:positive regulation by host of viral genome replication; IDA:UniProtKB. DR CDD; cd19819; Bbox1_ZFYVE1_rpt1; 1. DR CDD; cd19820; Bbox1_ZFYVE1_rpt2; 1. DR CDD; cd15734; FYVE_ZFYV1; 1. DR CDD; cd01851; GBP; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR042427; ZFYV1. DR InterPro; IPR047856; ZFYVE1_first_BBox1. DR InterPro; IPR047855; ZFYVE1_second_BBox1. 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; AGAP002036-PA; 1. DR PANTHER; PTHR46624:SF3; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF01363; FYVE; 2. DR SMART; SM00064; FYVE; 2. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50178; ZF_FYVE; 2. DR Genevisible; Q9HBF4; HS. 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 //