ZFYV1_MOUSE
ID ZFYV1_MOUSE Reviewed; 777 AA.
AC Q810J8; Q3TC20;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Zinc finger FYVE domain-containing protein 1;
GN Name=Zfyve1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [6]
RP FUNCTION.
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).
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) contact sites by forming a
CC complex with RAB18 and ZW10 (By similarity). Binds to
CC phosphatidylinositol 3-phosphate (PtdIns3P) through FYVE-type zinc
CC finger (By similarity). {ECO:0000250|UniProtKB:Q9HBF4,
CC ECO:0000269|PubMed:30970241, ECO:0000269|PubMed:31293035}.
CC -!- SUBUNIT: Interacts with RAB18 (in GTP-bound form) (By similarity).
CC Interacts with BSCL2 in a RAB18-dependent manner (By similarity).
CC Interacts with ZW10 (By similarity). {ECO:0000250|UniProtKB:Q9HBF4}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:25876663}.
CC Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q9HBF4}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:25876663}. Preautophagosomal
CC structure {ECO:0000250|UniProtKB:Q9HBF4}. Lipid droplet
CC {ECO:0000269|PubMed:31293035}. Mitochondrion
CC {ECO:0000269|PubMed:25876663}. Note=Resides predominantly in the
CC cisternal stacks of the Golgi. Colocalizes with TRIM13 on the
CC perinuclear endoplasmic reticulum. During starvation conditions,
CC localizes to omegasomes which are endoplasmic reticulum connected
CC strutures at the origin of preautophagosomal structures. Localizes to
CC lipid droplets in the presence of oleic acid (By similarity).
CC {ECO:0000250|UniProtKB:Q9HBF4}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:25876663}.
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DR EMBL; AK170954; BAE42137.1; -; mRNA.
DR EMBL; BC050015; AAH50015.1; -; mRNA.
DR CCDS; CCDS26028.1; -.
DR RefSeq; NP_898977.2; NM_183154.3.
DR RefSeq; XP_006515752.1; XM_006515689.3.
DR RefSeq; XP_006515753.1; XM_006515690.3.
DR RefSeq; XP_006515754.1; XM_006515691.2.
DR AlphaFoldDB; Q810J8; -.
DR BioGRID; 229946; 5.
DR STRING; 10090.ENSMUSP00000042224; -.
DR iPTMnet; Q810J8; -.
DR PhosphoSitePlus; Q810J8; -.
DR EPD; Q810J8; -.
DR MaxQB; Q810J8; -.
DR PaxDb; Q810J8; -.
DR PRIDE; Q810J8; -.
DR ProteomicsDB; 275365; -.
DR Antibodypedia; 143; 187 antibodies from 22 providers.
DR DNASU; 217695; -.
DR Ensembl; ENSMUST00000048319; ENSMUSP00000042224; ENSMUSG00000042628.
DR Ensembl; ENSMUST00000221919; ENSMUSP00000152501; ENSMUSG00000042628.
DR GeneID; 217695; -.
DR KEGG; mmu:217695; -.
DR UCSC; uc007odg.1; mouse.
DR CTD; 53349; -.
DR MGI; MGI:3026685; Zfyve1.
DR VEuPathDB; HostDB:ENSMUSG00000042628; -.
DR eggNOG; KOG1818; Eukaryota.
DR GeneTree; ENSGT00390000016097; -.
DR HOGENOM; CLU_020922_0_0_1; -.
DR InParanoid; Q810J8; -.
DR OMA; NCYENRG; -.
DR OrthoDB; 198211at2759; -.
DR PhylomeDB; Q810J8; -.
DR TreeFam; TF323237; -.
DR BioGRID-ORCS; 217695; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Zfyve1; mouse.
DR PRO; PR:Q810J8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q810J8; protein.
DR Bgee; ENSMUSG00000042628; Expressed in spermatid and 217 other tissues.
DR ExpressionAtlas; Q810J8; baseline and differential.
DR Genevisible; Q810J8; MM.
DR GO; GO:0005776; C:autophagosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0097629; C:extrinsic component of omegasome membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:1990462; C:omegasome; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0000407; C:phagophore assembly site; ISS:UniProtKB.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI.
DR GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; ISO:MGI.
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 Endoplasmic reticulum; Golgi apparatus; Lipid droplet; Metal-binding;
KW Mitochondrion; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..777
FT /note="Zinc finger FYVE domain-containing protein 1"
FT /id="PRO_0000098714"
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:0000250|UniProtKB:Q9HBF4"
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 CONFLICT 185
FT /note="I -> V (in Ref. 1; BAE42137)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="G -> S (in Ref. 1; BAE42137)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 86940 MW; DF1B0B45E948D4B1 CRC64;
MSAQTSLAEK GLNPGLMCQE SYACSGTDEA IFECDECCSL QCLRCEEELH RQERLRNHER
IRLKAGHVPY CDPCKGPNGH SPGVRQRAAV RCQTCKINLC LECQKRTHSG GNKRRHPITV
YLVSKVQESL EGEEMDEETK RKKMTERVVS FLLVDENEEI QVTNEEDFIR KLDCKPDQHL
KVVSIFGNTG DGKSHTLNHT FFYGREVFKT SPAQESCTVG VWAAYDPVHK VAVIDTEGLL
GATVNLSQRT RLLLKVLAIS DLVIYRTHAD RLHNDLFKFL GDASEAYLKH FTKELKATTA
RCGLDVPLST LGPAVIIFHE TVHTQLLGSD HPSEAPEKLI QDRFRKLGRF PEAFSSIHYK
GTRTYNPPTD FSGLRRALEQ LLENNTTRSP RHPGVIFKAL KALSDRFSGE IPDDQMAHSS
FFPDEYFTCS SLCLSCGAGC KNSMNHGKEG VPHEAKSRCR YSHQYDNRVY TCKACYERGK
EVSVVPKTSA STDSPWMGLA KYAWSGYVIE CPNCGVVYRS RQYWFGNQDP VDTVVRTEIV
HVWPGTDAFL KDNNNAAQRL LDGMNFMAQS VSELSLGPTK AVTSWLTDQI APAYWRPNSQ
ILSCNQCATS FKDNDTKHHC RACGEGFCDS CSSKTRPVPE RGWGPAPVRV CDSCYDARNV
QLDVTEAQAD DEGGTLIARK VGEAVQNTLG AVVTAIDIPL GLVKDAARPA YWVPDHEILH
CHNCRKEFSV KLSKHHCRAC GQGFCDECSH DCRAVPSRGW DHPVRVCFNC NKKPGDL
