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Zinc finger FYVE domain-containing protein 1 (Double FYVE-containing protein 1) (SR3) (Tandem FYVE fingers-1)

 ZFYV1_HUMAN             Reviewed;         777 AA.
Q9HBF4; J3KNL9; Q8WYX7; Q96K57; Q9BXP9; Q9HCI3;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
27-SEP-2017, entry version 144.
RecName: Full=Zinc finger FYVE domain-containing protein 1;
AltName: Full=Double FYVE-containing protein 1;
AltName: Full=SR3;
AltName: Full=Tandem FYVE fingers-1;
Name=ZFYVE1; Synonyms=DFCP1, KIAA1589, TAFF1, ZNFN2A1;
ORFNames=PP10436;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
TISSUE=Bone marrow stroma;
PubMed=11024279; DOI=10.1016/S0378-1119(00)00303-6;
Derubeis A.R., Young M.F., Jia L., Robey P.G., Fisher L.W.;
"Double FYVE-containing protein 1 (DFCP1): isolation, cloning and
characterization of a novel FYVE finger protein from a human bone
marrow cDNA library.";
Gene 255:195-203(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
INTERACTION WITH PTDINS3P, AND MUTAGENESIS OF CYS-770.
PubMed=11739631;
Ridley S.H., Ktistakis N., Davidson K., Anderson K.E., Manifava M.,
Ellson C.D., Lipp P., Bootman M., Coadwell J., Nazarian A.,
Erdjument-Bromage H., Tempst P., Cooper M.A., Thuring J.W.J.F.,
Lim Z.-Y., Holmes A.B., Stephens L.R., Hawkins P.T.;
"FENS-1 and DFCP1 are FYVE domain-containing proteins with distinct
functions in the endosomal and Golgi compartments.";
J. Cell Sci. 114:3991-4000(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION, INTERACTION
WITH PTDINS3P, AND MUTAGENESIS OF THR-616; LYS-617; HIS-619; ARG-621;
CYS-654; SER-733; LYS-734; HIS-736; ARG-738 AND CYS-770.
PubMed=11256955; DOI=10.1042/0264-6021:3550113;
Cheung P.C.F., Trinkle-Mulcahy L., Cohen P., Lucocq J.M.;
"Characterization of a novel phosphatidylinositol 3-phosphate-binding
protein containing two FYVE fingers in tandem that is targeted to the
Golgi.";
Biochem. J. 355:113-121(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10997877; DOI=10.1093/dnares/7.4.271;
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes.
XVIII. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro.";
DNA Res. 7:273-281(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Eye, and Melanoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-777 (ISOFORM 1).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[10]
INTERACTION WITH TRIM13, AND SUBCELLULAR LOCATION.
PubMed=22178386; DOI=10.1016/j.bbamcr.2011.11.015;
Tomar D., Singh R., Singh A.K., Pandya C.D., Singh R.;
"TRIM13 regulates ER stress induced autophagy and clonogenic ability
of the cells.";
Biochim. Biophys. Acta 1823:316-326(2012).
-!- SUBUNIT: Binds to phosphatidylinositol 3-phosphate (PtdIns3P)
through its FYVE-type zinc finger.
-!- INTERACTION:
P62136:PPP1CA; NbExp=2; IntAct=EBI-4401611, EBI-357253;
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack. Endoplasmic
reticulum. Note=Resides predominantly in the cisternal stacks of
the Golgi. Colocalizes with TRIM13 on the perinuclear endoplasmic
reticulum.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9HBF4-1; Sequence=Displayed;
Name=2;
IsoId=Q9HBF4-2; Sequence=VSP_008007;
Name=3;
IsoId=Q9HBF4-3; Sequence=VSP_056770;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in all tissues
examined, including, brain, placenta, lung, liver, skeletal
muscle, pancreas and kidney. Isoform 1 and isoform 2 are highly
expressed in heart. Isoform 2 is also detected in the testis.
-!- SEQUENCE CAUTION:
Sequence=AAL55826.1; Type=Frameshift; Positions=480; Evidence={ECO:0000305};
Sequence=BAB13415.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB55085.1; Type=Erroneous termination; Positions=760; Note=Translated as Trp.; Evidence={ECO:0000305};
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EMBL; AF251025; AAG23748.1; -; mRNA.
EMBL; AJ310569; CAC83950.1; -; mRNA.
EMBL; AF311602; AAK27339.1; -; mRNA.
EMBL; AB046809; BAB13415.1; ALT_INIT; mRNA.
EMBL; AK027399; BAB55085.1; ALT_TERM; mRNA.
EMBL; AL442663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81084.1; -; Genomic_DNA.
EMBL; BC053520; AAH53520.1; -; mRNA.
EMBL; BC014902; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF318319; AAL55826.1; ALT_FRAME; mRNA.
CCDS; CCDS41969.1; -. [Q9HBF4-2]
CCDS; CCDS61498.1; -. [Q9HBF4-3]
CCDS; CCDS9811.1; -. [Q9HBF4-1]
RefSeq; NP_001268663.1; NM_001281734.1. [Q9HBF4-3]
RefSeq; NP_001268664.1; NM_001281735.1. [Q9HBF4-2]
RefSeq; NP_067083.1; NM_021260.3. [Q9HBF4-1]
RefSeq; NP_848535.1; NM_178441.2. [Q9HBF4-2]
RefSeq; XP_016876862.1; XM_017021373.1. [Q9HBF4-2]
UniGene; Hs.335106; -.
ProteinModelPortal; Q9HBF4; -.
BioGrid; 119749; 10.
IntAct; Q9HBF4; 9.
MINT; MINT-8247369; -.
STRING; 9606.ENSP00000450742; -.
iPTMnet; Q9HBF4; -.
PhosphoSitePlus; Q9HBF4; -.
BioMuta; ZFYVE1; -.
DMDM; 34098716; -.
EPD; Q9HBF4; -.
MaxQB; Q9HBF4; -.
PaxDb; Q9HBF4; -.
PeptideAtlas; Q9HBF4; -.
PRIDE; Q9HBF4; -.
Ensembl; ENST00000318876; ENSP00000326921; ENSG00000165861. [Q9HBF4-3]
Ensembl; ENST00000394207; ENSP00000377757; ENSG00000165861. [Q9HBF4-2]
Ensembl; ENST00000555072; ENSP00000452232; ENSG00000165861. [Q9HBF4-2]
Ensembl; ENST00000556143; ENSP00000450742; ENSG00000165861. [Q9HBF4-1]
GeneID; 53349; -.
KEGG; hsa:53349; -.
UCSC; uc001xnl.5; human. [Q9HBF4-1]
CTD; 53349; -.
DisGeNET; 53349; -.
EuPathDB; HostDB:ENSG00000165861.13; -.
GeneCards; ZFYVE1; -.
HGNC; HGNC:13180; ZFYVE1.
HPA; HPA002898; -.
MIM; 605471; gene.
neXtProt; NX_Q9HBF4; -.
OpenTargets; ENSG00000165861; -.
PharmGKB; PA37752; -.
eggNOG; KOG1818; Eukaryota.
eggNOG; ENOG410XNRF; LUCA.
GeneTree; ENSGT00390000016097; -.
HOGENOM; HOG000044357; -.
HOVERGEN; HBG057679; -.
InParanoid; Q9HBF4; -.
KO; K17603; -.
PhylomeDB; Q9HBF4; -.
TreeFam; TF323237; -.
SIGNOR; Q9HBF4; -.
ChiTaRS; ZFYVE1; human.
GeneWiki; ZFYVE1; -.
GenomeRNAi; 53349; -.
PRO; PR:Q9HBF4; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000165861; -.
CleanEx; HS_ZFYVE1; -.
ExpressionAtlas; Q9HBF4; baseline and differential.
Genevisible; Q9HBF4; HS.
GO; GO:0005776; C:autophagosome; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0044233; C:ER-mitochondrion membrane contact site; IDA:MGI.
GO; GO:0097629; C:extrinsic component of omegasome membrane; IDA:UniProtKB.
GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
GO; GO:1990462; C:omegasome; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0000407; C:pre-autophagosomal structure; IDA:MGI.
GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IDA:ParkinsonsUK-UCL.
GO; GO:0016236; P:macroautophagy; IDA:ParkinsonsUK-UCL.
GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000306; Znf_FYVE.
InterPro; IPR017455; Znf_FYVE-rel.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF01363; FYVE; 2.
SMART; SM00064; FYVE; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS50178; ZF_FYVE; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Endoplasmic reticulum;
Golgi apparatus; Metal-binding; Reference proteome; Repeat; Zinc;
Zinc-finger.
CHAIN 1 777 Zinc finger FYVE domain-containing
protein 1.
/FTId=PRO_0000098713.
ZN_FING 598 659 FYVE-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00091}.
ZN_FING 715 775 FYVE-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00091}.
VAR_SEQ 1 415 Missing (in isoform 2).
{ECO:0000303|PubMed:11256955}.
/FTId=VSP_008007.
VAR_SEQ 507 520 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056770.
MUTAGEN 616 616 T->R: Partially restore PtdIns3P binding;
when associated with R-733.
{ECO:0000269|PubMed:11256955}.
MUTAGEN 617 617 K->A: Drastically reduce PtdIns3P
binding; when associated with A-619 and
A-621. Abolishes PtdIns3P binding; when
associated with A-734; A-736 and A-738.
{ECO:0000269|PubMed:11256955}.
MUTAGEN 619 619 H->A: Drastically reduce PtdIns3P
binding; when associated with A-617 and
A-621. Abolishes PtdIns3P binding; when
associated with A-734; A-736 and A-738.
{ECO:0000269|PubMed:11256955}.
MUTAGEN 621 621 R->A: Drastically reduce PtdIns3P
binding; when associated with A-617 and
A-619. Abolishes PtdIns3P binding; when
associated with A-734; A-736 and A-738.
{ECO:0000269|PubMed:11256955}.
MUTAGEN 654 654 C->S: Abolishes PtdIns3P binding; when
associated with S-770.
{ECO:0000269|PubMed:11256955}.
MUTAGEN 733 733 S->R: Partially restored PtdIns3P
binding; when associated with R-616.
{ECO:0000269|PubMed:11256955}.
MUTAGEN 734 734 K->A: Drastically reduce PtdIns3P
binding; when associated with A-736 and
A-738. Abolishes PtdIns3P binding; when
associated with A-617; A-619 and A-621.
{ECO:0000269|PubMed:11256955}.
MUTAGEN 736 736 H->A: Drastically reduce PtdIns3P
binding; when associated with A-734 and
A-738. Abolishes PtdIns3P binding; when
associated with A-617; A-619 and A-621.
{ECO:0000269|PubMed:11256955}.
MUTAGEN 738 738 R->A: Drastically reduce PtdIns3P
binding; when associated with A-734 and
A-736. Abolishes PtdIns3P binding; when
associated with A-617; A-619 and A-621.
{ECO:0000269|PubMed:11256955}.
MUTAGEN 770 770 C->S: Abolishes PtdIns3P binding; when
associated with S-654.
{ECO:0000269|PubMed:11256955,
ECO:0000269|PubMed:11739631}.
CONFLICT 120 120 V -> M (in Ref. 8; BC014902).
{ECO:0000305}.
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


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EIAAB46121 Bos taurus,Bovine,WD repeat and FYVE domain-containing protein 1,WD40- and FYVE domain-containing protein 1,WDFY1
EIAAB46123 Mouse,Mus musculus,WD repeat and FYVE domain-containing protein 2,WD40- and FYVE domain-containing protein 2,Wdfy2
E6600h Human Zinc Finger, FYVE Domain Containing Protein 96T
E2959h Human Zinc Finger, FYVE Domain Containing Protein 96T
E3585h Human Zinc Finger, FYVE Domain Containing Protein 96T
E6599h Human Zinc Finger, FYVE Domain Containing Protein 96T
E3584h Human Zinc Finger, FYVE Domain Containing Protein 96T
I3213 Zinc finger FYVE domain-containing protein 21 (ZFYVE21), Rat, ELISA Kit 96T


 

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