FYCO1_HUMAN
ID FYCO1_HUMAN Reviewed; 1478 AA.
AC Q9BQS8; B7ZKT7; Q3MJE6; Q86T41; Q86TB1; Q8TEF9; Q96IV5; Q9H8P9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=FYVE and coiled-coil domain-containing protein 1;
DE AltName: Full=Zinc finger FYVE domain-containing protein 7;
GN Name=FYCO1; Synonyms=ZFYVE7;
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 VARIANTS
RP GLN-250 AND ALA-321.
RX PubMed=11896456; DOI=10.1038/sj.ejhg.5200758;
RA Kiss H., Yang Y., Kiss C., Andersson K., Klein G., Imreh S., Dumanski J.P.;
RT "The transcriptional map of the common eliminated region 1 (C3CER1) in
RT 3p21.3.";
RL Eur. J. Hum. Genet. 10:52-61(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-250;
RP ALA-321 AND VAL-679.
RC TISSUE=Skeletal muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 41-1478 (ISOFORM 2), AND VARIANTS GLN-250
RP AND ALA-321.
RC TISSUE=Heart, Lung, and Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-1478 (ISOFORM 3), AND VARIANTS
RP GLN-250 AND ALA-321.
RC TISSUE=Ovary;
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 MRNA] OF 1213-1478 (ISOFORM 1).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH MAP1LC3B AND
RP RAB7A.
RX PubMed=20100911; DOI=10.1083/jcb.200907015;
RA Pankiv S., Alemu E.A., Brech A., Bruun J.A., Lamark T., Overvatn A.,
RA Bjorkoy G., Johansen T.;
RT "FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule
RT plus end-directed vesicle transport.";
RL J. Cell Biol. 188:253-269(2010).
RN [10]
RP SUBCELLULAR LOCATION, AND VARIANT CTRCT18 PRO-1376.
RX PubMed=21636066; DOI=10.1016/j.ajhg.2011.05.008;
RA Chen J., Ma Z., Jiao X., Fariss R., Kantorow W.L., Kantorow M., Pras E.,
RA Frydman M., Pras E., Riazuddin S., Riazuddin S.A., Hejtmancik J.F.;
RT "Mutations in FYCO1 cause autosomal-recessive congenital cataracts.";
RL Am. J. Hum. Genet. 88:827-838(2011).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP 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 [15]
RP INTERACTION WITH MAP1LC3B.
RX PubMed=24089205; DOI=10.1038/nature12606;
RA Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
RA Zhong Q.;
RT "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar
RT satellites.";
RL Nature 502:254-257(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND IDENTIFICATION BY
RP 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 [17]
RP VARIANT CTRCT18 270-GLN--LEU-1478 DEL.
RX PubMed=29914532; DOI=10.1186/s13023-018-0828-0;
RA Li J., Leng Y., Han S., Yan L., Lu C., Luo Y., Zhang X., Cao L.;
RT "Clinical and genetic characteristics of Chinese patients with familial or
RT sporadic pediatric cataract.";
RL Orphanet J. Rare Dis. 13:94-94(2018).
CC -!- FUNCTION: May mediate microtubule plus end-directed vesicle transport.
CC {ECO:0000269|PubMed:20100911}.
CC -!- SUBUNIT: Can form homodimers. Interacts (via C-terminus) with MAP1LC3B.
CC Interacts with RAB7A; the interaction with RAB7A induces FYCO1
CC recruitment to late endosomal/lysosomal compartments. Interacts with
CC MAP1LC3B (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BQS8; O95166: GABARAP; NbExp=2; IntAct=EBI-2869338, EBI-712001;
CC Q9BQS8; Q9H0R8: GABARAPL1; NbExp=2; IntAct=EBI-2869338, EBI-746969;
CC Q9BQS8; P60520: GABARAPL2; NbExp=2; IntAct=EBI-2869338, EBI-720116;
CC Q9BQS8; O60341: KDM1A; NbExp=2; IntAct=EBI-2869338, EBI-710124;
CC Q9BQS8; P33176: KIF5B; NbExp=3; IntAct=EBI-2869338, EBI-355878;
CC Q9BQS8; Q9H0B6: KLC2; NbExp=2; IntAct=EBI-2869338, EBI-726994;
CC Q9BQS8; Q9GZQ8: MAP1LC3B; NbExp=8; IntAct=EBI-2869338, EBI-373144;
CC Q9BQS8; Q9BXW4: MAP1LC3C; NbExp=2; IntAct=EBI-2869338, EBI-2603996;
CC Q9BQS8; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-2869338, EBI-912440;
CC Q9BQS8-2; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-25905795, EBI-12593112;
CC Q9BQS8-2; O14901: KLF11; NbExp=3; IntAct=EBI-25905795, EBI-948266;
CC Q9BQS8-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-25905795, EBI-2811583;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome. Endosome.
CC Lysosome. Note=Localizes to the external but not to the internal
CC membrane of autophagosomes, and upon autophagosome/late
CC endosome/lysosome fusion, it stays on the external surface of
CC autolysosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BQS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQS8-2; Sequence=VSP_019795, VSP_019797;
CC Name=3;
CC IsoId=Q9BQS8-3; Sequence=VSP_019796, VSP_019797;
CC Name=4;
CC IsoId=Q9BQS8-4; Sequence=VSP_054477;
CC -!- TISSUE SPECIFICITY: Expressed in heart and skeletal muscle.
CC {ECO:0000269|PubMed:11896456}.
CC -!- DISEASE: Cataract 18 (CTRCT18) [MIM:610019]: An opacification of the
CC crystalline lens of the eye becoming evident at birth or in infancy. It
CC frequently results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function.
CC {ECO:0000269|PubMed:21636066}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Pathogenic mutations in
CC FYCO1 can affect intracellular transport of autophagocytic vesicles
CC from the perinuclear area to the periphery, leading to an accumulation
CC of large numbers of vesicles and hence loss of lens transparency
CC (PubMed:21636066). {ECO:0000269|PubMed:21636066,
CC ECO:0000269|PubMed:29914532}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07218.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14559.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84991.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ292348; CAC33883.1; -; mRNA.
DR EMBL; AL833308; CAD89924.1; -; mRNA.
DR EMBL; AL832358; CAD91151.1; -; mRNA.
DR EMBL; AC099782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007218; AAH07218.1; ALT_INIT; mRNA.
DR EMBL; BC101468; AAI01469.1; -; mRNA.
DR EMBL; BC101470; AAI01471.1; -; mRNA.
DR EMBL; BC143368; AAI43369.1; -; mRNA.
DR EMBL; AK023397; BAB14559.1; ALT_INIT; mRNA.
DR EMBL; AK074165; BAB84991.1; ALT_FRAME; mRNA.
DR CCDS; CCDS2734.1; -. [Q9BQS8-1]
DR RefSeq; NP_078789.2; NM_024513.3. [Q9BQS8-1]
DR RefSeq; XP_006713396.1; XM_006713333.3. [Q9BQS8-1]
DR RefSeq; XP_006713397.1; XM_006713334.3. [Q9BQS8-1]
DR RefSeq; XP_011532413.1; XM_011534111.2. [Q9BQS8-1]
DR PDB; 5CX3; X-ray; 2.30 A; E/F/G/H=1273-1298.
DR PDB; 5D94; X-ray; 1.53 A; B=1276-1288.
DR PDB; 7BQI; X-ray; 1.30 A; A=1-178.
DR PDBsum; 5CX3; -.
DR PDBsum; 5D94; -.
DR PDBsum; 7BQI; -.
DR AlphaFoldDB; Q9BQS8; -.
DR SMR; Q9BQS8; -.
DR BioGRID; 122669; 103.
DR DIP; DIP-60600N; -.
DR ELM; Q9BQS8; -.
DR IntAct; Q9BQS8; 58.
DR MINT; Q9BQS8; -.
DR STRING; 9606.ENSP00000296137; -.
DR GlyGen; Q9BQS8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BQS8; -.
DR PhosphoSitePlus; Q9BQS8; -.
DR BioMuta; FYCO1; -.
DR DMDM; 322510128; -.
DR EPD; Q9BQS8; -.
DR jPOST; Q9BQS8; -.
DR MassIVE; Q9BQS8; -.
DR MaxQB; Q9BQS8; -.
DR PaxDb; Q9BQS8; -.
DR PeptideAtlas; Q9BQS8; -.
DR PRIDE; Q9BQS8; -.
DR ProteomicsDB; 7193; -.
DR ProteomicsDB; 78718; -. [Q9BQS8-1]
DR ProteomicsDB; 78719; -. [Q9BQS8-2]
DR ProteomicsDB; 78720; -. [Q9BQS8-3]
DR Antibodypedia; 29634; 155 antibodies from 25 providers.
DR DNASU; 79443; -.
DR Ensembl; ENST00000296137.7; ENSP00000296137.2; ENSG00000163820.16. [Q9BQS8-1]
DR GeneID; 79443; -.
DR KEGG; hsa:79443; -.
DR MANE-Select; ENST00000296137.7; ENSP00000296137.2; NM_024513.4; NP_078789.2.
DR UCSC; uc003cpb.6; human. [Q9BQS8-1]
DR CTD; 79443; -.
DR DisGeNET; 79443; -.
DR GeneCards; FYCO1; -.
DR HGNC; HGNC:14673; FYCO1.
DR HPA; ENSG00000163820; Tissue enhanced (skeletal).
DR MalaCards; FYCO1; -.
DR MIM; 607182; gene.
DR MIM; 610019; phenotype.
DR neXtProt; NX_Q9BQS8; -.
DR OpenTargets; ENSG00000163820; -.
DR Orphanet; 98991; Early-onset nuclear cataract.
DR Orphanet; 98994; Total early-onset cataract.
DR PharmGKB; PA28453; -.
DR VEuPathDB; HostDB:ENSG00000163820; -.
DR eggNOG; KOG1729; Eukaryota.
DR GeneTree; ENSGT00940000154044; -.
DR HOGENOM; CLU_004445_0_0_1; -.
DR InParanoid; Q9BQS8; -.
DR OMA; ELGMSIC; -.
DR OrthoDB; 962969at2759; -.
DR PhylomeDB; Q9BQS8; -.
DR TreeFam; TF341788; -.
DR PathwayCommons; Q9BQS8; -.
DR SignaLink; Q9BQS8; -.
DR SIGNOR; Q9BQS8; -.
DR BioGRID-ORCS; 79443; 4 hits in 1077 CRISPR screens.
DR ChiTaRS; FYCO1; human.
DR GenomeRNAi; 79443; -.
DR Pharos; Q9BQS8; Tbio.
DR PRO; PR:Q9BQS8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BQS8; protein.
DR Bgee; ENSG00000163820; Expressed in skeletal muscle tissue of rectus abdominis and 198 other tissues.
DR ExpressionAtlas; Q9BQS8; baseline and differential.
DR Genevisible; Q9BQS8; HS.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; IMP:UniProtKB.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; IMP:ParkinsonsUK-UCL.
DR Gene3D; 1.20.58.900; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042654; FYCO1.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
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; PTHR23164:SF18; PTHR23164:SF18; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50866; GOLD; 1.
DR PROSITE; PS50826; RUN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cataract; Coiled coil;
KW Cytoplasmic vesicle; Disease variant; Endosome; Lysosome; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..1478
FT /note="FYVE and coiled-coil domain-containing protein 1"
FT /id="PRO_0000245837"
FT DOMAIN 36..169
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 1337..1466
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT ZN_FING 1173..1231
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 586..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..33
FT /evidence="ECO:0000255"
FT COILED 225..280
FT /evidence="ECO:0000255"
FT COILED 394..555
FT /evidence="ECO:0000255"
FT COILED 596..1151
FT /evidence="ECO:0000255"
FT COMPBIAS 1233..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 381
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDC1"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 376..380
FT /note="QQKAD -> LHVGD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019795"
FT VAR_SEQ 376..380
FT /note="QQKAD -> HLSE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019796"
FT VAR_SEQ 381..1478
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019797"
FT VAR_SEQ 1315
FT /note="Q -> QASVGASKGLGNLLCESSACR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054477"
FT VARIANT 250
FT /note="R -> Q (in dbSNP:rs4683158)"
FT /evidence="ECO:0000269|PubMed:11896456,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_027006"
FT VARIANT 270..1478
FT /note="Missing (in CTRCT18; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29914532"
FT /id="VAR_084824"
FT VARIANT 282
FT /note="R -> H (in dbSNP:rs9875356)"
FT /id="VAR_027007"
FT VARIANT 321
FT /note="G -> A (in dbSNP:rs3733100)"
FT /evidence="ECO:0000269|PubMed:11896456,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_027008"
FT VARIANT 381
FT /note="T -> M (in dbSNP:rs3733101)"
FT /id="VAR_027009"
FT VARIANT 447
FT /note="R -> C (in dbSNP:rs33910087)"
FT /id="VAR_056882"
FT VARIANT 679
FT /note="A -> V (in dbSNP:rs3796375)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_027010"
FT VARIANT 994
FT /note="E -> K (in dbSNP:rs34801630)"
FT /id="VAR_056883"
FT VARIANT 1001
FT /note="N -> D (in dbSNP:rs13059238)"
FT /id="VAR_027011"
FT VARIANT 1376
FT /note="L -> P (in CTRCT18; dbSNP:rs387906965)"
FT /evidence="ECO:0000269|PubMed:21636066"
FT /id="VAR_065974"
FT CONFLICT 155
FT /note="Y -> C (in Ref. 2; CAD91151)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="D -> G (in Ref. 2; CAD91151)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="L -> S (in Ref. 5; BAB14559)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="T -> S (in Ref. 1; CAC33883)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="T -> I (in Ref. 2; CAD89924)"
FT /evidence="ECO:0000305"
FT CONFLICT 964
FT /note="K -> E (in Ref. 2; CAD89924)"
FT /evidence="ECO:0000305"
FT CONFLICT 1382
FT /note="A -> P (in Ref. 1; CAC33883)"
FT /evidence="ECO:0000305"
FT CONFLICT 1385
FT /note="G -> A (in Ref. 1; CAC33883)"
FT /evidence="ECO:0000305"
FT HELIX 6..31
FT /evidence="ECO:0007829|PDB:7BQI"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:7BQI"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:7BQI"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:7BQI"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:7BQI"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:7BQI"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:7BQI"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:7BQI"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:7BQI"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:7BQI"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:7BQI"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:7BQI"
FT STRAND 1276..1282
FT /evidence="ECO:0007829|PDB:5CX3"
FT HELIX 1285..1287
FT /evidence="ECO:0007829|PDB:5D94"
SQ SEQUENCE 1478 AA; 166983 MW; 11AB671A9F2B3D21 CRC64;
MASTNAESQL QRIIRDLQDA VTELSKEFQE AGEPITDDST SLHKFSYKLE YLLQFDQKEK
ATLLGNKKDY WDYFCACLAK VKGANDGIRF VKSISELRTS LGKGRAFIRY SLVHQRLADT
LQQCFMNTKV TSDWYYARSP FLQPKLSSDI VGQLYELTEV QFDLASRGFD LDAAWPTFAR
RTLTTGSSAY LWKPPSRSSS MSSLVSSYLQ TQEMVSNFDL NSPLNNEALE GFDEMRLELD
QLEVREKQLR ERMQQLDREN QELRAAVSQQ GEQLQTERER GRTAAEDNVR LTCLVAELQK
QWEVTQATQN TVKELQTCLQ GLELGAAEKE EDYHTALRRL ESMLQPLAQE LEATRDSLDK
KNQHLASFPG WLAMAQQKAD TASDTKGRQE PIPSDAAQEM QELGEKLQAL ERERTKVEEV
NRQQSAQLEQ LVKELQLKED ARASLERLVK EMAPLQEELS GKGQEADQLW RRLQELLAHT
SSWEEELAEL RREKKQQQEE KELLEQEVRS LTRQLQFLET QLAQVSQHVS DLEEQKKQLI
QDKDHLSQQV GMLERLAGPP GPELPVAGEK NEALVPVNSS LQEAWGKPEE EQRGLQEAQL
DDTKVQEGSQ EEELRQANRE LEKELQNVVG RNQLLEGKLQ ALQADYQALQ QRESAIQGSL
ASLEAEQASI RHLGDQMEAS LLAVRKAKEA MKAQMAEKEA ILQSKEGECQ QLREEVEQCQ
QLAEARHREL RALESQCQQQ TQLIEVLTAE KGQQGVGPPT DNEARELAAQ LALSQAQLEV
HQGEVQRLQA QVVDLQAKMR AALDDQDKVQ SQLSMAEAVL REHKTLVQQL KEQNEALNRA
HVQELLQCSE REGALQEERA DEAQQREEEL RALQEELSQA KCSSEEAQLE HAELQEQLHR
ANTDTAELGI QVCALTVEKE RVEEALACAV QELQDAKEAA SREREGLERQ VAGLQQEKES
LQEKLKAAKA AAGSLPGLQA QLAQAEQRAQ SLQEAAHQEL NTLKFQLSAE IMDYQSRLKN
AGEECKSLRG QLEEQGRQLQ AAEEAVEKLK ATQADMGEKL SCTSNHLAEC QAAMLRKDKE
GAALREDLER TQKELEKATT KIQEYYNKLC QEVTNRERND QKMLADLDDL NRTKKYLEER
LIELLRDKDA LWQKSDALEF QQKLSAEERW LGDTEANHCL DCKREFSWMV RRHHCRICGR
IFCYYCCNNY VLSKHGGKKE RCCRACFQKL SEGPGSPDSS GSGTSQGEPS PALSPASPGP
QATGGQGANT DYRPPDDAVF DIITDEELCQ IQESGSSLPE TPTETDSLDP NAAEQDTTST
SLTPEDTEDM PVGQDSEICL LKSGELMIKV PLTVDEIASF GEGSRELFVR SSTYSLIPIT
VAEAGLTISW VFSSDPKSIS FSVVFQEAED TPLDQCKVLI PTTRCNSHKE NIQGQLKVRT
PGIYMLIFDN TFSRFVSKKV FYHLTVDRPV IYDGSDFL
