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   24-JAN-2024, entry version 173.
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; PRO_0000449630 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-2869338, EBI-25475888;
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.
DR   RefSeq; XP_006713397.1; XM_006713334.3.
DR   RefSeq; XP_011532413.1; XM_011534111.2.
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; 111.
DR   DIP; DIP-60600N; -.
DR   ELM; Q9BQS8; -.
DR   IntAct; Q9BQS8; 60.
DR   MINT; Q9BQS8; -.
DR   STRING; 9606.ENSP00000296137; -.
DR   TCDB; 9.B.17.2.4; the vamp-associated protein (vap) family.
DR   GlyGen; Q9BQS8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BQS8; -.
DR   PhosphoSitePlus; Q9BQS8; -.
DR   SwissPalm; Q9BQS8; -.
DR   BioMuta; FYCO1; -.
DR   DMDM; 322510128; -.
DR   EPD; Q9BQS8; -.
DR   jPOST; Q9BQS8; -.
DR   MassIVE; Q9BQS8; -.
DR   MaxQB; Q9BQS8; -.
DR   PaxDb; 9606-ENSP00000296137; -.
DR   PeptideAtlas; Q9BQS8; -.
DR   ProteomicsDB; 7193; -.
DR   ProteomicsDB; 78718; -. [Q9BQS8-1]
DR   ProteomicsDB; 78719; -. [Q9BQS8-2]
DR   ProteomicsDB; 78720; -. [Q9BQS8-3]
DR   Pumba; Q9BQS8; -.
DR   Antibodypedia; 29634; 175 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   AGR; HGNC:14673; -.
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; 5394846at2759; -.
DR   PhylomeDB; Q9BQS8; -.
DR   TreeFam; TF341788; -.
DR   PathwayCommons; Q9BQS8; -.
DR   SignaLink; Q9BQS8; -.
DR   SIGNOR; Q9BQS8; -.
DR   BioGRID-ORCS; 79443; 4 hits in 1157 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 200 other cell types or tissues.
DR   ExpressionAtlas; Q9BQS8; baseline and differential.
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   CDD; cd15726; FYVE_FYCO1; 1.
DR   CDD; cd17698; RUN_FYCO1; 1.
DR   Gene3D; 1.20.58.900; -; 1.
DR   Gene3D; 2.60.120.680; GOLD domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047337; FYVE_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; IPR047336; RUN_FYCO1.
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; PTHR46753; FYVE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46753:SF2; FYVE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF02759; RUN; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF140741; RUN domain-like; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR   PROSITE; PS50866; GOLD; 1.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   Genevisible; Q9BQS8; HS.
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; uncertain 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
//