FYCO1_MOUSE
ID FYCO1_MOUSE Reviewed; 1437 AA.
AC Q8VDC1; Q3V385; Q7TMT0; Q8BJN2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=FYVE and coiled-coil domain-containing protein 1;
GN Name=Fyco1;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=12461651; DOI=10.1007/s00335-002-3037-y;
RA Kiss H., Darai E., Kiss C., Kost-Alimova M., Klein G., Dumanski J.P.,
RA Imreh S.;
RT "Comparative human/murine sequence analysis of the common eliminated region
RT 1 from human 3p21.3.";
RL Mamm. Genome 13:646-655(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-866.
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-366 AND 827-1437.
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum, and Retina;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [7]
RP TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: May mediate microtubule plus end-directed vesicle transport.
CC {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000250}.
CC Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Note=Localizes to the
CC external but not to the internal membrane of autophagosomes, and upon
CC autophagosome/late endosome/lysosome fusion, it stays on the external
CC surface of autolysosomes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart and testis. Expressed in the eye
CC lens. {ECO:0000269|PubMed:12461651, ECO:0000269|PubMed:21636066}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53712.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AJ428065; CAD20987.1; -; mRNA.
DR EMBL; BC053712; AAH53712.1; ALT_SEQ; mRNA.
DR EMBL; AK081259; BAC38178.2; -; mRNA.
DR EMBL; AK044587; BAE43322.1; -; mRNA.
DR CCDS; CCDS40819.1; -.
DR RefSeq; NP_001103723.2; NM_001110253.2.
DR RefSeq; NP_683727.3; NM_148925.3.
DR RefSeq; XP_017168648.1; XM_017313159.1.
DR PDB; 5WRD; X-ray; 1.90 A; C/D=1235-1253.
DR PDBsum; 5WRD; -.
DR AlphaFoldDB; Q8VDC1; -.
DR SMR; Q8VDC1; -.
DR BioGRID; 201392; 10.
DR IntAct; Q8VDC1; 5.
DR STRING; 10090.ENSMUSP00000081764; -.
DR iPTMnet; Q8VDC1; -.
DR PhosphoSitePlus; Q8VDC1; -.
DR SwissPalm; Q8VDC1; -.
DR EPD; Q8VDC1; -.
DR jPOST; Q8VDC1; -.
DR MaxQB; Q8VDC1; -.
DR PaxDb; Q8VDC1; -.
DR PeptideAtlas; Q8VDC1; -.
DR PRIDE; Q8VDC1; -.
DR ProteomicsDB; 267548; -.
DR Antibodypedia; 29634; 155 antibodies from 25 providers.
DR DNASU; 17281; -.
DR Ensembl; ENSMUST00000084715; ENSMUSP00000081764; ENSMUSG00000025241.
DR Ensembl; ENSMUST00000167595; ENSMUSP00000133222; ENSMUSG00000025241.
DR GeneID; 17281; -.
DR KEGG; mmu:17281; -.
DR UCSC; uc029xgt.2; mouse.
DR CTD; 79443; -.
DR MGI; MGI:107277; Fyco1.
DR VEuPathDB; HostDB:ENSMUSG00000025241; -.
DR eggNOG; KOG1729; Eukaryota.
DR GeneTree; ENSGT00940000154044; -.
DR HOGENOM; CLU_004445_0_0_1; -.
DR InParanoid; Q8VDC1; -.
DR OMA; ELGMSIC; -.
DR OrthoDB; 962969at2759; -.
DR PhylomeDB; Q8VDC1; -.
DR TreeFam; TF341788; -.
DR BioGRID-ORCS; 17281; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Fyco1; mouse.
DR PRO; PR:Q8VDC1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VDC1; protein.
DR Bgee; ENSMUSG00000025241; Expressed in soleus muscle and 233 other tissues.
DR ExpressionAtlas; Q8VDC1; baseline and differential.
DR Genevisible; Q8VDC1; MM.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; ISS:UniProtKB.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; ISO:MGI.
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; 2.
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; Coiled coil; Cytoplasmic vesicle; Endosome;
KW Lysosome; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BQS8"
FT CHAIN 2..1437
FT /note="FYVE and coiled-coil domain-containing protein 1"
FT /id="PRO_0000245838"
FT DOMAIN 36..169
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 1296..1425
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT ZN_FING 1132..1190
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1191..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..30
FT /evidence="ECO:0000255"
FT COILED 223..270
FT /evidence="ECO:0000255"
FT COILED 305..846
FT /evidence="ECO:0000255"
FT COILED 873..1110
FT /evidence="ECO:0000255"
FT COMPBIAS 1253..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1165
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1185
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:0000250|UniProtKB:Q9BQS8"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQS8"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQS8"
FT CONFLICT 19
FT /note="D -> V (in Ref. 2; AAH53712)"
FT /evidence="ECO:0000305"
FT HELIX 1244..1252
FT /evidence="ECO:0007829|PDB:5WRD"
SQ SEQUENCE 1437 AA; 162336 MW; 2AD12D8E10C54F61 CRC64;
MASSSTETQL QRIIRDLQDA ATELSHEFKE GGEPITDDST SLHKFSYKLE YLLQFDQKEK
ASLLGSKKDY WDYFCACLAK VKGANDGIRF VRSISELRTS LGKGRAFIRY SLVHQRLADT
LQQCFMNTKV TSDWYYARSP FLKPKLSSDI VGQLYELTEV QFDLAPRGYD LDAAWPTFAR
RTLATSTSAY MWKPPSRSSS MSSLVSNYLQ TQEMASSLDL NCSLNNEALE SFDEMRLELD
QLEVREKQLQ ERVQQLDREN QALRMLVSRQ GGQLQVEKEM GYLAVEDSIG LVSLVAELQK
QGDVSQATVK KLQSCLQALE LNVDKKEYSP SALQLENMAK ELDTVRGSLG RENQLLASLS
ERLARAEKGE KTPPDTELHQ EPVPADLVLK FQELKGKLQA LEGENTEAQE LNRQQSIKLE
QLAKELQLKE EARASLAHLV KDVVPLQEEL SGKKQESAQL RRQLQESLAH LSSVEEELAE
ARQQEKQHRE EKQLLEQEAT SLTWQLQLLE TQLGQVSQLV SDLEEQKKQL MQERDHLSQR
VGTLEQLAEV HGPPQSAEMP EKRQQCLREE QVNNSTVSEA EQEELQKELQ NMVDRNQLLE
GKLQALQTDY KALQQREAAI QGSLASLEAE QASIRHLGNQ MEASLLAVKK AKETMKAQVA
EKEAALQSKE SECQRLQEEA DQCRLQAEAQ AQELRALENQ CQQQIQLIEV LSAEKGQQGL
SLPQVNTDQL ALSQAQLEIH QGEAQRLQNE VVDLQAKLQV ALGDRDKLQS QLGVAETVLR
EHKTLVQQLK EQNEALNRAH VQELLQCSER EGILQEESIY KAQKQEQELR ALQAELSQVR
CSSEGAHLEH AELQDQLHRA NTDTAELGIQ VCALTAEKDR MEEALASLAQ ELQDSKEAAL
QERKGLELQV MQLQQEKEKL QEKVKAAEEA ASSFSGLQAQ LAQAEQLAQS LQETAHQEQD
ALKFQLSAEI MDHQNRLKTA NEECGHLRAQ LEEQGQQLQM TKEAVQELEI TKAAMEEKLN
CTSSHLAECQ ATLLRKDEES TMLQTSLERT QKELEKATSK IQEYYNKLCQ EVTNRERNDQ
KMLADLDDLN RTKKYLEERL IELLRDKDAL WQKSDALEFQ QKLSAEEKCL GDMEVNHCHD
CKREFSWIVR RHHCRICGRI FCYYCCNNYV VTKPSGKKER CCRACFQKFG EGSGSNDSSG
SGTSQGEPSP MVSPAEASPQ SIGSQGINSV CRPPDDAVFD IITDEELCQI QESGSSLPET
PTETDSMDPN TAEQDTTSNS LTPEDTEDVP MGQDAEICLL KSGELMIKLP LTVEEVASFG
EGSRELFVRS STYSLITITV AEPGLTISWV FSSDPKSISF SVVFQETEDT PLDQCKVLIP
TTRCNSHKEN IRGQLKVRIP GIYLLIFDNT FSRFISKKVL YHLTVDRPVI YDGSDFP
