GenomeNet

Database: UniProt
Entry: FCHO1_DANRE
LinkDB: FCHO1_DANRE
Original site: FCHO1_DANRE 
ID   FCHO1_DANRE             Reviewed;         897 AA.
AC   E7FBF7;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   25-APR-2018, entry version 38.
DE   RecName: Full=F-BAR domain only protein 1;
GN   Name=fcho1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   FUNCTION IN BMP SIGNALING, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP   ACVR1L.
RX   PubMed=22484487; DOI=10.1038/ncb2473;
RA   Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA   Tsang M., Traub L.M.;
RT   "Distinct and separable activities of the endocytic clathrin-coat
RT   components Fcho1/2 and AP-2 in developmental patterning.";
RL   Nat. Cell Biol. 14:488-501(2012).
CC   -!- FUNCTION: May function in an early step of clathrin-mediated
CC       endocytosis. May regulate Bmp signaling by regulating clathrin-
CC       mediated endocytosis of Bmp receptors.
CC       {ECO:0000269|PubMed:22484487}.
CC   -!- SUBUNIT: May oligomerize and form homotetramer (By similarity).
CC       Interacts with acvr1l/alk8; linking this receptor to clathrin-
CC       mediated endocytosis. {ECO:0000250, ECO:0000269|PubMed:22484487}.
CC   -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Embryos display dorsoventral patterning
CC       defects analogous to the one associated with Bmp signal failure.
CC       {ECO:0000269|PubMed:22484487}.
CC   -!- SIMILARITY: Belongs to the FCHO family. {ECO:0000305}.
DR   EMBL; CR450804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   UniGene; Dr.162336; -.
DR   SMR; E7FBF7; -.
DR   STRING; 7955.ENSDARP00000033648; -.
DR   PaxDb; E7FBF7; -.
DR   PRIDE; E7FBF7; -.
DR   ZFIN; ZDB-GENE-120613-1; fcho1.
DR   eggNOG; KOG2398; Eukaryota.
DR   eggNOG; ENOG410Y7RY; LUCA.
DR   InParanoid; E7FBF7; -.
DR   PRO; PR:E7FBF7; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR   GO; GO:0030509; P:BMP signaling pathway; IGI:ZFIN.
DR   GO; GO:0048268; P:clathrin coat assembly; ISS:UniProtKB.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR030121; FCHo1.
DR   InterPro; IPR028565; MHD.
DR   InterPro; IPR018808; Muniscin_C.
DR   PANTHER; PTHR23065:SF6; PTHR23065:SF6; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF10291; muHD; 1.
DR   SMART; SM00055; FCH; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS51072; MHD; 1.
PE   1: Evidence at protein level;
KW   Coated pit; Coiled coil; Complete proteome; Endocytosis; Membrane;
KW   Reference proteome.
FT   CHAIN         1    897       F-BAR domain only protein 1.
FT                                /FTId=PRO_0000417673.
FT   DOMAIN        2    248       F-BAR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01077}.
FT   DOMAIN      630    894       MHD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00404}.
FT   REGION        1    276       Mediates membrane-binding. {ECO:0000250}.
FT   COILED      134    154       {ECO:0000255}.
SQ   SEQUENCE   897 AA;  99110 MW;  A022631EFBB23343 CRC64;
     MIHFFHTLQG EKNAGFDVLY HNMKHGQIAT KELAEFVRER AAIEETYSKS MSKLAKMASN
     GSPLGTFAPM WDVFRVSSDK LALCHLELMR KMNDLIRDIN KYSDEQVKIH RKTKEEAIGT
     LESVQSLQVQ NGHLQKTREG YHSKCVELER LRKEGVPQKE LEKAELKCKK AAESFAGSIE
     KFNRAGGDFE QKMSESAQKF QDIEEAHLRQ MKLLIKGYSH SIEDTHVQVG QVHEEFKQNV
     ENIGIENLIQ KFTEQKGTGK ERPEGPVGFE EYLSSLASEN SKKSRAKAFR IPGLGKRDKE
     PDSTVHVYFL QNNSPLEVDD EGFVIRADVK QNDIEKEGNF YSSDSDFDDE EPKKFHIQIR
     PVASSNRSNS AANEQELKAT VGALTLPPNR VVSVKKQLSR RSEGEGESVP QRVIAKVEVC
     ACRLSSTASG SDALFGPPLE SAFKSHSFSG REQLQNAFAA SEFFSKFYSS SLENVEDSGL
     DSPSHQPLGV SPDPTGWAAW PSSQSQSKDS INAASQSRGG SNRPTPSPNP APSSQSNTEW
     MNDIIREGPY SQIMQDSSER LALAPPRSVR SKRSSVAITR KNSDFSRSLC SSPLPDPNAS
     TCVLYSKMLN CAPAGLSRGP SPISLSAQES WPVAAAITEY INAYFRGGEH NRCLVKITGD
     LTMSFPAGIT RIFTANPNAP VLSFRLVNIS RVDHFLPNQK LLYSDPSQSD PDTKDFWFNM
     QALTLHLQRE AELNPQASYY NVALLKYQAS SQDPSRAPLL LSAECQRSGT VTRVSLDYHC
     CPATAPATQL TSVQVLLPLD HSATDLQCQP PAAWNAEERR LLWKLDDLSS VSGSGTLCAS
     WQCLEVPRGP APSLAVQFVG SGASLSGLDV ELVGSRYRMS LVKKRFATGK YMAGCSL
//
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