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 03-AUG-2022, entry version 50.
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 Danionidae; Danioninae; 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., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., 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., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., 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., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT 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-mediated
CC endocytosis of Bmp receptors. {ECO:0000269|PubMed:22484487}.
CC -!- SUBUNIT: May oligomerize and form homotetramer (By similarity).
CC Interacts with acvr1l/alk8; linking this receptor to clathrin-mediated
CC 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 defects
CC analogous to the one associated with Bmp signal failure.
CC {ECO:0000269|PubMed:22484487}.
CC -!- SIMILARITY: Belongs to the FCHO family. {ECO:0000305}.
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DR EMBL; CR450804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E7FBF7; -.
DR SMR; E7FBF7; -.
DR STRING; 7955.ENSDARP00000033648; -.
DR PaxDb; E7FBF7; -.
DR ZFIN; ZDB-GENE-120613-1; fcho1.
DR eggNOG; KOG2398; Eukaryota.
DR InParanoid; E7FBF7; -.
DR PRO; PR:E7FBF7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 CDD; cd07674; F-BAR_FCHO1; 1.
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; IPR042735; FCHo1_F-BAR.
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; Endocytosis; Membrane; Reference proteome.
FT CHAIN 1..897
FT /note="F-BAR domain only protein 1"
FT /id="PRO_0000417673"
FT DOMAIN 2..248
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 630..894
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 1..276
FT /note="Mediates membrane-binding"
FT /evidence="ECO:0000250"
FT REGION 475..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..154
FT /evidence="ECO:0000255"
FT COMPBIAS 475..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
