ID   FCHO2_DANRE             Reviewed;         848 AA.
AC   Q502I9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=F-BAR domain only protein 2;
GN   Name=fcho2; ORFNames=zgc:112167;
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 MRNA].
RC   TISSUE=Larva;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function in an early step of clathrin-mediated
CC       endocytosis. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FCHO family. {ECO:0000305}.
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DR   EMBL; BC095680; AAH95680.1; -; mRNA.
DR   RefSeq; NP_001018617.1; NM_001020781.1.
DR   AlphaFoldDB; Q502I9; -.
DR   SMR; Q502I9; -.
DR   STRING; 7955.ENSDARP00000051270; -.
DR   PaxDb; Q502I9; -.
DR   PRIDE; Q502I9; -.
DR   GeneID; 553949; -.
DR   KEGG; dre:553949; -.
DR   CTD; 115548; -.
DR   ZFIN; ZDB-GENE-050522-228; fcho2.
DR   eggNOG; KOG2398; Eukaryota.
DR   InParanoid; Q502I9; -.
DR   OrthoDB; 638761at2759; -.
DR   PhylomeDB; Q502I9; -.
DR   Reactome; R-DRE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-DRE-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q502I9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR   GO; GO:0043009; P:chordate embryonic development; IMP:ZFIN.
DR   GO; GO:0048268; P:clathrin coat assembly; ISS:UniProtKB.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR   GO; GO:0010324; P:membrane invagination; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR036168; AP2_Mu_C_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR030122; FCHo2.
DR   InterPro; IPR028565; MHD.
DR   InterPro; IPR018808; Muniscin_C.
DR   PANTHER; PTHR23065:SF8; PTHR23065:SF8; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF10291; muHD; 1.
DR   SMART; SM00055; FCH; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF49447; SSF49447; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS51072; MHD; 1.
PE   2: Evidence at transcript level;
KW   Coated pit; Coiled coil; Endocytosis; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..848
FT                   /note="F-BAR domain only protein 2"
FT                   /id="PRO_0000266008"
FT   DOMAIN          4..250
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          580..848
FT                   /note="MHD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT   REGION          292..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          87..114
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        292..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..486
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   848 AA;  93657 MW;  9C1A429C396DEA1F CRC64;
     MITPYFLENF WGNKNSGFYV LYHNMKHGQI SSKELSDFIR ERATIEEAYS RSMTKLAKTA
     SNFSQLGTFA PVWDVFKQST EKLAACHMEL VRKLQELIKE VQKYVDEQAK NHKKTKEEVA
     STLEAVHNIQ SVSQALLKSK ENYINKTLEQ ERMRKEGAKQ GDLDKAGLKV KKATESYKSY
     VEKYATAKTE FEQRMTETAQ KFQGIEEEHI LRMQEIIHSY SLSVEETHIQ IGEVQQEFVN
     NMENTSVESL IEKLAESRGT GKERPGPIEF EECNVSIATE GAKPRKRKTF AIPGRRKEKD
     TDSTESTEVE AVNASNGAPP GFYGAIDLHN ANVPQLDDEG FCIRPEVNEN DAKENSFYSS
     SDSEDEDEPR KFHVQIKPVQ TNNGTHQHKV TIDELKASIG NISLSPTPAV HMKRNQSNDE
     LARPKIPQPP LNDRFSSNDL LSLDPFGPTS TGSSSSLPQS SVPPPNRPTT PLGTSSIVPP
     PRPLSRPKLA TGKLTGITES GRPFSPPKLL NSSPPPPAAP LARAESFSSL SSNTSLSASN
     TPTVEDDVFV GKLPTFEKRC ETPAGTSRGP SPVTLASQDA LPIAVAFTES VNAYFKGADP
     SKCIVKITGD MTLSFPSGII KIFTSSPSPA VLSFKLLNAS RLEQIMPNQQ LLHSDSSQSD
     TNTKDFWMNM PALTSFLRKS SEQNPAASYY NVDILKYQVC SNGIQSTPLN LVVYWKCSRS
     TTDLRVDYRY NPEAMQPPAP LTNVQVLVPV NGGVMNMQSL PNAIWNAEQN KSLWKLSDIS
     DKSENEGSGS LRAKFELSEG PSIPATLAVQ FFSEGSSLSG VDMELAGSGY RLSLNKKRFA
     TGRYMADC