ID   A0A2K6FM56_PROCO        Unreviewed;       776 AA.
AC   A0A2K6FM56;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=F-BAR domain only protein 2 {ECO:0000256|ARBA:ARBA00018998};
GN   Name=FCHO2 {ECO:0000313|Ensembl:ENSPCOP00000015046.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000015046.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000015046.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC       {ECO:0000256|ARBA:ARBA00004283}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004283}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004283}.
CC   -!- SIMILARITY: Belongs to the FCHO family.
CC       {ECO:0000256|ARBA:ARBA00011064}.
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DR   RefSeq; XP_012520083.1; XM_012664629.1.
DR   AlphaFoldDB; A0A2K6FM56; -.
DR   STRING; 379532.ENSPCOP00000015046; -.
DR   Ensembl; ENSPCOT00000025658.1; ENSPCOP00000015046.1; ENSPCOG00000019242.1.
DR   GeneID; 105826636; -.
DR   KEGG; pcoq:105826636; -.
DR   CTD; 115548; -.
DR   GeneTree; ENSGT00940000157105; -.
DR   OMA; ANHSTEM; -.
DR   OrthoDB; 2996449at2759; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR   GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl.
DR   GO; GO:0048268; P:clathrin coat assembly; IEA:Ensembl.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:Ensembl.
DR   GO; GO:0010324; P:membrane invagination; IEA:Ensembl.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
DR   CDD; cd07673; F-BAR_FCHO2; 1.
DR   CDD; cd09267; FCHo2_MHD; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR030122; FCHo2_F-BAR.
DR   InterPro; IPR028565; MHD.
DR   InterPro; IPR018808; Muniscin_C.
DR   PANTHER; PTHR23065:SF8; F-BAR DOMAIN ONLY PROTEIN 2; 1.
DR   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF10291; muHD; 1.
DR   SMART; SM00055; FCH; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS51072; MHD; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT   DOMAIN          3..254
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          508..775
FT                   /note="MHD"
FT                   /evidence="ECO:0000259|PROSITE:PS51072"
FT   REGION          268..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   776 AA;  84857 MW;  BD38C838A68546D1 CRC64;
     MVMAYFVENF WGEKNSGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS RSMTKLAKSA
     SNYSQLGTFA PVWDVFRTST EKLANCHLDL VRKLQELIKE VQKYGEEQVK SHKKTKEEVA
     GTLEAVQTIQ SITQALQKAK ENYNAKCVEQ ERLKKEGATQ REIEKAAVKS KKATDTYKLY
     VEKYALAKAD FEQKMTETAQ VHEEFINNMA NTTVESLIQK FAESKGTGKE RPGLIEFEEC
     DPASAVEGMK PRRRKPFALS GIIKKEKDAE SVECPDADSL NIPDVDEEGY SIKPEANQND
     TKENHFYSSS DSDSEDEEPK KYRIEIKPVH PNNSHHTMAS LDELKVSIGN ITLSPAISRH
     SPVQMNRNSS NEELKSKPSA VPNEKGTSDL LAWDPLFGPS LDSSSSSSLT SSSSARPTTP
     LSVGTIVPPP RPASRPKLTS GKLSGINEIP RPFSPPITSN TSPPPAAPLA RAESSSSISS
     SASLSAANTP TVGVSRGPSP VSLGNQDTLP VAVALTESVN AYFKGADPTK CIVKITGDMT
     ISFPSGVIKV FTSNPSPAVL CFRVKNISRL EQILPNAQLV FSDPSQCDSN TKDFWMNMQA
     VTVYLKKLSE QNPAASYYNV DVLKYQVSAN GIQSTPLNLA TYWKCSASTT DLRVDYKYNP
     EAMVAPTVLS NIQVVVPVDG GVTNMQSLPP AIWNAEQMKA FWKLSGISEK SENGGSGSLR
     AKFDLSEGPG KPTTLAVQFL SEGSTLSGID VELVGTGYRL SLVKKRFATG RYLADC
//