FCHO2_PONAB
ID FCHO2_PONAB Reviewed; 810 AA.
AC Q5R807;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=F-BAR domain only protein 2;
GN Name=FCHO2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions in an early step of clathrin-mediated endocytosis.
CC Has both a membrane binding/bending activity and the ability to recruit
CC proteins essential to the formation of functional clathrin-coated pits.
CC Has a lipid-binding activity with a preference for membranes enriched
CC in phosphatidylserine and phosphoinositides (Pi(4,5) biphosphate) like
CC the plasma membrane. Its membrane-bending activity might be important
CC for the subsequent action of clathrin and adaptors in the formation of
CC clathrin-coated vesicles. Involved in adaptor protein complex AP-2-
CC dependent endocytosis of the transferrin receptor, it also functions in
CC the AP-2-independent endocytosis of the LDL receptor (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. May form homotetramer. Interacts
CC with AP2A1. Interacts with EPS15, EPS15R, ITSN1 and ITSN2; recruit
CC those scaffolding proteins which in turn may interact with the adaptor
CC protein complex AP-2 at the plasma membrane. Interacts with DAB2 (via
CC DPF motifs); mediates LDL receptor/LDLR endocytosis (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=Associated with forming but not mature clathrin-
CC coated vesicles. The recruitment to coated-pits precede the one of
CC clathrin and the adaptor protein complex AP-2 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Mainly undergoes monoubiquitination but also
CC polyubiquitination (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FCHO family. {ECO:0000305}.
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DR EMBL; CR859949; CAH92103.1; -; mRNA.
DR RefSeq; NP_001126228.1; NM_001132756.1.
DR AlphaFoldDB; Q5R807; -.
DR SMR; Q5R807; -.
DR STRING; 9601.ENSPPYP00000017377; -.
DR GeneID; 100173197; -.
DR KEGG; pon:100173197; -.
DR CTD; 115548; -.
DR eggNOG; KOG2398; Eukaryota.
DR InParanoid; Q5R807; -.
DR OrthoDB; 638761at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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: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 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; 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 PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51072; MHD; 1.
PE 2: Evidence at transcript level;
KW Coated pit; Coiled coil; Disulfide bond; Endocytosis; Isopeptide bond;
KW Membrane; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..810
FT /note="F-BAR domain only protein 2"
FT /id="PRO_0000266007"
FT DOMAIN 3..250
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 542..809
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 3..274
FT /note="Mediates dimerization and binding to membranes
FT enriched in Pi(4,5)-P2 and induces their tubulation"
FT /evidence="ECO:0000250"
FT REGION 301..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..810
FT /note="Mediates interaction with DAB2, EPS15, EPS15R and
FT ITSN1"
FT /evidence="ECO:0000250"
FT COILED 87..156
FT /evidence="ECO:0000255"
FT COMPBIAS 403..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQN2"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQN2"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UQN2"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
FT DISULFID 147
FT /note="Interchain (with C-273)"
FT /evidence="ECO:0000250"
FT DISULFID 273
FT /note="Interchain (with C-147)"
FT /evidence="ECO:0000250"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q0JRZ9"
SQ SEQUENCE 810 AA; 88984 MW; D06374C7DB75EFD3 CRC64;
MVMAYFVENF WGEKNSGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS RSMTKLAKSA
SNYSQLGTFA PVWDVFKTST EKLANCHLDL VRKLQELIKE VQKYGEEQVK SHKKTKEEVA
GTLEAVQTIQ STTQALQKSK ENYNAKCVEQ ERLKKEGATQ REIEKAAVKS KKATDTYKLY
VEKYALAKAD FEQKMTETAQ KFQDIEETHL IHIKEVIGSL SNAIKEIHLQ IGQVHEEFIN
NMANTTVESL IQKFAESKGT GKERPGLIEF EECDTASAVE GIKPRKRKTF ALPGIIKKEK
DAESVECPDA DSLNIPDVDE EGYSIKPETN QNDTKENHFY SSSDSDSEDE EPKKYRIEIK
PMHPNNSHHT MASLDELRVS IGNITLSPAI SRHSPVQMNR NLSNEELTKS KPSAPPNERG
TSDLLAWDPL FGPSLDSSSS SSLTSSSSAR PTTPLSVGTI VPPPRPASRP KLTSGKLSGI
NEIPRPFSPP VTSNTSPPPA APLARAESSS SISSSASLSA ANTPTVGVSR GPSPVSLGNQ
DTLPVAVALT ESVNAYFKGA DPTKCIVKIT GDMTMSFPSG IIKVFTSNPT PAVLCFRVKN
ISRLEQILPN AQLVFSDPSQ CDSNTKDFWM NMQAVTVYLK KLSEQNPAAS YYNVDVLKYQ
VSSNGIQSTP LNLATYWKCS ASTTDLRVDY KYNPEAMVAP SVLSNIQVVV PVDGGVMNMQ
SLPPAIWNAE QMKAFWKLSS ISEKSENGGS GSLRAKFDLS EGPSKPTTLA VQFLSEGSTL
SGVDFELVGT GYRLSLIKKR FATGRYLADC
