ID H0WUB7_OTOGA Unreviewed; 882 AA.
AC H0WUB7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=FCH and mu domain containing endocytic adaptor 1 {ECO:0000313|Ensembl:ENSOGAP00000005811.2};
GN Name=FCHO1 {ECO:0000313|Ensembl:ENSOGAP00000005811.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000005811.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000005811.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AAQR03128756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03128757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WUB7; -.
DR STRING; 30611.ENSOGAP00000005811; -.
DR Ensembl; ENSOGAT00000006502.2; ENSOGAP00000005811.2; ENSOGAG00000006490.2.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000160489; -.
DR HOGENOM; CLU_007107_0_0_1; -.
DR InParanoid; H0WUB7; -.
DR OMA; TDSAVMD; -.
DR TreeFam; TF328986; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0035612; F:AP-2 adaptor complex 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:0050870; P:positive regulation of T cell activation; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR CDD; cd07674; F-BAR_FCHO1; 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; IPR042735; FCHo1_F-BAR.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR PANTHER; PTHR23065:SF6; F-BAR DOMAIN ONLY PROTEIN 1; 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, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225}.
FT DOMAIN 1..248
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 624..882
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 292..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..192
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 411..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..530
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 96039 MW; 2E3D6A1E4879141E CRC64;
MSYFGEHFWG EKNHGFEVLY HSVKQGPIST KELADFIRER ATIEETYSKA MAKLSKLASN
GTPVGTFAPL WEVFRVSSDK LALCHLELTR KLQDLIKDVL RYGDEQLKTH KKCKEEVMGT
VDAVQVLAGV SQLLPKSREN YLNRCMDQER LRRESTSQKE MDKAETKTKK AAENLRRSVE
KYNSARADFE QKMLDSALRF QAIEETHLRH MKALLGSYAH SVEDTHVQIG QVHEEFKQNI
ENISVEMLLR KFAESKGTGQ EKPGPLDFEA YSAAALQEMK RLRGAKAFRL PGLSRREREP
EPHAAADFLE PSSGTCPEVD EEGFTVRPDL GVLRTAEPSR FSSSDSDFDD EEPRKFYVHI
KPAPARAPAC SPEAAAAQLR ATAGSLILPP GPGGTMKRHS SRDTAGKPQR PRSAPRTSSC
AEKVQSDEQV AKNLFGPPLE SAFDHEDFTG SSSLGFTSSP SPFSSSSPEN VEDSGLDSPS
HAAPGPSPDS WVPRPGTPQS PPNCRAPHPE SRGTRVVPPP DSPQPLAPSP GPWGLEALAG
GDLMPTPADS TAQDGLAAPT RRPRSRKVSC PLTRSNGNLS RSLSPSPLGS SAPSSAPERP
SFSSQTGHGV SRGPSPVVLG SQDALPVATA FTEYVHAYFR GHSPSCLARV TGELTMTFPA
GIVRVFSGTP PPPVLSFRLV HMTPIEHFQP NADLLFSDPS QSDPETKDFW LNMAALTEAL
QRQAEQNPAA SYYNVVLLRY QFSRPGPQSV PLQLSAHWQC GTTLTQVSVE YSYRPGATAV
PTPLTNVQIL LPVGEPVTNV RLQPAATWNL EEKRLMWKLP DVSEAGGSGR LSASWEPLSG
PSTPSPVAAQ FTSEGATLSG VDLELVGSGY RMSLVKRRFA TG
//
