ID A0A091JHB1_EGRGA Unreviewed; 545 AA.
AC A0A091JHB1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Formin-binding protein 1 {ECO:0000313|EMBL:KFP19288.1};
DE Flags: Fragment;
GN ORFNames=Z169_11677 {ECO:0000313|EMBL:KFP19288.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP19288.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP19288.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP19288.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}.
CC -!- SIMILARITY: Belongs to the FNBP1 family.
CC {ECO:0000256|ARBA:ARBA00009426}.
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DR EMBL; KK501991; KFP19288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091JHB1; -.
DR STRING; 188379.A0A091JHB1; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07676; F-BAR_FBP17; 1.
DR CDD; cd11629; HR1_FBP17; 1.
DR Gene3D; 6.10.140.470; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR037449; FNBP1_F-BAR.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF13; FORMIN-BINDING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..258
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 332..409
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 478..539
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 287..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..180
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 339..399
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 424..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP19288.1"
FT NON_TER 545
FT /evidence="ECO:0000313|EMBL:KFP19288.1"
SQ SEQUENCE 545 AA; 63185 MW; 95488C5C3E5A2C7C CRC64;
LQDQFDNLEK HTQWGIDVLE KYIKFVKERT EIELSYAKQL RNLSKKYQPK KNSKEEEEYR
YTSTRAFLAT LNEMNDYAGQ HEVISENMTS LITGELTRYV QELKQERKSH FHDGRKAQQH
IETCWKQLEA SKRRFERDCK EADRAQQYFE KMDADINVTK ADVEKARQQA QLRHQMAEDS
KAEYSSTLQK FNSEQHDHYY THIPNIFQKI QEMEERRIVR IGESMKTFAE VDRQVIPIIG
KCLDEITKAA ESIDHKNDSQ LVIEAFKSGF EPPGDVDFED FTQPMKRTVS ESSLSNSRGD
GKSELKFGGK SKGKLWPFIK KNKGAGPEDF SNLPPEQRRK KLQQKVDELN KDIQKEMDQR
DALTKMKDVY IKNPQMGDAA SVDHRLAELG QNIEKLRLEV QKFEGWLAEV EGRLPMRTEQ
ARRQSGLYEA QNTSAVNSCA QDRESPDGSY TEEQSQETEM KVPATDFDDE FDDEEPLPTI
GTCKALYTFE GQNEGTISVA EGEMLYVIEE DKGDGWTRIR RNEDEEGYVP TSYVEVYLDK
NAKGA
//
