ID A0A3B3XFM3_9TELE Unreviewed; 568 AA.
AC A0A3B3XFM3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Formin binding protein 1b {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000013842.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000013842.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B3XFM3; -.
DR Ensembl; ENSPMET00000032368.1; ENSPMEP00000013842.1; ENSPMEG00000016218.1.
DR Proteomes; UP000261480; Unplaced.
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 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; 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 SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 6..270
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 342..419
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 501..562
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 301..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..376
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 435..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 65735 MW; 634EC10146C50B87 CRC64;
MDKIETLIKE QQLKDQFDNL EKHTQWGIEF VEKYNKFVKE RSEIEINYAK QIRNLSKKYQ
PKKNSREEEE SKYSFCRAFF TTLNELNDYA GQHEVIAENL TSQIFVELTR YLQELKAERK
THFHDGRKAQ QYIESSWKQL ESCKRRFERD CKEADRAQQY FEKMDADINV TKADVEKARQ
QAQMRHQMAS DSKGDYSSYL QKFNQEQNDH YHTIIPNIFQ KLQDMEEKRI ERIGACMKAF
AEVDRQVLPI VGKCLDGMTT AAESIEPKTD SQQVVESYKS GFEPPSDVEF EDYGQAMKRT
VSENSLSNAK EGKEKPAGKS KPKLWPFIKN KNKGSGPEDF SHLPPEQRRK KLQGKIDDLN
KDIHKEMDQR DALTKMKDVY IKNPQMGDPT SVDPRLTEIA QNIEKLQAEV QKFEGWLAEV
EERMPSKSDS HRRSGLYETQ SNIAVSNNCA QDRESPDGSY TEEQNTETQV KANINPTPNP
NTIPTTMPDD EEFDDDDEPL ATIGTCKALY PFEGHNEGTI AVAEGELLYV IEEDKGDGWT
RVRRNQDEEG YVPTSYIEVN LEPNAKDS
//
