FNBP1_XENLA
ID FNBP1_XENLA Reviewed; 610 AA.
AC Q6GNV5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Formin-binding protein 1 homolog;
GN Name=fnbp1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required to coordinate membrane tubulation with
CC reorganization of the actin cytoskeleton during endocytosis.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form
CC filamentous structures. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Lysosome
CC {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}.
CC Note=Enriched in cortical regions coincident with F-actin. Also
CC localizes to endocytic vesicles and lysosomes. {ECO:0000250}.
CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its
CC concave surface. The end-to-end polymerization of dimers of these
CC domains provides a curved surface that fits best membranes with around
CC 600 A diameter, and may drive tubulation (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}.
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DR EMBL; BC073396; AAH73396.1; -; mRNA.
DR RefSeq; NP_001085826.1; NM_001092357.1.
DR AlphaFoldDB; Q6GNV5; -.
DR SMR; Q6GNV5; -.
DR DNASU; 444253; -.
DR GeneID; 444253; -.
DR KEGG; xla:444253; -.
DR CTD; 444253; -.
DR Xenbase; XB-GENE-1003124; fnbp1.L.
DR OrthoDB; 348563at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 444253; Expressed in heart and 20 other tissues.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; 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 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; IPR028532; FNBP1/FBP17.
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:SF13; PTHR15735:SF13; 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; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Coated pit; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endocytosis; Lipid-binding; Lysosome; Membrane;
KW Reference proteome; SH3 domain.
FT CHAIN 1..610
FT /note="Formin-binding protein 1 homolog"
FT /id="PRO_0000261433"
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 397..474
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 543..604
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 295..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..259
FT /evidence="ECO:0000250"
FT COILED 392..484
FT /evidence="ECO:0000250"
FT COMPBIAS 334..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 166
FT /note="Mediates end-to-end attachment of dimers"
FT /evidence="ECO:0000250"
SQ SEQUENCE 610 AA; 70316 MW; E5738AF9D48EA926 CRC64;
MSWGTELWDQ FDNLEKHTQW GIEVLEKYIK FVKERAEIES NYAKQLRNLS KKYQTKKNSK
EEEESKYTSC KAFQTTLNEM NDYAGQHEVI SENAASLITV ELTRFVQELK QERKQHFHEG
RKAQQQIETC WKQLEASKRR FERDCKEAER AQQHFEKMDA DINVTKADVE KARQQAQIRH
QMSDDSKGDY SSVLQKFNRE QHEHYFTHIP GIFQKLQDME EKRIGRMGES LKTYADIDRQ
VVPIIGKCLD GITKSAESIS EKQDSQMVVE SFKSGFEPPG DIDFEDFTQN MKRTVSDTSL
TKADSKSDPK VPSKSRNKLW PFIKKNKLMS LLTSPHQPPP PPPASSSPSA VPNGPHSPKQ
QKEPLSHRFN DFMTSKPKMH CFRSLKRGGS TPEDFSNLPP EQRRKKLQQK VDELNKDIQK
EIDQRDALTK MRDVYTKNPQ MGDAASVGQK LVEIGNNIEK LRVEVQKFEG WLAEVEGRLS
ARNDSSRRQS GLYDTQNTQT VNNCAQDRES PDGSYTEDHS QEPEVKVTPT EFDDDFDDEE
PLPTIGTCKA IYPFDGENEG TISVTEGEIL KVIEEDKGDG WTRIRRSEED EGYVPTSYIE
VYLDRNAKDS
