ID G3UMH2_LOXAF Unreviewed; 606 AA.
AC G3UMH2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Formin-binding protein 1-like {ECO:0000256|ARBA:ARBA00019975};
DE AltName: Full=Transducer of Cdc42-dependent actin assembly protein 1 {ECO:0000256|ARBA:ARBA00032854};
GN Name=FNBP1L {ECO:0000313|Ensembl:ENSLAFP00000029031.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000029031.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000029031.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000029031.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000029031.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000029031.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- SIMILARITY: Belongs to the FNBP1 family.
CC {ECO:0000256|ARBA:ARBA00009426}.
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DR AlphaFoldDB; G3UMH2; -.
DR STRING; 9785.ENSLAFP00000029031; -.
DR Ensembl; ENSLAFT00000027234.1; ENSLAFP00000029031.1; ENSLAFG00000016688.3.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000183047; -.
DR InParanoid; G3UMH2; -.
DR OMA; YADGWWE; -.
DR TreeFam; TF351162; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; 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:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:0010324; P:membrane invagination; IEA:Ensembl.
DR GO; GO:0097320; P:plasma membrane tubulation; IEA:Ensembl.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0006900; P:vesicle budding from membrane; IEA:Ensembl.
DR GO; GO:0030050; P:vesicle transport along actin filament; IEA:Ensembl.
DR CDD; cd07675; F-BAR_FNBP1L; 1.
DR CDD; cd11628; HR1_CIP4_FNBP1L; 1.
DR CDD; cd12072; SH3_FNBP1L; 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; IPR035494; FNBP1L_F-BAR.
DR InterPro; IPR035493; FNBP1L_SH3.
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:SF14; FORMIN-BINDING PROTEIN 1-LIKE; 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 Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000007646};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..263
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 398..475
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 539..600
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 477..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..174
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 405..439
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 477..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 70104 MW; E9C3C545982C6FFD CRC64;
RTWLKCLWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK
DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR
KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH
MADENKNEYA AQLQNYNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV
IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS
ASKQESGKMD AKTTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTFSIEPV
HYCMNEIKTG KPRIPSFRSL KRGVSLIMGG PALEDFSHLP PEQRRKKLQQ RIDELNRELQ
KESDQKDALN KMKDVYEKNP QMGDPGSLQP KLAETMSNID RLRMDIHKNE AWLSEVEGKT
GGRGDRRHSS DINHLVTQGR ESPEGSYTDD ANQEVRGPPQ QHGHHNEFDD EFEDDDPLPA
IGHCKAIYPF DGHNEGTLAM KEGEVLYIIE EDKGDGWTRA RRQNGEEGYV PTSYIDVTLE
KNSKGA
//
