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Database: UniProt
Entry: A0A1V4JYU1_PATFA
LinkDB: A0A1V4JYU1_PATFA
Original site: A0A1V4JYU1_PATFA 
ID   A0A1V4JYU1_PATFA        Unreviewed;       547 AA.
AC   A0A1V4JYU1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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|EMBL:OPJ77314.1};
GN   ORFNames=AV530_007664 {ECO:0000313|EMBL:OPJ77314.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ77314.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ77314.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ77314.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ77314.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ77314.1}.
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DR   EMBL; LSYS01005497; OPJ77314.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4JYU1; -.
DR   STRING; 372326.A0A1V4JYU1; -.
DR   Proteomes; UP000190648; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
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:UP000190648};
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          339..416
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          480..541
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          422..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          130..174
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          346..380
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        436..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  63829 MW;  7F82B049000B7989 CRC64;
     MSWGTELWDQ FDNLDKHTQW GIDFLEKYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSPK
     DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMGHRVYGE LMRYSHDLKT ERKMHLQEGR
     KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH
     MADENKNEYA AQLQNFNGEQ HKHYYIVIPQ IYKQLQEMDE RRTIKLSECY KGFADSERKV
     IPIISKCLEG MILAAKSVDE HRDSQLVIDC FKSGFEPPGD FPFEDYSQNI YRTISDGTIS
     TPKQEGMRID SKTTMGKAKG KLWLFGKKPK GPALEDFSHL PPEQRRKKLQ QRIDELNREL
     QKETDQKDAL IKMKDVYEKN PQMGDPSSLQ PKLTETMSNM DRLRMEIHKN EAWLSEVEGK
     VAARSDRRHS SDINHLVTQG RESPEGSYTD DANQEVRGPP QQHAHPNEFD DEFEDDDPLP
     AIGHCKAIYP FDGHNEGTLA MKEGEILYII EEDKGDGWTR ARRHNGEEGY VPTSYIDVTL
     EKNSKGS
//
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