ID A0A2Y9NSD0_DELLE Unreviewed; 616 AA.
AC A0A2Y9NSD0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Formin-binding protein 1 isoform X6 {ECO:0000313|RefSeq:XP_022434172.1};
GN Name=FNBP1 {ECO:0000313|RefSeq:XP_022434172.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022434172.1};
RN [1] {ECO:0000313|RefSeq:XP_022434172.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022434172.1};
RG RefSeq;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_022434172.1; XM_022578464.2.
DR AlphaFoldDB; A0A2Y9NSD0; -.
DR Ensembl; ENSDLET00000010090; ENSDLEP00000009145; ENSDLEG00000006640.
DR Proteomes; UP000248483; 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 CDD; cd07676; F-BAR_FBP17; 1.
DR CDD; cd11629; HR1_FBP17; 1.
DR CDD; cd12071; SH3_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; IPR035492; FNBP1_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: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};
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:UP000248483};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 399..476
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 545..606
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 293..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 71140 MW; 8265E67B88F42E4C CRC64;
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK
EEEEYRYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV ELARYVQELK QERKSHFHDG
RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQMRH
QMAEDSKADY SSILQKFNHE QHEYYHTHIP NIFQKIQEME ERRIVRIGES VKTYAELDRQ
VIPIIGKCLD GIVKAAESID PKNDSQLAIE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
SNSRGEGKSE LKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP SAVPNGPQSP
KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG GATPEDFSNL PPEQRRKKLQ QKVDELNKEI
QKEMDQRDAI TKMKDVYLKN PQMGDPASLD HKLAEVSQNI EKLRLEAQKF EAWLAEVEGR
LPARSEQARR QSGMYDVQNP PAVNNCAQDR ESPDGSYTEE QSQESEVKVL ATDFDDEFDD
EESLPAIGTC KALYTFEGQN EGTISVVEGE TLYVIEEDKG DGWTRIRRSE DEEGYVPTSY
VEVYLDKNAK GAKTYI
//
