ID A0A3B4ZDE4_9TELE Unreviewed; 600 AA.
AC A0A3B4ZDE4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Formin binding protein 1 {ECO:0000313|Ensembl:ENSSPAP00000006480.1};
GN Name=FNBP1 {ECO:0000313|Ensembl:ENSSPAP00000006480.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000006480.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000006480.1}
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; A0A3B4ZDE4; -.
DR Ensembl; ENSSPAT00000006615.1; ENSSPAP00000006480.1; ENSSPAG00000004950.1.
DR GeneTree; ENSGT00950000183047; -.
DR Proteomes; UP000261400; 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 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; 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 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 373..450
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 533..594
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 293..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 380..407
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 466..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 69215 MW; 7E5F4DA26A7806A7 CRC64;
MSWGSELWDQ FDNLEKHTQW GIEFVEKYTK FVKERSEIET NYAKQIRNLS KKYQPKKNSR
EEEESKYTFC RAFLMTLNEL NDYAGQHEVI AENLTSQIIA DLTRYLGELK SERKSHFHDG
RKAQQHIESS WKQLESCKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQMRH
QMATDSKGDY SSYLQKFNQE QNEHYYTVIP NIFQKLQDME ERRIERIGVC MKTFADVDRQ
VLPIVGKCLD GMTKAAESIE PKTDSKQVVE SYKSGFEPPG DVEFEDYGQA MKRTASDTSL
SNSRDGKEKP AGKTKGKLWP FIKNKNKSPK QHKEPLSHRL NDFMTSKPKM HCLRSLRRGL
SLKLGSGPED FSHLPPEQRR KKLQGKLDEL NKDIQKETDQ RDALTKMKDV YVKNPQMGDP
ASVDPRLSEI GQNIEKLQFE VQKFEGWLAE VEERMPSKSD SHRRSGLYET QNNTTVSNNC
AQDRESPDGS YTEEQNSETQ VKANPAPAPG PAPNPTSSTP EFDDEFDDEE TLPTIGTCKA
LYPFEGHNEG TISVAEGELL YVIEEDKGDG WTRVRRNEDE EGYVPTSYVE VFLETNAKDS
//
