ID A0A3B4TXE0_SERDU Unreviewed; 843 AA.
AC A0A3B4TXE0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=F-BAR domain only protein 2 {ECO:0000256|ARBA:ARBA00018998};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000010966.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000010966.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000256|ARBA:ARBA00004283}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004283}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004283}.
CC -!- SIMILARITY: Belongs to the FCHO family.
CC {ECO:0000256|ARBA:ARBA00011064}.
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 AlphaFoldDB; A0A3B4TXE0; -.
DR STRING; 41447.ENSSDUP00000010966; -.
DR Ensembl; ENSSDUT00000011168.1; ENSSDUP00000010966.1; ENSSDUG00000008017.1.
DR GeneTree; ENSGT00940000157105; -.
DR OrthoDB; 2996449at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR CDD; cd07673; F-BAR_FCHO2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR030122; FCHo2_F-BAR.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR PANTHER; PTHR23065:SF8; F-BAR DOMAIN ONLY PROTEIN 2; 1.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF10291; muHD; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51072; MHD; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 4..250
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 575..843
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 280..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..114
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 281..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 92993 MW; 75635ABF68F4D2CD CRC64;
MITPYFLENF WGEKNNGFDV LYHNMKHGQI SSKELTDFIR ERSTIEEAYA RSMTKLAKSA
GNFSQLGTFA PVWDVFKSST EKLASCHMEL VRKLQELIKE VQKYVEEQAK AHKKTKEEVA
STLEAVQNIQ TTSQALQKSK EIYNAKTVEQ ERLRKEGATQ RDVDKAGVKA KKATETYKSY
VEKYATAKSE FEQKMAETAQ KFQDIEESHI LHMKEIIQSY SQSVDETHIQ IGELHNEFVR
NIENTSVESL IQKLAESKGT GKERPGPIEF EECNTAIATE GAKPRKRKPF GIPGRRKDKD
TDSTESTEVE AANTANGAPP GYYGAIDIQN AHETEERQTW LKPTTGKSQQ NVPQVDAEGF
CIRPEVNEND AKENSFYSSS DSEDEDEPRK FHVEIKPVQP NNGTHQNRAT IDELKASIGN
IILSPSTSGQ MRRNQSSDEL AKPRVPTSYE LNNDLLSLDP FSPTLAAGSS SSVSSSTVPV
PNRPTTPLTA GALVPPPRPS SRPKLPTGKL TGINEIVRPF SPPKTSNASP PPSAPLARAE
SSSSLSSNAS LSAGNTPTVG TSRGPSPVTL ASQDALPIAV AFTESVNAYF KGADPTKCIV
KITGDMTLSF PMGIIKVFTT NPSPAVLTFK LKNTSRLEQI LPNQQLLYSD PSQSDSNSKD
FWFNMQALTS YLRKASDQNP SASYYNVDIL KYQVLSDGIH STPLNLAVYW KCTPSTTDLR
VDYRYNPDSM FSPWPLSNVQ ILVPVDGGVT NMQSLPNSIW NSEQNKCLWK LSDISEKSEN
EGAGSLRAKF ELSNGPSNPS TLAVQFMSEG STLSGVDMEL QGAGYRLSLS KKRFATGRYM
ADC
//
