ID A0A1S3PC34_SALSA Unreviewed; 1191 AA.
AC A0A1S3PC34;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=F-BAR domain only protein 1-like isoform X2 {ECO:0000313|RefSeq:XP_014025079.1};
GN Name=LOC106584373 {ECO:0000313|RefSeq:XP_014025079.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014025079.1};
RN [1] {ECO:0000313|RefSeq:XP_014025079.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014025079.1};
RG RefSeq;
RL Submitted (NOV-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}.
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DR RefSeq; XP_014025079.1; XM_014169604.1.
DR AlphaFoldDB; A0A1S3PC34; -.
DR STRING; 8030.ENSSSAP00000088494; -.
DR PaxDb; 8030-ENSSSAP00000088494; -.
DR OMA; TDSAVMD; -.
DR OrthoDB; 2996449at2759; -.
DR Proteomes; UP000087266; Chromosome ssa23.
DR Bgee; ENSSSAG00000070105; Expressed in ovary and 6 other cell types or tissues.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR CDD; cd07674; F-BAR_FCHO1; 1.
DR CDD; cd09268; FCHo1_MHD; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
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; IPR042735; FCHo1_F-BAR.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR PANTHER; PTHR23065:SF6; F-BAR DOMAIN ONLY PROTEIN 1; 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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 1..248
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 921..1188
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 283..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 130347 MW; 80DFEDCFAB871F25 CRC64;
MAFFKNNFWG EKNAGFDVLY HNMKHGQIAT KELAEFVRER AAIEETYSKS MSKLAKMACN
GSPLGTFAPM WDLFRVSSDK LALCHLELMR KMNDLIRDIN KYGDEQVKVH RKTKEEQVGT
LEAVQAVQVQ SGHLQKSREG YHAKCIELDR LRKEGAPQKE LEKAEMKSKK SAESFAVCIE
KYNRVGGDFE QKMSESAQKF QDIEEAHLRQ MKQLIKGYSH SIEDTHVQVG QVHEEFKQNV
ENIGIDNLIQ RFAEQKGTGK DKPALVGFEE YMTALVPEGS KKSRGKAFRI PGLGKRDKEP
DSTDSAVTET PNSPLEVDEE GFVIRADVNQ NGCSMEDNFY SSDSDFDDEE PKKFHIQIRP
VGSSNSAATE MELKATVGAL TLPPNRGVSI KRHLSRNSST TGRSEGEGEG ATHREGEQDG
LCRSTSSPDP SRLSSTASGS DSLFGPPLES AFKSKSFAGR DQLQRAESVF GASEYAAFSS
DSSSPENIED SGLDSPSHQP LGPSPEPAGW AAWPSASQSK EPAGLGRPED PFLTVFRDPS
PERSPHPQDN PVSIWAAAPR SSRPPPDMDP SALCFPAFSQ SLAPPELDPA LWSCKHIPPE
DPFLAAFERT VTQETLPPPD AWAPPRPRPS RDGRGIEVQG DPFSSSLSDS KTLPTPSSCS
RKDRDRKRDR SAPPPESPDD PFAITMIGSP THQSALAAAT GILTHIVSSS RLTLNSNSLP
LSHPKKELVH WNSVHNPFSE GTSAGSLALG GVVREGGRKH RESRSESEPR RSGLPLTRHS
GPQEDLCFST DKDQNCLDLN TSQPPCNMAS HKSSKHSFRQ DSAELLVAAP PRPARAKRSS
GRLSGCERSR SVCSSPQPDP SPDLTSSSSS SPSEWGAQTR APSPARGGQP SPLSHLHQDH
APLHMHLSRG PSPISMSTQE LWPVAAAITE YINAYFKGGQ HNRCLVKITG DLTMSFPAGI
TRIFTANPNA PVLSFRLVNI SRVNHFLPNQ KLLYSDPSQS DPDTRDFWFN MQALNLYLQR
EAELNPLASY YNVALLKYQV SSQDPGRAPL LLSAECQRSG TVTRVALDYH CCPATAPSTQ
LTAVQVLLPL DHTATDLQCQ PPAAWNAEER QLLWKLPNLS PTNHSKGSGT LCASWQCLEV
PRGPPPSLAV QFVGSGASLS GMDVELVGSR YRMSLVKKRF ATGKYMAGCS L
//
