ID A0AAD9E5J0_9TELE Unreviewed; 2067 AA.
AC A0AAD9E5J0;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=Protein flightless-1 homolog {ECO:0000256|ARBA:ARBA00071559};
GN ORFNames=P4O66_019534 {ECO:0000313|EMBL:KAK1805188.1};
OS Electrophorus voltai.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=2609070 {ECO:0000313|EMBL:KAK1805188.1, ECO:0000313|Proteomes:UP001239994};
RN [1] {ECO:0000313|EMBL:KAK1805188.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB-2022 {ECO:0000313|EMBL:KAK1805188.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK1805188.1};
RA Bian C.;
RT "Electrophorus voltai genome.";
RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
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:KAK1805188.1}.
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DR EMBL; JAROKS010000003; KAK1805188.1; -; Genomic_DNA.
DR Proteomes; UP001239994; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:TreeGrafter.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:TreeGrafter.
DR GO; GO:0051014; P:actin filament severing; IEA:TreeGrafter.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:TreeGrafter.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:TreeGrafter.
DR GO; GO:0030239; P:myofibril assembly; IEA:TreeGrafter.
DR CDD; cd11280; gelsolin_like; 2.
DR CDD; cd11290; gelsolin_S1_like; 1.
DR CDD; cd11292; gelsolin_S3_like; 1.
DR CDD; cd11288; gelsolin_S5_like; 1.
DR FunFam; 3.80.10.10:FF:000033; FLII, actin remodeling protein; 1.
DR FunFam; 3.80.10.10:FF:000050; FLII, actin remodeling protein; 1.
DR FunFam; 3.80.10.10:FF:000054; FLII, actin remodeling protein; 1.
DR FunFam; 3.40.20.10:FF:000020; protein flightless-1 homolog isoform X1; 1.
DR FunFam; 3.40.20.10:FF:000030; protein flightless-1 homolog isoform X1; 1.
DR FunFam; 3.40.20.10:FF:000031; protein flightless-1 homolog isoform X1; 1.
DR FunFam; 3.40.20.10:FF:000034; protein flightless-1 homolog isoform X1; 1.
DR FunFam; 3.40.20.10:FF:000021; protein flightless-1 homolog isoform X2; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.40.20.10; Severin; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR055414; LRR_R13L4/SHOC2-like.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR PANTHER; PTHR11977:SF51; PROTEIN FLIGHTLESS-1 HOMOLOG; 1.
DR PANTHER; PTHR11977; VILLIN; 1.
DR Pfam; PF00626; Gelsolin; 5.
DR Pfam; PF23598; LRR_14; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SMART; SM00364; LRR_BAC; 6.
DR SMART; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 5.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR PROSITE; PS51450; LRR; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP001239994};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1331..1352
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 410..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1995..2016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1643..1653
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2067 AA; 234350 MW; E25AB49A6BB18AE4 CRC64;
MAATGVLPFI RGVDLSGNDF KGGYFPEHVK SMTSLRWLKL NRTGLCYLPE ELSSLQKLEH
LSVSHNSLTT LHGELSSLPN LRAVVARANN LKNSGVPDDI FQLDDLSVLD LSFNQLTEIP
RDLENSRNML VLNLSHNSID NIPNQLFINL TDLLYLDLSD NKLDSLPPQM RRLVHLQTLI
LNNNPLMHAQ LRQLPAMVAL QTLHLRNTQR TQSNMPTSLE GLTSLADVDL SCNDLTRVPE
CLYSLASLKR LNLSNNQITE MSLCIDQWTQ LETLNLSRNM LNSLPSAICK LSKLKKLYLN
SNKLDFDGVP SGVGKLSSLE EFMAANNNLE LIPEGLCRCG KLKKLVLNKN RLVTLPEAIH
FLTDLEVLDV RENPNLVMPP KPVDRAAEWY NIDFSLQNQL RLAGASPATV AAAGGGNSPR
DPMARKMRLR RRKDSTQDDQ AKQVLKGMSD VAQEKNKSME ENGDMKYSDL KSKRWDKNLE
KPPLDYSEFF MEDVGHVPGV TVWQIENFLP VQVDEAFHGK FYEADCYIVL KTFLDDNGAL
TWQIFYWIGQ DATLDKKAGS AIHAVNLRNY LGAECRTIRE EMGDESEEFG AVFDNEISYI
EGGTASGFYT VEDTQYPTRL YRVYGKKNIR LESVPLKAAS LDPRFVFLLD TGLEIYVWRG
ANATLSGTTK ARLFAEKINK NERKGKAEIT SLVQNQEPPE FWEVLGGQPE EIKKHVPNDF
TPVRPKLYKV GLGLGYLELP QINYKLSVEH KNRLKLDVLP ELRLLQSLLD TKGVYILDCW
SEVFIWIGRK SPRLVRAAAL KLGQEMCSML HRPKHAVVIR NLEGTEVQVF KSKFKNWDDV
LKVDYTKNAE SVQQTDGLSG KVKKDADQKG QMKADLTALF LPRQPPMPLS EAEQMMEEWN
EDLDGMEGFV LEGKKFARLP EEEFGHFHTQ DCYVFLCRYW VPVEYEDEKG KEKGEEGQGE
DEDKQPEEDF QCVVYFWQGR EASNMGWLTF TFSLQKKFES LFPGKLEVVR MTQQQENLKF
LSHFKRKFII HKGKRKLKVD NVQPSLYHIR TNGSALCTRT IQIPTDSSNL NSEFCYILKV
PFESTDNQGI VYTWVGRAAD PDEAKLAEDI MNSMFDDSYS KQVINEGEEP ENFFWVGIGT
QKPYDEDAEY MKFARLFRCS NEKGYFSVSE KCSDFCQDDL ADDDIMLLDN GKEVYMWVGT
QTSQVEIKLS LKACQVIFVR KLRPFAALPH HEYQLEKKYD IHFADGKLFA QYRKILLSEC
PQCPEPKVFS KFEELEQHMR KQHELFCCKL CAKHLKVIFS YERKWYNRKD LARHRTQGDP
DDTSHRGHPL CKFCDDRYLD NDELLKHLRR DHYFCHFCDA DGAQEYYSDY RYLSEHFREI
HYLCEEGRCS TEQFTHAFRT EIDYKAHKAA AHSKNRAEAR QNRQIDIQFT YAPRQQRRND
GLVGGDDYEE VDRFNRQGRS GRGRAPGLQQ NVRSWRYNRE EEEDRELVAA IQASQAVRRQ
EERGQFHERG SQKPRKEEKM DTDELRSSRG AAKPPGDMQG RSLKKNNVPM KGEDFPALGA
GVTLPPPTQN TIKSSPVFLK KEDFPSLVQS GTAGSAPVTA VYTAQARKHS SFHEEDFPAL
VSKIKPQKPN GSTTSAWSQA GSKPVVPNNK PVPLQMKSAP AQPAPVFSAN DPPPSCSVSR
APASHRKKQL ASSENAKTAP KVRSPVSSDD EDGGKTTHEI RTAPTMLEIS SLLTVKTGLS
QMNPKAGKKK KQTINTPAGT SSHNGDLVTH VAHKENVPDT KPPDVSVSKG PVVPKANRLI
NGYKENTADK ISYTSIPEEP PAAKKQPVSD FTHVPEEDFP ALITKKPPPG FKAAFPLKNA
QTDLPPPPGL GPVVSKPPPG FTGVPLNSNV VEPTVSIYNR SAPSFGKYHM PENFKERNMD
LIQSIKNFLK NDESKFNEFK NYSGQFRQGL ISAAQYHRSC HVLLGDNFSR VFNELLVLLP
DTSKQQELLT AHADRKALEK QQQSSKPQKN KKKAWQTSTS SSSLELDCQV CPTCKQVLAL
KDFNTHKTLH IGADEFPSLQ DISKIIS
//
