ID A0A087X4B1_POEFO Unreviewed; 1737 AA.
AC A0A087X4B1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Supervillin c {ECO:0000313|Ensembl:ENSPFOP00000000614.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000000614.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000000614.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family.
CC {ECO:0000256|ARBA:ARBA00008418}.
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DR EMBL; AYCK01023995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000000615.2; ENSPFOP00000000614.2; ENSPFOG00000000597.2.
DR eggNOG; KOG0445; Eukaryota.
DR GeneTree; ENSGT00940000166828; -.
DR OMA; TIACTPM; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR CDD; cd11289; gelsolin_S2_like; 1.
DR Gene3D; 3.40.20.10; Severin; 5.
DR Gene3D; 1.10.950.10; Villin headpiece domain; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977:SF87; SUPERVILLIN ISOFORM X1; 1.
DR PANTHER; PTHR11977; VILLIN; 1.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF02209; VHP; 1.
DR SMART; SM00262; GEL; 5.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 5.
DR SUPFAM; SSF47050; VHP, Villin headpiece domain; 1.
DR PROSITE; PS51089; HP; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT DOMAIN 1664..1737
FT /note="HP"
FT /evidence="ECO:0000259|PROSITE:PS51089"
FT REGION 36..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1737 AA; 193554 MW; C1D4DF521804F706 CRC64;
LEPRAERIAR YKAERRRELA ERYGDLEELP SKWVRRDGKE LSNPATSARG GEFNSDDLGE
RVNGRTRDVT NGVKADAPAE PNYLALPLYR QYNGCCSSVK DKDVAKYSKK VVELATVSDY
RQMQTCRHDL VGCSVSQTSL TGEQKRLSCK YRRTTDLPNL SQNCQDSANV PSEDGLLVHP
GPDASQLHTR VSVGQLRSSL LQQTEGSAVE TSGPDPGHTT SSLDLAAGPE GGRRRGRRYL
QGSAVGRKTS ERFRTQPITA NEMEESTGPE LKLYQQISSW LLDADENDKK ADVKTDDRAK
MSVAAKMSLF RELEKSAASD SSALLKPRSA NSLPERRARR NNDLRFLTQP ITCEEMVSMR
ASCIKFVAYF VVLCRAPPAA EVPSGQSESV EVGDESCRMS MREKLALFNR LSVPEKNGSG
PADGPSERRK QKGARYRTQP ITVDEVSLLQ KGPIQLPAFS LSPNLYDRQQ ASSVNLKPSE
MRLTQPKSEL SEPEPAQRGL QDHNSEPCLK GILKKSRPDD SEGSGTDGQE LPPLNQQNGE
DCTDPEMFGR TEGPERPEPH RDTSVRVAPW RQRARNRRET PIQLPSDLDS QITSSVGNGT
QGEEQSVERL EEEDKPKQKA LVSVGVCSAN PQETPESPRG KVRNRHAFMS LQTIKTNNLY
LLCWSNTPML HVEPVFASVF AINTPQYIMC FNQSKEAEPE LQMEEGEESK TEQQSNKQEA
EMNIERSEFY SSGFDSAASP ETVLHIDPPH EETPADGLKI SGGLPPPPAG GPTPCGDVAA
TETDQDLAIL CQSSTPILIS EKYKEVWSTI IFTHETRPKP LDKDSHHKIL KLYGNCYDLK
LNQTNFGYLV ENSEVLLLVA FVCRLSSAVT EHRRAVRPSR RTQGSRNPLR ALAAREDIRQ
DYMGERDNSA AEERDQAEKN CKNSSSPDSH PATSSEKEMS KSFPPFSNLM LIHIKGRRQV
QVRVVEPSVR SLNSGDCFLL VDPNHCILWS GEFANKEERA KALELAAFIQ SRRELGCRAS
QVVHLEEGLN TDGPEAADFW SLLGGRKQYR AAGAPEEDEL FEQGVVESNC VYSLMEDRLV
PHEQAWASIP STALLDSSEV LVFDFGSEVY LWHGRDVSPS RRNVALQLTH QVWVGEYDYC
NCRVNPLDPT QCNPSVQPRG EGRPSWALLA VVTEDNETAL FREKFLSPMC GSDDAAEVDS
EGNAMQSLPV EPPSSDVLTP CDIKALASGG LLEGDASVRT VLSGVDVHRG RGVITLEEGR
AMELRTVSVD TWHVLEFDDS EIQVESTGQL HEGDSYVIRW TYSITAFDNR SSQDECGNVS
KPQENTAFFL WRGRHSSVSG RDTAAFLSIG MNNQEDSQLV VPQGKEPPCF LQLFQGGLVI
HKGKREEPTS TAGGTADWRL FCVRGELPEE ALLLEGDCCC SSLRSRGSFV LLNSQQGVLY
LWTGCKAHSS TREVSKRAVE RLIEMSPSEL GLCRSNPVTV HFVEEGSEPS DFWTALGQMD
RKAYDCMLQD PGKYNFTPRL FHLSASSGRF EAEELRSPIR LPGVVMAMPF VQESLYSVPQ
PALFLLDNRL EVYLWQRGQP EQTGSSAAAW SLWHSERKCA MQTVLQYCKE INPRRPPQAY
LIFEGSEPLT FTNVFPRWER NHGPLTQRDS GEVKLTLVQD ALAQLMKAQY PVEELLQSPL
PAGVDPQHLE VYLSDQDFQK LTSTLLLFQA VLEMKRDEYA SLPSWEQTDL KKSKGLF
//
