ID A0A8J1TAL5_OWEFU Unreviewed; 607 AA.
AC A0A8J1TAL5;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAH1800321.1};
GN ORFNames=OFUS_LOCUS24223 {ECO:0000313|EMBL:CAH1800321.1};
OS Owenia fusiformis (Polychaete worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Canalipalpata; Sabellida; Oweniida; Oweniidae; Owenia.
OX NCBI_TaxID=6347 {ECO:0000313|EMBL:CAH1800321.1, ECO:0000313|Proteomes:UP000749559};
RN [1] {ECO:0000313|EMBL:CAH1800321.1}
RP NUCLEOTIDE SEQUENCE.
RA Martin C.;
RL Submitted (MAR-2022) 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:CAH1800321.1}.
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 EMBL; CAIIXF020000011; CAH1800321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J1TAL5; -.
DR OrthoDB; 5971719at2759; -.
DR Proteomes; UP000749559; Unassembled WGS sequence.
DR GO; GO:0005884; C:actin filament; IEA:TreeGrafter.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0030427; C:site of polarized growth; IEA:TreeGrafter.
DR GO; GO:0051015; F:actin filament binding; IEA:TreeGrafter.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:TreeGrafter.
DR CDD; cd11959; SH3_Cortactin; 1.
DR FunFam; 2.30.30.40:FF:000398; Hematopoietic cell-specific Lyn substrate 1; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035716; Cortactin_SH3.
DR InterPro; IPR003134; Hs1_Cortactin.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1.
DR PANTHER; PTHR10829:SF23; CORTACTIN, ISOFORM A; 1.
DR Pfam; PF02218; HS1_rep; 7.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51090; CORTACTIN; 7.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000749559};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..415
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 66715 MW; E457E39B0E753AA1 CRC64;
MWKASAGHNA NVNVSNGDDD DWETDPDFVN DVSEKEQRWG AKTVEGSGHQ GSISISKLRE
DVTHDDTKVK AKEAEAGPKA SYGYGGKFGV EKDKQDKSAV GHDYQAKLAA HASQTDSAKG
FGGKYGVQKD RVDKAAVGFE YDGKTDKHES QKDYAKGFGG KYGVQKDRVD KSAVGWEHHE
ETAKHESQRD YSAGFGGKYG VQTDRVDKSA VGYEHQEKLA QHDSQKDYSA GFGGKYGVQT
DRVDQSAVGF EHQEKLSQHD SQKDYAQGFG GKYGVQRDRQ DSAAKGYDEV TKTELHESQK
DFKKGFGGKF GVDTEHQDQA AHGYDEMEAP SPSYQKPRAD SGSSGAKNLR ARFENMAKQG
EDDARKRAEE ERARRKAKED KEREEQQRQN KERFAREKAE KEASRPAAPA PQAAADMVYD
DAASAGPVST EGAETIYSEA QSVGEVQPES VYSDATSTPG QQAEESIYNE VEPMPSRVPP
PAAASAQQGD VYEDTNFEPE PIYNTADPAE GVYEDTPVVA ATPPSSGTSA NQEIYDDTQA
ENVYESAPDG EIKAKALYDY QATDDDELTF DPEEIITNIE KIDEGWWRGS CRGKVGLFPA
NYVQEFQ
//
