ID A0A1S3J5H1_LINUN Unreviewed; 589 AA.
AC A0A1S3J5H1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Disheveled-associated activator of morphogenesis 1 {ECO:0000313|RefSeq:XP_013405640.1};
GN Name=LOC106170343 {ECO:0000313|RefSeq:XP_013405640.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013405640.1};
RN [1] {ECO:0000313|RefSeq:XP_013405640.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013405640.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013405640.1; XM_013550186.1.
DR AlphaFoldDB; A0A1S3J5H1; -.
DR STRING; 7574.A0A1S3J5H1; -.
DR EnsemblMetazoa; XM_013550186.1; XP_013405640.1; LOC106170343.
DR GeneID; 106170343; -.
DR KEGG; lak:106170343; -.
DR InParanoid; A0A1S3J5H1; -.
DR OrthoDB; 5392160at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR PANTHER; PTHR45725; FORMIN HOMOLOGY 2 FAMILY MEMBER; 1.
DR PANTHER; PTHR45725:SF10; FORMIN-LIKE PROTEIN 13; 1.
DR Pfam; PF02181; FH2; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..589
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010233696"
FT DOMAIN 358..589
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 76..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 589
FT /evidence="ECO:0000313|RefSeq:XP_013405640.1"
SQ SEQUENCE 589 AA; 64744 MW; E565367A5D65D004 CRC64;
MELYFLFCLL FCYFQALNGI ERELIHVTSK EKVTSLMRLA QTLEQHVQHL PLGDTMQQPP
TADTYTRATV GDILESIQED PSNNSYDEEY DSVQTEANGN LRPASGDTDA HSFGDNHGRI
VNYMTEISSD YSCVDDGEEE DGEQKDREES GEEWVEGEEQ EDGEEAGEEQ EGNHEEKEEE
GDEKKEEDGV EEDSHLEAFS VDPSAKAHVK EEIQYTDEVH QGSNSKEHVY SEDSEISVAA
SMRALSDLLQ ELDNGEQSAE ETMAEGSVQK PDCSNEECLP TTQSSTLITG SVDSGQSQSD
VPPSTPTNSS TAPLPTPSPP TPLPQGTPPP LPPPLCAPPP PPSAPPPPGG QFGMKTGRTL
KKTTQQKLRM FRFSTLPVNA VDNSVWKDLR DLTSSINTKA LEDMFALEEN KTQRTASTAV
QPGLSKQQPK SLLDPKKAQN LGIFLMGLKM SAAQLKQKLD IVDETSGGLT TEQITAIRRY
QPDKNEQKTL EQYSGVVSDL DRADQFMLEL CRIPHLDLKL ELLLAIRELA AQIDDIEPSM
ELVSVACDEL LGSQMFVVVL EYILAVGNYI NSSGGKGGLM GFHLSSLLK
//
