ID A0A498LLE5_LABRO Unreviewed; 989 AA.
AC A0A498LLE5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Disheveled-associated activator of morphogenesis 1-like isoform X1 {ECO:0000313|EMBL:RXN08831.1};
GN ORFNames=ROHU_011370 {ECO:0000313|EMBL:RXN08831.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN08831.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN08831.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN08831.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN08831.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) 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:RXN08831.1}.
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DR EMBL; QBIY01013297; RXN08831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498LLE5; -.
DR STRING; 84645.A0A498LLE5; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45725:SF16; DISHEVELED-ASSOCIATED ACTIVATOR OF MORPHOGENESIS 1; 1.
DR PANTHER; PTHR45725; FORMIN HOMOLOGY 2 FAMILY MEMBER; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498LLE5};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 35..386
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 525..920
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 938..969
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 486..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..542
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 989 AA; 113927 MW; D91A7CA5ECE92E52 CRC64;
MSFLCCCLKK SDHPEITYRL RHDSNFTLQT MEPTLPMPPT EELDAMFTEL VDELDLTEKH
REAMFALPAE KKWQIYCSKK KRKSLLALEK EDEEERNKTI ESLKTALRTQ PMRFVTRFID
LDGLTCILNF LKTMDYETTE SQIHTSLIGC IKALMNNSQG RANVLAHSES INIIAQSLAT
ENIKTKVAVL EIMGAVCLVP GGHKKILEAM LHYQKFACER TRFQTLLNDL DRSTGRYRDE
VNLKTAIMSF INAVLSQGAG ETSLEFRIHL RYEFLMLGIQ PVIDKLRSHE NSTLDRHLDF
FEMLRNEDEL ALAKRFENVH IDTKSATQVF DLIRKRINHT DAFPHFMSVL QHCLHMPYKR
NGNTVQYWLL LDRIVQQIVL QNDKGHDPDV APLENFDVKN VVRMLVNENE VKQWKEQAEK
MRKEHNELQQ KLEKKERECD AKAQEKEEMM QTLNKMKEKL EKESSEHKLV KQQVADLSAR
LHEMSNRANI PGGPPVVPLA PGSIPPPPPG PASIPPPPPP GGAPPPPPPP PGGPPPPPGL
PGFGNKLEGT VWLDLDDLKV FKQLDLEDIE KTFSAYQRQQ KESEDDTVTS KKVRELSVID
GRRAQNCNIL LSKLKLSNEE IKRAILTMDE QEDLPKDMLE QLLKFVPEKS DVDLLEEHKH
ELERMAKADR FLYEMSRINH YQQRLQSLYF KKKFTERIAE IKPKVEALSK ASKEILQSKN
LRQLLEVVLA FGNYMNKGQR GNAYGFKVSS LNKIADTKSS IDKNVTLLHY LITILEQKYP
KVSLIHDDLQ SVPEAAKVNM TELEKDINNL RTGLKSVETE LEYQKDQPQT YGDKFVSVVS
QFITVAGFSF SEVEDSLQDA KDSFEKAVKH FGEDATRMQP DEFFGIFDQF LQGFSEAKQD
NENMRRRKEE EERRARMEAQ LKEQREKERK ARKAKENCEE DGEFDDLVSA LRSGEVFDKD
LSKMKHNRKR PVKQSAESSR ERPITKLNF
//
