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Database: UniProt
Entry: A0A498L919_LABRO
LinkDB: A0A498L919_LABRO
Original site: A0A498L919_LABRO 
ID   A0A498L919_LABRO        Unreviewed;       927 AA.
AC   A0A498L919;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=FERM domain-containing 4B-like isoform X2 {ECO:0000313|EMBL:RXN03853.1};
GN   ORFNames=ROHU_035769 {ECO:0000313|EMBL:RXN03853.1};
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:RXN03853.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN03853.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN03853.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN03853.1};
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:RXN03853.1}.
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DR   EMBL; QBIY01013469; RXN03853.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498L919; -.
DR   STRING; 84645.A0A498L919; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13191; FERM_C_FRMD4A_FRMD4B; 1.
DR   CDD; cd17200; FERM_F1_FRMD4B; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR021774; CUPID.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR047176; FRMD4A/B.
DR   InterPro; IPR041785; FRMD4A/B_FERM_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR46079; FERM DOMAIN-CONTAINING PROTEIN 4; 1.
DR   PANTHER; PTHR46079:SF1; FERM DOMAIN-CONTAINING PROTEIN 4B; 1.
DR   Pfam; PF11819; CUPID; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT   DOMAIN          5..284
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          504..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          336..373
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          453..480
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        518..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..667
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..712
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   927 AA;  106671 MW;  6CEDB5E74CDE6DAE CRC64;
     MTEGRLCQVL LLDDRQLELL VQPKLLSRDL LDLVSSHFNL KEKEYFGISF IDEKGQTNWL
     QLDRRVLDHD FSKKSGPLEL KFQVRFYIES VAYLKDATTV ELFFRNAKIS LYNCNESDED
     TRSDLKKLPA FPTAVLKEHP SLAFCEDKVI EHYKKLKGLS RGQAIIRYLT LVESLPAYGV
     HYYKVKDKQG LPWWLGVSYK GIGQYDLQDK LKPRKLFLWK QLENLYFREK KFAVEVNDPQ
     RRTASRRTFG QSGQVIYTWY ASHSLIKTIW VMAISQHQFY LDRKQSKAKI TTARSLGDIA
     MDLTETGAPR NSKLVSMESK DKLIMASNGS LVSSNSADNE VNEEQKKEKI AELKNKQESI
     KEMLALKEEE LKKMCLREAE LTGVLPKEYP LALGEKPPTV RRRVGTAFKL DDLFPYDADP
     HLRNLESCFA LQKKIVEAAK KLAYENELCK TVKKKRRRNL VDATKKLQEI ENQINDYRVK
     IGKEPTQRAS VIIADDVNLD SLSDCLNLDD DEPSQRQRSR SVQYSPRPNS SNSFSASCHS
     DHIDHANDDY QDCSRLNYGE VQEPVAYIHG DALSTHSSPY RQPSRQPSDS RSMPPTPQLP
     RNAYSSIQLS THFRQRSGSL ESQSQFLTES EPSEPVFTIS PPRRSNSTEI LDDGSSYTSQ
     SSVEYSVPGG HSRAKNRHRR RQGNIYANTG SMPNLAQNDT RGYTPQPRQQ PTTTAYYVTG
     YPRYIEPEVH PNGPYMYETE MEGHYNVNPS YYRHDPHGNY GQDEIDGLAH NLYATLRPSR
     TRPPSRNENI VKNMQRAEVV EHLRGWYNRQ HRQQGYDTYR APQQNMGYRT MSSNYVRSDS
     TTSYSTVSSG NWHGRPVTAM SEYDMPPAHH QSYGYNTVHY SQPLHSRSYI DVNHHDSHMS
     SPMDSSFDSE DQQTLYWHEN SKPGTIV
//
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