ID A0A498N2T5_LABRO Unreviewed; 586 AA.
AC A0A498N2T5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE SubName: Full=Merlin-like protein {ECO:0000313|EMBL:RXN27081.1};
GN ORFNames=ROHU_020534 {ECO:0000313|EMBL:RXN27081.1};
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:RXN27081.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN27081.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN27081.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN27081.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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:RXN27081.1}.
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DR EMBL; QBIY01012082; RXN27081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498N2T5; -.
DR STRING; 84645.A0A498N2T5; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR CDD; cd17186; FERM_F1_Merlin; 1.
DR Gene3D; 1.20.5.450; -; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 6.10.360.10; -; 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; IPR011174; ERM.
DR InterPro; IPR011259; ERM_C_dom.
DR InterPro; IPR041789; ERM_FERM_C.
DR InterPro; IPR046810; ERM_helical.
DR InterPro; IPR000798; Ez/rad/moesin-like.
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; IPR008954; Moesin_tail_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23281:SF20; FERM DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23281; MERLIN/MOESIN/EZRIN/RADIXIN; 1.
DR Pfam; PF00769; ERM_C; 1.
DR Pfam; PF20492; ERM_helical; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PIRSF; PIRSF002305; ERM; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF48678; Moesin tail domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 14..304
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT COILED 315..467
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 521..555
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 68..71
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000256|PIRSR:PIRSR002305-1"
FT BINDING 287
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000256|PIRSR:PIRSR002305-1"
SQ SEQUENCE 586 AA; 68798 MW; 2BEA1700AE04C5D9 CRC64;
MSILGLKKKQ PKTFKVKVST MDAEMEFSCE VKWKGKDLFD LVCRTIGLRE TWFFGLRYTV
KDTYAWLKPD KRVLDQEVPK DSPITFHFLA KFFPEKVEDE LVQEITQHLF FLQVKKQILD
EEIFCSPEAS VLLASYAVQA KYGDYDPNFH KPGFLAQDEL LPKRVLMQYQ MTPDMWEEKI
TAWYAEHRNI TRDEAEMEYL KIAQDLEMYG VSYFSITQNK RDTELLLGVD AQGLHIYSPN
NKLSPNKSFP WSGIRNISYS EKEFTIKPLD KKKEVFKFYS SQLRVNKLIL QLCIGNHDLF
MRRRKVDSIE VQQMKAQAKE EKARKKVERQ ILAREKQMRE EAERAKEEME RRLFQLQDEA
RMANEALLRS EETADLLAEK AQIAEEEAKL LAHKAAEAEQ ERQRLEVTAL KTKEEKRLME
QKMREAEQLA VKLVEQSERR LKEADHLKQD LSEAKDAERR AKQKLLEITK TTYPLIAAYS
SPPPPTGPES PEMAVDVGSS IRMDFKDSDM KRLSMEIERE RLEYMEKSKH LQDQLKELKS
EIESLKLEEQ QQAGLYSLRS YAEPPYIPHS NRNSAYMAQM AFYEEV
//
