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Database: UniProt
Entry: A0A093HJ94_STRCA
LinkDB: A0A093HJ94_STRCA
Original site: A0A093HJ94_STRCA 
ID   A0A093HJ94_STRCA        Unreviewed;       551 AA.
AC   A0A093HJ94;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 29.
DE   SubName: Full=Merlin {ECO:0000313|EMBL:KFV81796.1};
DE   Flags: Fragment;
GN   ORFNames=N308_00865 {ECO:0000313|EMBL:KFV81796.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV81796.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV81796.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV81796.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KL206367; KFV81796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093HJ94; -.
DR   STRING; 441894.ENSSCUP00000012248; -.
DR   Proteomes; UP000053584; 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   Gene3D; 1.20.5.450; -; 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; 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:UP000053584}.
FT   DOMAIN          14..304
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   COILED          311..464
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          517..544
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"
FT   NON_TER         551
FT                   /evidence="ECO:0000313|EMBL:KFV81796.1"
SQ   SEQUENCE   551 AA;  65128 MW;  3F3D36B5920013D1 CRC64;
     MSIRGLKKKQ PKTFKVKIIT VDAEMEFSCE MKWKGKDLFD LVCRALGLRE TWFFGLQYTI
     KGMCTWLKMD KKVLDQEIPK DDPISFRFLA KFYPEKAEEE LLQEITQHLF FLQVKKQILD
     EEIYCSPEAT VLLASYAVQA KYGDYDPNFH EPGFLAHDEL LPKRVLRQYQ LTAEMWEEKI
     TAWYAEHRGI ARDEAEMNYL KIAQDLEMYG VNYFPIAQNK NHTDLLLGVD AKGIHIYSIN
     NRFSPNKSFE WSAIRNISYS EKELTIKPLD KKAEVFKFFS SQLKVNKLIL QLCIGNHDLF
     MRRRKVDSIE IQQMKAQARE EKARKKMENQ RLAREKQLRE EAERAKEELE RRLFQLEDEA
     RQANEALLRS QEAAELLAEK AQIAEEEAKL LAQNAAEAEQ ERQRLEITAL KTKEEKRLME
     QKMREAELIA VKLVKESDRR AKEAEHLKQD LHEAREAERK AKQKLLDITR LNYPHMVKYP
     QYSPSDTRDA NFDKGSIKLD LKDIDLKRLS FEIERERLDY IEKSKKFEDR LKELKSEIHA
     LKLEEKQSGL Y
//
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