ID A0A5E4BIT2_MARMO Unreviewed; 943 AA.
AC A0A5E4BIT2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=FERM domain-containing protein {ECO:0000259|PROSITE:PS50057};
GN ORFNames=MONAX_5E020417 {ECO:0000313|EMBL:VTJ69136.1};
OS Marmota monax (Woodchuck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Marmota.
OX NCBI_TaxID=9995 {ECO:0000313|EMBL:VTJ69136.1, ECO:0000313|Proteomes:UP000335636};
RN [1] {ECO:0000313|EMBL:VTJ69136.1, ECO:0000313|Proteomes:UP000335636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CABDUW010000449; VTJ69136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5E4BIT2; -.
DR Proteomes; UP000335636; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13184; FERM_C_4_1_family; 1.
DR CDD; cd17203; FERM_F1_EPB41L3; 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; IPR030691; Band4.1-L3_FERM_F1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FA.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR007477; SAB_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR PANTHER; PTHR23280:SF20; BAND 4.1-LIKE PROTEIN 3; 1.
DR Pfam; PF05902; 4_1_CTD; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF04382; SAB; 1.
DR PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 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 Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP000335636}.
FT DOMAIN 193..474
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 17..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 104724 MW; 47A0DA776351EF7E CRC64;
MLRQDGEGCS NITVLNSAEP RCLLQGGRGE PRRAALGCGF LPTPSPAHRR LGREPEPGPH
AAACPASRPT PEQSTMTTES GSDSESKADQ ETEPQEAAGA QGQAGAQPGP PEPPSGSGSG
SLEEPPALEQ FEAAAAHSTP VRREVTDKEQ EFAAAAAKQL EYQQFEEDKL SQKSYSSKLS
RSPLKIVKKP KSMQCKVILL DGSEYSCDVE KRSRGQVLFD KVCEHLNLLE KDYFGLTYRD
AENQKNWLDP AKEIKKQIRS GAWQFSFNVK FYPPDPAQLS EDITRYYLCL QLRDDIVSGR
LPCSFVTLAL LGSYTVQSEL GDYDPDECGN DYISEFRFAP NHTKELEDKV IELHKSHRGM
TPAEAEMHFL ENAKKLSMYG VDLHHAKDSE GVEIMLGVCA SGLLIYRDRL RINRFAWPKV
LKISYKRNNF YIKIRPGEFE QFESTIGFKL PNHRAAKRLW KVCVEHHTFF RLLLPEAPPK
KFLTLGSKFR YSGRTQAQTR RASALIDRPA PYFERSSSKR YTMSRSLDGA SVNENHEIYM
KDSMSAAEVG TGQYATTKGI SQTNLITTVT PEKKAEEERD EEDERRKKAE EATPVSAIRH
EGKTDSERTD TAADGETTAT EELDKTQDEL MKHQTNISEL KRTFLETSTD TAVTNEWEKR
LSTSPVRLAA RQEDAPMIEP LVPEEKVETK IESSETETET TPHPQPLSTE KVVQETVLVE
ERRVMNVHAS GDASYTAGED ADAPAQPIPT EAVSVKEKEG SAVTEGSKEE RQEESAKAGS
EQEETARASQ EQEEEQGAAT QVSETSEQKP HFESSTVKME TISYGSVPTG GVKLEVSTKE
VPVVHTETKT ITYESSQVDP GADLEPGVLM SAQTITSETT STTTTTHITK TVKGGISETR
IEKRIVITGD ADIDHDQALA QAIKEAKEQH PDIRWRGLTR GII
//
