ID E3M259_CAERE Unreviewed; 1080 AA.
AC E3M259;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=CRE-FRM-3 protein {ECO:0000313|EMBL:EFO89812.1};
GN Name=Cre-frm-3 {ECO:0000313|EMBL:EFO89812.1};
GN ORFNames=CRE_07319 {ECO:0000313|EMBL:EFO89812.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}.
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DR EMBL; DS268422; EFO89812.1; -; Genomic_DNA.
DR RefSeq; XP_003109670.1; XM_003109622.1.
DR AlphaFoldDB; E3M259; -.
DR STRING; 31234.E3M259; -.
DR EnsemblMetazoa; CRE07319.1; CRE07319.1; WBGene00058262.
DR GeneID; 9821338; -.
DR KEGG; crq:GCK72_023807; -.
DR CTD; 9821338; -.
DR eggNOG; KOG3531; Eukaryota.
DR HOGENOM; CLU_284872_0_0_1; -.
DR InParanoid; E3M259; -.
DR OMA; CHLFNSD; -.
DR OrthoDB; 2876516at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0050811; F:GABA receptor binding; IEA:EnsemblMetazoa.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IEA:EnsemblMetazoa.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13193; FERM_C_FARP1-like; 1.
DR CDD; cd17098; FERM_F1_FARP1_like; 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; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FA.
DR InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45858; FERM DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45858:SF5; MOESIN/EZRIN/RADIXIN HOMOLOG 1; 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 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; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 10..294
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 495..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 121584 MW; 4BE77CFD6086F988 CRC64;
MNSSKRGRLV CIKVRMLDDT VAVFHLGHKA VGQTLLDEVC RHLNLLECDY FGLSFIDMNG
NHCWLDREKT ILRQITNGST DAKFYFVVKF YTPNPIDLEE EYTRYLFTMQ IKRDLALGEL
HCSDNTASLL SAYLVQSECG DFSSEDYPDA TYLSHTRFVP NQTLEFQKKV MDNHRNFIGM
TPGESDLAML EVARRCDFYG VKLHAAKDID GNDAALSVMH LGIKVFRQLQ LDTTFSWARI
RKLSFKRRKL LVKLHPDSYQ YLKETVEFSF DTRDECKNFW KKCVEHHAFF RCVQAEEPKK
ETRFFISKGS SFRYHGRTQK QLIDYVREHH KRREPFTRPL RSAASTRKGT YSSTYGLVSD
RPTKHRNGSV YEANQTDPYS SKHQNTHSSM PHIAHISSQP ADHSFSGTLD ARVGTSVTRD
PSSTITQHRL RQLKRSERCI SDVDTVERPQ RSCRPVSNAI NVSSVTNSKE QPDLSISLPN
VLSDDLQMVC KEIEMEQNDP PKSVSGDNFQ QRRSSRDYDN VSEDSYRLSD HERSTRSEVG
VSSKYAAATI FNSTFVARKP GSNVVKRVVA HSKSTPNSTD DEEGALKSAS EYQTFRHIKE
YPFARNANIV PIEIDGPNVD LSSRRSPSAT TTTTRTAPNI TTTVTTTSKV LTSSGAILMK
PKVISNDHQE TSSGTHSSRV SPESGTYGAL GPLPGRVITK DNMMITPEGF KEKKPKPNPP
PKPSFPIQAV HAETEIVREV KTERAQSHPL VHMQEEIPFS RAPLKFEEQK ERKSSLSRPA
LISVQSEDNP DVQKCHLFNS DIPYTLTMRN VESTQSLPYS TFKNVADAKK QAYESNSLKR
VSKSPEFKRR KSLDLVPRKR LPSPGNFSAQ DHTISPTTPD SDVLEYLLRR RSLLGDKSVI
KTKSKRTDPR RQTQPVRFDL PPSPCSPTAG GSTPFISILN DDLFDECVSE SRSLHEDMDR
LDKTTPHNQS ISSFMSQKSR RDSEDSDVMP PPPDEILNRA LISSSRPGPP PPPPKSLAAA
VKVAEMKAAA AGKMHFSGNS KSCHTTDSPP FIDDSPKNSS ASDAPSVPSP QKDRLTFSHF
//