ID A0A484C9V4_PERFV Unreviewed; 1031 AA.
AC A0A484C9V4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=FERM domain-containing protein {ECO:0000259|PROSITE:PS50057};
GN ORFNames=EPR50_G00186820 {ECO:0000313|EMBL:TDH00286.1};
OS Perca flavescens (American yellow perch) (Morone flavescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8167 {ECO:0000313|EMBL:TDH00286.1, ECO:0000313|Proteomes:UP000295070};
RN [1] {ECO:0000313|EMBL:TDH00286.1, ECO:0000313|Proteomes:UP000295070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YP-PL-M2 {ECO:0000313|EMBL:TDH00286.1};
RC TISSUE=Blood {ECO:0000313|EMBL:TDH00286.1};
RA Feron R., Morvezen R., Bestin A., Haffray P., Klopp C., Zahm M., Cabau C.,
RA Roques C., Donnadieu C., Bouchez O., Christie M., Larson W., Guiguen Y.;
RT "A chromosome-scale genome assembly of the yellow perch, Perca
RT flavescens.";
RL Submitted (JAN-2019) 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:TDH00286.1}.
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DR EMBL; SCKG01000018; TDH00286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A484C9V4; -.
DR STRING; 8167.A0A484C9V4; -.
DR OrthoDB; 5391231at2759; -.
DR Proteomes; UP000295070; Chromosome 18.
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; cd17106; FERM_F1_EPB41L; 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; 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; 2.
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:UP000295070}.
FT DOMAIN 208..490
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 114630 MW; 8AC45FB41F256D2C CRC64;
MTTEAGSETE VKEKAEESAA QPDQSEKAKE ETQEVPNAEG EEKEKEKEKE GKEGKGIARY
LPTWLKKQKS QSQTSPTKEV PPTEEAVSKV TQGEDGPAPE VNGHAEEEEE EREAVKSEHV
KEKEAESHST ASADTEPAKE EKLEESAEKV PDETTVTTEG EGAEEQKKEQ EGEEEEEEEE
GGGGGEEGHT SIFQSPLRLV RKTKMKLMAC HVALLDGTDF NCEVEKRAKG QYLFFKVCEH
LNLMEKDYFG LLYTDSHEQK CWLDPTKEIK RQIRSNNWQF VFNVKFYPPD PSLLTEDITR
YLLCLQLRED VASGRLPCSF VTHALLGSYT LQAEVGDYEP DQPRPLDSVS QLTFAPNQSK
EMEEKILELH KSHRGMTPAQ ADTQFLENAK KLSMYGVDLH HAKDSEGVDI MLGVCANGLL
VYKDRLRINR FAWPKILKIS YKRNNFYIKI RPGETEQFES TVGFKLQNHR SAKRLWKVCV
ENHSFFRLNA PEPPAKARFL TLGSKFRYSG RTQAQTRVAS SLIDRPAPNF ERTSSKRISR
SLDGAPVINI TEASSENGRE PHLELHSDSK VKEVDLSPSD AEATPTQSLG ASELALSQDH
DKTQEDVLKH QASISQLKRS FMEAPPPSPP QPNQWEKRLT SSPATIRIQQ QQHVESAPQA
EAAAADNTMS DTKEPAKTTE VEIEETVVVQ EVSIAPKPGL VTVTTSSPAG PPAEQETREQ
EVTVEEEVAV AEEAKVSKQE SVSSESDSEE EAEYHPNVSV SIYHTQIPEE KEEEEEQEEE
AEDKTAAEQG MSAPDAPSLP AEVSQAVEAT SQEVEEDAEK RKNAEEEKEA EREMEESADD
PMMTPEEAPN GHALPEESAT GMVDPAEEEE EPKMNGEASL AEAEPRPQVI CCSEPPVVKT
EMVTISDTFA AQKTEIATKE VPIVHTETKT ITYEAAQLDG NSDGEPGVLM TAQTITSESL
CTTTTTHITK MLKGGLSETR IEKRIVITGD CDIDHDQALA QAIKEAKEQH PDMSVTRVVV
HKETELAEEE D
//
