ID A0A3P8U722_AMPPE Unreviewed; 1154 AA.
AC A0A3P8U722;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Erythrocyte membrane protein band 4.1-like 3b {ECO:0000313|Ensembl:ENSAPEP00000033124.1};
GN Name=EPB41L3 {ECO:0000313|Ensembl:ENSAPEP00000033124.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000033124.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000033124.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000033124.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3P8U722; -.
DR Ensembl; ENSAPET00000033993.1; ENSAPEP00000033124.1; ENSAPEG00000023521.1.
DR GeneTree; ENSGT00940000157047; -.
DR Proteomes; UP000265080; Chromosome 10.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 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 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:UP000265080}.
FT DOMAIN 93..374
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 128336 MW; C939D732B5A010E7 CRC64;
MTTESGTDSE AKQLQENKET QKGKGKAASQ PSQAAAEPTS PQNQPEQLPA AAGHSTPARK
EQEQVEEDQV SHRSSTSRLS RSPLRGVKKV KIMQCKITLL DGSDYTLNVE KRVKGHVLFD
KVCDHLNLLE KDYFGITYRD MENQKNWLDP SKELKKQIRT GPWNFAFNVK FYPPDPSQLT
EDITRYYLCL QLRDDVVSGR LPCSFATHTV LGSYTVQSEL GDYDPEELAS DYISELRFAP
NQTKELEEKV MELHKTYKGM TPAEAEMHFL ENAKKLSMYG VDLHHAKDSE GVEIMLGVCA
SGLLIYRDRL RINRFAWPKI LKISYKRNNF YIKIRPGEFE QFESTIGFKL PNHRAAKRLW
KVCVEHHTFF RLVSPEAPPK KFLSLGSKFR YSGRTQAQTR RASSQIIRPA PFFERSSSKR
YNMSRSLDGA PIMENHETLM KDNAAAKVIA KGDIITTVTT EKKVEEDKSE QEDTHKDAAE
TPEAVATTPL RQDTKCSPHV YTADPLPSEL SLPSSPVSST KIRRRRRENA RKRASSVSPA
KSSTGCRRRQ AHADRKAALL EEQALLLSAR KQRLEQGKSR GGTLFSFSLH LPDLSSILDE
DGYITFPDLS EMRFLPECAQ NFLPIKSPSL IPCFLFIFFF LLSTSFSVPY ALTLSFPLAL
CLCYLEPKAA SLTASIAQGY HDHDSSEEEE TDSEQTDFAF DGDITATESE ADEDSEMQTQ
DTEPSADAVK HQTNISELKR SFLETGGSTP GLTEWEKRLS SSPVHSPRAH EAPMIEPLEP
QDTKDEQPTG DEAKEEVNAK ATEAAGYLVK YVVDSIITDG ATSSGPHGIS LSTTMDDDVF
MDGTLKEVEE KTPDSQDEVS ERSVVKVSPG AVRQEVSQAI SDKKGTLIIL KDAEDKEDTE
GKEMSTLDEK EKSVVPREHE TNKNDMLPAS MGKEMFKADT SVVTEAQTTE VKMLSPKVEI
KTDDMIPLKG IDSPKKAMAS WISEEVKTEA SEVISVAAKE MKTSDGLKQN AEIFTFEDIQ
SEQSESNLST LGWVSSSQKA SPDQQEKAVV AVETEAESTK LTAPTSPDIV EVATKDMPVV
HTETKTITYE AAEVDTNGDA DPGVLLSAQT ITSETTSTTT TTHITKTVKG GISETRIEKR
IVITGDADID HDEE
//
