ID   A0A3Q1FUF4_9TELE        Unreviewed;       959 AA.
AC   A0A3Q1FUF4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Erythrocyte membrane protein band 4.1 like 3 {ECO:0000313|Ensembl:ENSAPOP00000020094.1};
GN   Name=EPB41L3 {ECO:0000313|Ensembl:ENSAPOP00000020094.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000020094.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000020094.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3Q1FUF4; -.
DR   Ensembl; ENSAPOT00000030163.1; ENSAPOP00000020094.1; ENSAPOG00000023793.1.
DR   GeneTree; ENSGT00940000157047; -.
DR   Proteomes; UP000257200; Unplaced.
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   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:UP000257200}.
FT   DOMAIN          93..389
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..715
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        477..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        681..714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   959 AA;  106224 MW;  1F1A2170EE151264 CRC64;
     MTTESGADSE AKQLQENKET QKGKGKAASQ PSQAAAEPTS PQNQPEQLPA AAGHSTPARK
     EQEQAEEDLV SHRSSTSRLS RSPLRGVKKV KIMQCKITLL DGSDYTLNVE KRVKGHVLFD
     KVCDHLNLLE KDYFGITYRD MENQKNWLDP SKELKKQIRT GPWNFAFNVK FYPPDPSQLT
     EDITRYYLCL QLRDDVVSGR LPCSFATHTV LGSYTVQSEL GDYDPEELGS DYISELRFAP
     NQTKELEEKV MELHKTYKGM TPAEAEMHFL ENAKKLSMYG VDLHHAKLVG SLYESLAPAE
     GEDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKILKISY KRNNFYIKIR PGEFEQFEST
     IGFKLPNHRA AKRLWKVCVE HHTFFRLVSP EAPPKKFLSL GSKFRYSGRT QAQTRRASSQ
     IIRPAPFFER SSSKRYNMSR SLDGAPIMEN HETLMKDNAV AKVITKGDII TAVTTEKKVE
     EDKSEQEDTH KDAAETPEAV ATTPLRQDTK DTEPSAEVVK HQTNISELKR SFLETGGSTP
     GLTEWEKRLS SSPVHSPRAH EAPMIEPLEP QDTNDEQPTG DEAKEEVNAK ATEAAGYLVK
     YVVDSIITDG ATSSGPHGIS LSTTMDDDVF MDGTLKEVEE KTPDSQDEVS ERSVVKVSPG
     AVRQEVSQAI SDKKGTLIIL KDAEDKEDTE GKETSTLDEK EKSVVPREYE TDKNDTLPAS
     IGKEMFKADT SVVAEAQTTE VKMLSPKVEI KTDDMIPLKG IDSPKKAMAS WISEEVKTEA
     SEVISVSAKE MKTSDGLQEN AEIFTFEDVR SEQSESNLVQ ITVSESSTAS LAVSTLGWVS
     SSQKASPDQQ EKAVVAVETE AESAKLTAPT SPDVVEVATK DMPVVHTETK TITYEAAEVD
     TNGDADPGVL LSAQTITSET TSTTTTTHIT KTVKGGISET RIEKRIVITG DADIDHDEE
//