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Database: UniProt
Entry: A0A3Q2V7L6_HAPBU
LinkDB: A0A3Q2V7L6_HAPBU
Original site: A0A3Q2V7L6_HAPBU 
ID   A0A3Q2V7L6_HAPBU        Unreviewed;       774 AA.
AC   A0A3Q2V7L6;
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=Protein 4.1-like {ECO:0000313|Ensembl:ENSHBUP00000006580.1};
GN   Name=EPB41L3 {ECO:0000313|Ensembl:ENSHBUP00000006580.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000006580.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000006580.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q2V7L6; -.
DR   Ensembl; ENSHBUT00000005060.1; ENSHBUP00000006580.1; ENSHBUG00000008062.1.
DR   GeneTree; ENSGT00940000157047; -.
DR   Proteomes; UP000264840; 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:UP000264840}.
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          478..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Basic and acidic 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        478..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   774 AA;  86468 MW;  EFBDD909E6438868 CRC64;
     MTTESGADSE AKQPQENKET EKGKAKAASQ PSQVAAEPAL PQNQPEQLPA AVGHSTPARK
     EQEQQEEDLV SHRSSTSRLS RSPLRGVKKV KIMQCKVTLL DGLDFTLNVE KRAKGQFLFD
     KVCDHLNLLE KDYFGITYRD VENQKNWLDP SKELKKQIRT GPWNFAFNVK FYPPDPSQLT
     EDITRYYLCL QLRDDVVSGR LPCSFATHTV LGSYTAQSEL GDYDSEELAS DYLSELRFAP
     NQTKELEEKV MELHKTYKGM SPADAEMHFL ENAKKLSMYG VDLHHAKLVG NLYECLAPAE
     GEDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKILKISY KRNNFYIKIR PGEFEQFEST
     IGFKLPNHRA AKRLWKVCVE HHTFFRLVSP EAPPKKFLTL GSKFRYSGRT QAQTRRASSQ
     IIRPAPFFER TSSKRYNMSR SLDGAPIMEN HETLMKDNAA DGEAKVIAKG DIITTVTTEK
     KAEEEKAEEG DAKKDTAETP EPAATSPLRQ DTKTDSEQTD FAFDGEMTAT ESEADEDSEM
     RTQDTEPPAE VVKHQTNISE LKRSFLETDG SITTPGLTEW EKRLSSSPMR SPRSDEAPMI
     EPLELDTKED EPAADETKEV EPKITEAPAG QEEKPVIEME ALPAKSAGPS SPDITAVATK
     DMPVIHTETK TITYEAAEVE TNGDADPGVL LSAQTITSET TSTTTTTHIT KTVKGGISET
     RIEKRIVITG DADIDHDEAL AQAIKEAKEQ HPDMSVTKVV VHKETEITPE EGED
//
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