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Database: UniProt
Entry: A0A340WQH4_LIPVE
LinkDB: A0A340WQH4_LIPVE
Original site: A0A340WQH4_LIPVE 
ID   A0A340WQH4_LIPVE        Unreviewed;       905 AA.
AC   A0A340WQH4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Band 4.1-like protein 3 isoform X2 {ECO:0000313|RefSeq:XP_007449220.1};
GN   Name=EPB41L3 {ECO:0000313|RefSeq:XP_007449220.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007449220.1};
RN   [1] {ECO:0000313|RefSeq:XP_007449220.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_007449220.1; XM_007449158.1.
DR   AlphaFoldDB; A0A340WQH4; -.
DR   GeneID; 103070519; -.
DR   CTD; 23136; -.
DR   OrthoDB; 5319111at2759; -.
DR   Proteomes; UP000265300; 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   CDD; cd17203; FERM_F1_EPB41L3; 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; IPR030691; Band4.1-L3_FERM_F1.
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; 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:UP000265300}.
FT   DOMAIN          110..391
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          464..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..730
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   905 AA;  100810 MW;  D25BFE85BF080043 CRC64;
     MTTESGSDLE SKPEQEAEPQ EGHAGAQLGA QPGAEPDTEE QPRALEQLEE AAAHSTPVRK
     EVADKDQEFA AEPAKQPEYQ QFEDDKLSQK SSSSKLSRSP LKIVKKPKSM QCKVILLDGS
     EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY FGLTYRDAEN QKNWLDPAKE IKKQIRSGAW
     HFSFNVKFYP PDPSQLSEDI TRYYLCLQLR DDIVSGRLPC SSVTLATLGS YTVQSELGDY
     DPDECGSDYI SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMYFLENA KKLSMYGVDL
     HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRSNFYIK IRPGEFEQFE
     STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL TLGSKFRYSG RTQAQTRRAS
     ALIDRPAPYF ERSSSKRYTM SRSLDGEVGT GQYITTKGIS QTNLITTVTP EKKAEEEQGE
     EDDRRQKAEE STPVAAIRPE GKTDSERTDT AADGETTATE SDQEEDAELK AQELDKTQDD
     LMKHQTNISE LKRTFLETST DTAITNEWEK RLSTSPVRLA ARQEEAPMIE PLVPEETKQS
     SGEKLMDGSE IFSLLESARK PTEFIGGVAS TSQSWVQKME AKMESGKIET ETTQHPQPLS
     TQKVVQETAL VEERHVMNVH TSGDSSYAAR DDMDAVTQAA SADVSDVKGK EVSALTEGAK
     EEKGEVADKA VLEQGEVAAA SQEPEEEQSA AIHVSEASEQ KPHFESSTVK TETISFGSVS
     PGGVKLEIST KEVPVVHTET KTITYESSQV DLGADLEPGV LMSAQTITSE TTSTTTTTHI
     TKTVKGGISE TRIEKRIVIT GDADIDHDQA LAQAIKEAKE QHPDMSVTKV VVHKETEITP
     EDGED
//
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