ID A0A6J3Q0M9_TURTR Unreviewed; 869 AA.
AC A0A6J3Q0M9;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Band 4.1-like protein 1 isoform X2 {ECO:0000313|RefSeq:XP_033695666.1, ECO:0000313|RefSeq:XP_033695667.1};
GN Name=EPB41L1 {ECO:0000313|RefSeq:XP_033695666.1,
GN ECO:0000313|RefSeq:XP_033695667.1, ECO:0000313|RefSeq:XP_033695668.1,
GN ECO:0000313|RefSeq:XP_033695669.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033695668.1};
RN [1] {ECO:0000313|RefSeq:XP_033695666.1, ECO:0000313|RefSeq:XP_033695667.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033695666.1,
RC ECO:0000313|RefSeq:XP_033695667.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_033695666.1; XM_033839775.1.
DR RefSeq; XP_033695667.1; XM_033839776.1.
DR RefSeq; XP_033695668.1; XM_033839777.1.
DR RefSeq; XP_033695669.1; XM_033839778.1.
DR OrthoDB; 5391231at2759; -.
DR Proteomes; UP000245320; Chromosome 15.
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; cd17201; FERM_F1_EPB41L1; 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:SF24; BAND 4.1-LIKE PROTEIN 1; 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:UP000245320}.
FT DOMAIN 97..378
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 97249 MW; 0E996C893C430E2C CRC64;
MTTETGPDSE VKKAQEEAPQ QPEAAAAATT PVTPAGHGHP EANSNEKHPP HQDARPAEQS
LDMEEKDFGE ADGLSERTTP SKAQKSPQKI AKKYKSAVCR VTLLDASEYE CEVEKHGRGQ
VLFDLVCEHL NLLEKDYFGL TFCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP
AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDAE EHVGNYVSEL
RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML
GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA
KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS
SSKRYTMSRS LDGAEFSRPA SVSENHDARP DSDKREEDGE SGGRRSEAEE GEVRTPTKIK
ELKFLDKPED VLLKHQASIN ELKRTLKEPN SKLIHRDRDW ERERRLPSSP ASPSPKGTPE
KVNERAGLRE GSEEKVKPPR PRAPESDTGD EDQDQERDAV FLKDNHLAIE RKCSSITVSS
TSSLEAEVDF TVIGDYHGSA FEDFSRSLPE LDRDKSDSET EGLVFSRDLN KRGPSQDDES
GGIEDSPDRR ACSTPDMPQF EPVKTETMTV SSLAIRKKIE PEAVLQTRVA TVDTTQQVDG
TAPGGKEFIT TTPSITTETI STTMENSLKS GKGAAAMIPG PQTVATEIRS LSPIIGKDVL
TSTYGATAET LSTSTTTHVT KTVKGGFSET RIEKRIIITG DEDVDQDQAL ALAIKEAKLQ
HPDMLVTKAV VYRETDPSPE ERDKKPQES
//