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Database: UniProt
Entry: A0A674DV51_SALTR
LinkDB: A0A674DV51_SALTR
Original site: A0A674DV51_SALTR 
ID   A0A674DV51_SALTR        Unreviewed;       680 AA.
AC   A0A674DV51;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Band 4.1-like protein 1 {ECO:0000313|Ensembl:ENSSTUP00000099451.1};
GN   Name=LOC115150885 {ECO:0000313|Ensembl:ENSSTUP00000099451.1};
OS   Salmo trutta (Brown trout).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000099451.1, ECO:0000313|Proteomes:UP000472277};
RN   [1] {ECO:0000313|Ensembl:ENSSTUP00000099451.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A674DV51; -.
DR   Ensembl; ENSSTUT00000106736.1; ENSSTUP00000099451.1; ENSSTUG00000043834.1.
DR   GeneTree; ENSGT00940000158442; -.
DR   Proteomes; UP000472277; 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: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:UP000472277}.
FT   DOMAIN          77..358
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..443
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   680 AA;  77298 MW;  02F0312870075199 CRC64;
     MPTEPGPESE VKNAAEVSSQ QKGAAAGMQD SASDGKMAKQ DSKLIDDHRE TDDVSEKTTP
     CKTPKSPQKT SKRPKTVPFK VTLLDTSDYE AGIEKHCKGQ ALLDKVCEHL NLLEKDYFGL
     TFSEADSQKN WLDPSKEIKK QMRTAPWHFA FSVKFYPPDP SQLTEDITRY YLCLQLRDDM
     LSGRLPCSFV THALLGSYAV QAELGDYDTD DHGPDYVSDF RFAPNQTREL EERVMELHRN
     YRGMTPADAE INFLENAKKL SMYGVDLHHA KDSEGIDIML GVCANGLLIY RDRLRINRFA
     WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRAA KRLWKVCIEH HTFFRLVSPE
     PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPHFERS TSKRYLLSRS LDGGRYHGCQ
     DQEDHEEDQD EERDPEEDQD QEEAGVTTPS KKKEIKFLDK SEDVLLKHQA SINELKKALR
     GPNSKLTNRE KRLSRTSPGG TPERKAVSRE NWERRPRPGS TSEEDHERDT VVFMKETQLG
     IERKCSSITV SSTSSLEAEV DFTVIMDLHT GVEDFSKGLS ELGEKDAMKG HNRYLISRLM
     LTVCVVFQTV KGGYSETRIE KRIIITGDDD VDQHQALAMA IQEAKQQHPD MLVTKAVVVR
     ETESPAKEQH RKSEVGGAAM
//
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