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Database: UniProt
Entry: A0A674CLZ0_SALTR
LinkDB: A0A674CLZ0_SALTR
Original site: A0A674CLZ0_SALTR 
ID   A0A674CLZ0_SALTR        Unreviewed;       875 AA.
AC   A0A674CLZ0;
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 3 {ECO:0000313|Ensembl:ENSSTUP00000084790.1};
GN   Name=LOC115195571 {ECO:0000313|Ensembl:ENSSTUP00000084790.1};
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:ENSSTUP00000084790.1, ECO:0000313|Proteomes:UP000472277};
RN   [1] {ECO:0000313|Ensembl:ENSSTUP00000084790.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A674CLZ0; -.
DR   Ensembl; ENSSTUT00000090196.1; ENSSTUP00000084790.1; ENSSTUG00000036735.1.
DR   GeneTree; ENSGT00940000157047; -.
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: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:UP000472277}.
FT   DOMAIN          92..388
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..761
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..777
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   875 AA;  98371 MW;  774002A07540B038 CRC64;
     MTTEPNSESS ADQQEASAVP LLEADSFPPA AAHSTPVRKK QNGERAERGV VPQENQLEPS
     QAEEDRTSHR SSTSKLSRSP GGGRSVRSYK TMQCKVTLLD GSDYTCVVEK RERGHVLFHK
     VCEQLNLLEK DYFGITFRDI ENQKNWLDPS KEMKKQIRGV AWNFSFNVKF YPPDPAQLSE
     DITRYYLCLQ LRDDVVSGRL PCSFATHTVL GSYTVQSELG DYDPEESGTD YVSEFRFAPN
     QTKELEEKIM DLHKNYKGMM PAEAEMHFLE NVKKLSMYGV DLHHAKLVGS LFECLSPAKG
     EDSEGVEIML GVCSSGLLIY RDRLRINRFA WPKVLKISYK RNNFYIKIRP GEFEQFESTI
     GFKLPNHRAA KRLWKVCVEH HTFFRLVSPE TPPKKFLNLG SKFRYSGRTQ AQTRRASSQI
     VRPAPCFERS TSKRYIMSRS LDGAPQSTPK RSSPQKTVSP RIKPPASLNG TKPTEMGSDL
     YGRAKGIAVS DLITTVTPEK KVEERKAEEE VEVEVQVEEE DETTKATEMS QPSPTSPIRH
     DTKTDLTDTC VDGELTATES DQDDESELKT QDTVGTPEEL LKHATNISEL KRSFLETGAD
     TAGLTEWEKR LSSSPLRSLR LDEAPMIEPL ELDEVPSKED EREDERAMAA GGSIEEEINH
     SPVDTKTTVP KPTFEEMSPE LTALLQSARY QTSTRGWTAS PAHSQALLKT TEKVERIVLQ
     TEVVSSQQTE EVEDQPKEQP AEDQEQPVEK QPDDRPDNIE KQAGQQPEQT SVLESPEVLT
     FNRADVMEET EMLVTQEVPV IHTEMKTITY RSLEGDADTD PEAGVLMSAQ TITSETTSTT
     TTTHITKTVK GGISETRIEK RIVISGDADI DHDED
//
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