ID A0A3P9PUI6_POERE Unreviewed; 1298 AA.
AC A0A3P9PUI6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Erythrocyte membrane protein band 4.1 like 1 {ECO:0000313|Ensembl:ENSPREP00000025547.1};
GN Name=EPB41L1 {ECO:0000313|Ensembl:ENSPREP00000025547.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000025547.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000025547.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000025547.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSPRET00000025802.1; ENSPREP00000025547.1; ENSPREG00000017165.1.
DR GeneTree; ENSGT00940000158442; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000017165; Expressed in caudal fin and 1 other cell type or tissue.
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 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:UP000242638}.
FT DOMAIN 52..333
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1298 AA; 145691 MW; 3ED570442ED03169 CRC64;
MQDSSSDNKM AKQEQNSKHQ DDHRETEDTS EKTSPNKNLK SPQKGSKRLK TATFKVALLD
SSEYEGEIEK HSKGQTLMDM VCEHLNLLEK DYFGLTFADT ESQKNWLDPS KDIKKQMRNS
PWQFAFAVKF YPPDPSQLTE DITRYYLCLQ LRDDILSGRL PCSFVTHALL GSYAIQAELG
DYDLDDHGSD YVGDFRFAPN QTRELEERVM DLHRTYKGMT PAEAEMNFLE NAKKLSMYGV
DLHHAKDSEG IEIMLGVCAN GLLIYRDRLR INRFAWPKIL KISYKRSNFY IKIRPGEYEQ
FESTIGFKLP NHRAAKRLWK VCIEHHTFFR LVSPEPPPKG FLVMGSKFRY SGRTQAQTRQ
ASALIDRPAP HFERSASRRY LLSRSLDGEF SRPVSSMCEN HDGLSRRSAS EQRRLRSPSV
DEQEQEADLE PSLDQDEDDR DPDQSQDMEQ DKDQDGNTTP SRKREIRFLD KSQDVLLKHQ
ASINELKRAL REPNSKLMAR EKRLSATSPT GTPEKKALGG RSVGKDAVNS PSVEGFVQKA
LVTSPEGSEE WVLIEKQQPY QPDHDWRAEE KNKSHISDSS WDKKELEKEI DITKMIHKEE
AGYIRKEVKS HIDEFPSART PREAAVCSET WPSAIQLPEN VDWLQDKSQS KPSQASGPEA
NSDAAPGSRQ IKDKMGSKLR KKGRPQSLNV GIPAELNRKS GSDSSGEDNE DSDSDNTSEK
TSKRGDQSDA SPVIMRKDNQ GLTKDQFVGV CKDNRKEEFG EVKEVSSQVK QKVNQMGMAT
IDLGMLNGPG KIEHDSSLPS GKVEHVVKVR GKGLIDNKEL AEVKLRQVRT HERKVSSSGG
EDVEGFLGDR SQRTSLHRLS GSSYQSEITR IVPLKPERSK SVACKDERDQ LGQEEFTRLV
KREYRWSVGS PEGSSDLHWT DIAGFHQAFP GDPEGFAKME NLDEGFQASR GSMENQQFNL
KGSALPKVAP PAPPVKTQKA KESGLILRNS RNAGREQSLD AAKKRHSEPV STPAIYEEPF
GDLKKESGER RPQPGLASEE EQERDTVASM RDTQLGIERK CSSMTVSSTS SLEAEVDFTV
ITDLHSGTED FSKGGSEFGE REQQPEVGRE DFEETSRFYS ARLMGSRDKF PMEEKLPEEG
THEPPVARKD ASAVSVAHKL KRTDTNGSEV HQNITDVSPQ SPAAVSSQET PAAPKENGSP
VKASPQGRES VVSPLTITAE SITSATTTQV TKTVKGGYSE TRIEKRIIIT GDDDVDQHQA
LAMAIQEAKQ QHPDMLVTKA VVIRETESPT EEQRRAES
//
