ID U3KE75_FICAL Unreviewed; 903 AA.
AC U3KE75;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Erythrocyte membrane protein band 4.1 like 1 {ECO:0000313|Ensembl:ENSFALP00000013329.2};
GN Name=EPB41L1 {ECO:0000313|Ensembl:ENSFALP00000013329.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000013329.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000013329.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000013329.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; U3KE75; -.
DR STRING; 59894.ENSFALP00000013329; -.
DR Ensembl; ENSFALT00000013385.2; ENSFALP00000013329.2; ENSFALG00000012755.2.
DR eggNOG; KOG3527; Eukaryota.
DR GeneTree; ENSGT00940000158442; -.
DR HOGENOM; CLU_003623_3_1_1; -.
DR Proteomes; UP000016665; Chromosome 20.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UP000016665}.
FT DOMAIN 96..377
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 100409 MW; A66FDE03C05830D2 CRC64;
MTTETGPGSE VRNAQEEAQQ QPLEAAAQGP TAAPSPAGRD TDPHEKLGAQ PDSRNMEPGT
DMEDKDYSET DGLSDKTTPS KTQKSPQKTT KKVKSALCRV TLLDASEYEC EVEKHARGQV
LFDMVCEHLN LLEKDYFGLT FCDSDSQKNW LDPSKEIKKQ IRSGPWNFAF TVKFYPPDPA
QLTEDITRYY LCLQLRADII TGRLPCSFVT HALLGSYAVQ AELGDHDTEE HVGNYVSELR
FAPNQTRELE ERIMELHKTY RGMTPGEAEI HFLENAKKLS MYGVDLHHAK DSEGIDIMLG
VCANGLLIYR DRLRINRFAW PKILKISYKR SNFYIKIRPG EYEQFESTIG FKLPNHRSAK
RLWKVCIEHH TFFRLVSPEP PPKGFLVMGS KFRYSGRTQA QTRQASALID RPAPFFERSS
SKRYTMSRSL DGEFSRPASV SENHDAGPEG EKQDEDGELG SRRRSETEDE EVTTPTKIKE
LKPEHETTPR HKQEFLDKPE DVLLKHQASI NELKRTLKEP NSKLVHRDRD RRLPSSPASS
SPKHEEETPK GTPEKATETM EEDTLEDFAS EHGASLSMES FTQKSLVSSP ERAGVREGPE
ERVKPPRHRA PESDTGDEEP DQEKDSVFLK DNHLAIERKC SSITVSSTSS LEAEVDFTVI
GDFHGTAFED ISRSLPELDK DKSETEDEGL VSLQHTDKVV PGLEEDVKGR DKVSQASPDV
SQPELSAPKA DTVTVKKPEA EGSTPHRVST TDTAQVDGGT PGSRDSTTTA QAGATETALV
TSDHGTKAGK GAAPTTDLRS LSPISSGSAG KEVLTSIFSA TAETLSTSTT THVTKTVKGG
FSETRIEKRI IITGDEDVDQ DQALALAIKE AKLQHPDMLV TKAVVYRETE PSPEERDKKP
QES
//
