ID A2AUK5_MOUSE Unreviewed; 879 AA.
AC A2AUK5;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE SubName: Full=Erythrocyte membrane protein band 4.1 like 1 {ECO:0000313|Ensembl:ENSMUSP00000099425.2};
GN Name=Epb41l1 {ECO:0000313|Ensembl:ENSMUSP00000099425.2,
GN ECO:0000313|MGI:MGI:103010};
GN Synonyms=Epb4.1l1 {ECO:0000313|MGI:MGI:103010};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000099425.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:15345747}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [2] {ECO:0007829|PubMed:16452087}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [3] {ECO:0007829|PubMed:17114649}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [4] {ECO:0007829|PubMed:18034455}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5] {ECO:0000313|Ensembl:ENSMUSP00000099425.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000099425.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7] {ECO:0000313|Ensembl:ENSMUSP00000099425.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000099425.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; NP_001006665.1; NM_001006664.3.
DR RefSeq; NP_001278049.1; NM_001291120.1.
DR RefSeq; NP_038538.1; NM_013510.4.
DR ProteomicsDB; 340930; -.
DR Antibodypedia; 26438; 107 antibodies from 20 providers.
DR DNASU; 13821; -.
DR Ensembl; ENSMUST00000029155.16; ENSMUSP00000029155.9; ENSMUSG00000027624.21.
DR Ensembl; ENSMUST00000103136.8; ENSMUSP00000099425.2; ENSMUSG00000027624.21.
DR Ensembl; ENSMUST00000103137.10; ENSMUSP00000099426.4; ENSMUSG00000027624.21.
DR GeneID; 13821; -.
DR KEGG; mmu:13821; -.
DR UCSC; uc008nni.2; mouse.
DR AGR; MGI:103010; -.
DR CTD; 2036; -.
DR MGI; MGI:103010; Epb41l1.
DR VEuPathDB; HostDB:ENSMUSG00000027624; -.
DR GeneTree; ENSGT00940000158442; -.
DR OrthoDB; 5391231at2759; -.
DR TreeFam; TF351626; -.
DR BioGRID-ORCS; 13821; 0 hits in 45 CRISPR screens.
DR ChiTaRS; Epb41l1; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000027624; Expressed in visual cortex and 242 other cell types or tissues.
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 1: Evidence at protein level;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Proteomics identification {ECO:0007829|EPD:A2AUK5,
KW ECO:0007829|MaxQB:A2AUK5};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
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..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..696
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 447..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 98315 MW; 2EB501A4B4DCA325 CRC64;
MTTETGPDSE VKKAQEETPQ QPEAAAAVTT PVTPAGHSHP ETNSNEKHLT QQDTRPAEQS
LDMDDKDYSE ADGLSERTTP SKAQKSPQKI AKKFKSAICR VTLLDASEYE CEVEKHGRGQ
VLFDLVCEHL NLLEKDYFGL TYCDADSQKN 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 SVSENHDAGP DGDKREDDAE SGGRRSEAEE GEVRTPTKIK
ELKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWDRERRLPS
SPASPSPKGT PEKASERAGL REGSEEKVKP PRPRAPESDT GDEDQDQERD AVFLKDNHLA
IERKCSSITV SSTSSLEAEV DFTVIGDYHG GAFEDFSRSL PELDRDKSDS ETEGLVFARD
LKGPSSQEDE SGGLEDSPDR GACSTPEMPQ FESVKAETMT VSSLAIRKKI EPEAMLQSRV
SAADSTQVDG GTPMVKDFMT TPPCITTETI STTMENSLKS GKGAAAMIPG PQTVATEIRS
LSPIIGKDVL TSTYGATAET LSTSTTTHVT KTVKGGFSET RIEKRIIITG DEDVDQDQAL
ALAIKEAKLQ HPDMLVTKAV VYRETDPSPE ERDKKPQES
//
