ID A0A1W2P6I5_MOUSE Unreviewed; 513 AA.
AC A0A1W2P6I5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Erythrocyte membrane protein band 4.1 like 2 {ECO:0000313|Ensembl:ENSMUSP00000151233.2};
DE Flags: Fragment;
GN Name=Epb41l2 {ECO:0000313|Ensembl:ENSMUSP00000151233.2,
GN ECO:0000313|MGI:MGI:103009};
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:ENSMUSP00000151233.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:19144319}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [2] {ECO:0007829|PubMed:19131326}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000151233.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000151233.2,
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 [4] {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 [5] {ECO:0000313|Ensembl:ENSMUSP00000151233.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000151233.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR ProteomicsDB; 332406; -.
DR Antibodypedia; 1358; 271 antibodies from 35 providers.
DR Ensembl; ENSMUST00000219805.2; ENSMUSP00000151233.2; ENSMUSG00000019978.17.
DR Ensembl; ENSMUST00000219900.2; ENSMUSP00000151332.2; ENSMUSG00000019978.17.
DR AGR; MGI:103009; -.
DR MGI; MGI:103009; Epb41l2.
DR VEuPathDB; HostDB:ENSMUSG00000019978; -.
DR GeneTree; ENSGT00940000155617; -.
DR OMA; ESICTTM; -.
DR ChiTaRS; Epb41l2; mouse.
DR Proteomes; UP000000589; Chromosome 10.
DR Bgee; ENSMUSG00000019978; Expressed in retinal neural layer and 279 other cell types or tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0008092; F:cytoskeletal protein binding; 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; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR PANTHER; PTHR23280:SF17; BAND 4.1-LIKE PROTEIN 2; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 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 Proteomics identification {ECO:0007829|EPD:A0A1W2P6I5,
KW ECO:0007829|MaxQB:A0A1W2P6I5};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 211..492
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 513
FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000151233.2"
SQ SEQUENCE 513 AA; 58479 MW; E9AAB9C1C3B5A758 CRC64;
MTTEVGSASE VKKGSDQAGA DASKEKAKEV ENEQTPVSEP EEEKGSQPGP PVERQSTPRL
RKRGKDPSEN RGISRFIPPW LKKQRSYNLV VAKDGGDKKE PTQADVEDQI LGKEESLPEE
ESRAKGDAEE MAQRKHLEVQ VEVREAKPAL KSSVETQPAE EVRKDKEETI QDTQEEKLEG
GAAKRETKEV QTSELKAEVA SQKATKKTKT VLAKVTLLDG TEYSCDLEKR AKGQVLFDRV
CEHLNLLEKD YFGLLFQDHP EQKNWLDPAK EIKRQLKNLP WLFTFNVKFY PPDPSQLTED
ITRYFLCLQL RQDIASGRLP CSFVTHALLG SYTLQAEHGD YDPEEYDSID LGDFQFAPAH
TKELEEKVSE LHKTHRGLSP AQADSQFLEN AKRLSMYGVD LHHAKDSEGV DIKLGVCANG
LLIYKDRLRI NRFAWPKILK ISYKRSNFYI KVRPAELEQF ESTIGFKLPN HRAAKRLWKV
CVEHHTFYRL VSPEQPPKTK FLTLGSKFRY SGR
//
