E41L2_MOUSE
ID E41L2_MOUSE Reviewed; 988 AA.
AC O70318; G3X9B8;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Band 4.1-like protein 2;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 2 {ECO:0000312|MGI:MGI:103009};
DE AltName: Full=Generally expressed protein 4.1;
DE Short=4.1G;
GN Name=Epb41l2 {ECO:0000312|MGI:MGI:103009};
GN Synonyms=Epb4.1l2 {ECO:0000312|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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH FKBP2.
RC TISSUE=Brain;
RX PubMed=9531554; DOI=10.1083/jcb.141.1.143;
RA Walensky L.D., Gascard P., Fields M.E., Blackshaw S., Conboy J.G.,
RA Mohandas N., Snyder S.H.;
RT "The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue
RT of the erythrocyte membrane cytoskeletal protein 4.1.";
RL J. Cell Biol. 141:143-153(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-606, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-86; SER-201; SER-582
RP AND SER-698, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND TYR-606, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-201; SER-395;
RP SER-543; SER-555; SER-561; SER-582; SER-610; SER-630 AND THR-745, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Required for dynein-dynactin complex and NUMA1 recruitment at
CC the mitotic cell cortex during anaphase.
CC {ECO:0000250|UniProtKB:O43491}.
CC -!- SUBUNIT: Interacts with FCGR1A. Interacts with TRPC4 (By similarity).
CC Interacts (via CTD domain) with FKBP2 (PubMed:9531554). Interacts with
CC NUMA1; this interaction is negatively regulated by CDK1 during
CC metaphase and promotes anaphase-specific localization of NUMA1 in
CC symmetrically dividing cells (By similarity).
CC {ECO:0000250|UniProtKB:O43491, ECO:0000269|PubMed:9531554}.
CC -!- INTERACTION:
CC O70318; Q9JLB0: Pals2; NbExp=3; IntAct=EBI-643339, EBI-771456;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cell cortex {ECO:0000250|UniProtKB:O43491}. Cell membrane
CC {ECO:0000250|UniProtKB:O43491}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF044312; AAC40083.1; -; mRNA.
DR EMBL; AC153547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466540; EDL04798.1; -; Genomic_DNA.
DR CCDS; CCDS23754.1; -.
DR RefSeq; NP_001186194.1; NM_001199265.1.
DR RefSeq; NP_038539.2; NM_013511.3.
DR AlphaFoldDB; O70318; -.
DR SMR; O70318; -.
DR BioGRID; 199460; 35.
DR IntAct; O70318; 8.
DR STRING; 10090.ENSMUSP00000055122; -.
DR iPTMnet; O70318; -.
DR PhosphoSitePlus; O70318; -.
DR SwissPalm; O70318; -.
DR EPD; O70318; -.
DR jPOST; O70318; -.
DR MaxQB; O70318; -.
DR PaxDb; O70318; -.
DR PeptideAtlas; O70318; -.
DR PRIDE; O70318; -.
DR ProteomicsDB; 277537; -.
DR Antibodypedia; 1358; 246 antibodies from 34 providers.
DR DNASU; 13822; -.
DR Ensembl; ENSMUST00000053748; ENSMUSP00000055122; ENSMUSG00000019978.
DR Ensembl; ENSMUST00000092645; ENSMUSP00000090314; ENSMUSG00000019978.
DR GeneID; 13822; -.
DR KEGG; mmu:13822; -.
DR UCSC; uc007erk.2; mouse.
DR CTD; 2037; -.
DR MGI; MGI:103009; Epb41l2.
DR VEuPathDB; HostDB:ENSMUSG00000019978; -.
DR eggNOG; KOG3527; Eukaryota.
DR GeneTree; ENSGT00940000155617; -.
DR HOGENOM; CLU_003623_0_0_1; -.
DR InParanoid; O70318; -.
DR OMA; DSVCEHL; -.
DR OrthoDB; 262540at2759; -.
DR PhylomeDB; O70318; -.
DR TreeFam; TF351626; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 13822; 0 hits in 41 CRISPR screens.
DR ChiTaRS; Epb41l2; mouse.
DR PRO; PR:O70318; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O70318; protein.
DR Bgee; ENSMUSG00000019978; Expressed in retinal neural layer and 276 other tissues.
DR ExpressionAtlas; O70318; baseline and differential.
DR Genevisible; O70318; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:MGI.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISS:MGI.
DR GO; GO:0042731; F:PH domain binding; IDA:MGI.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:MGI.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR030546; E41L2.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
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:SF17; PTHR23280:SF17; 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 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 Acetylation; Actin-binding; Cell cycle; Cell division; Cell membrane;
KW Cytoplasm; Cytoskeleton; Membrane; Mitosis; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43491"
FT CHAIN 2..988
FT /note="Band 4.1-like protein 2"
FT /id="PRO_0000219398"
FT DOMAIN 211..492
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..651
FT /note="Hydrophilic"
FT REGION 514..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..837
FT /note="Spectrin--actin-binding"
FT REGION 804..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..988
FT /note="C-terminal (CTD)"
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 COMPBIAS 670..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:O43491"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43491"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43491"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43491"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 606
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 745
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 660
FT /note="F -> L (in Ref. 1; AAC40083)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="E -> G (in Ref. 1; AAC40083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 988 AA; 109940 MW; D3DA78BFA14E3FBB 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 SGRTQAQTRE ASTLIDRPAP QFERASSKRV
SRSLDGAPIG VVDQSPPGEG SVPGPGVISY TTIQDGRRDS KSPTKATPLP AEGKKNTLRV
DGDNIYVRHS NLMLEDLDKA QEAILKHQAS ISELKRNFMA STPEPRPSEW EKRRVTPLPF
QPQASSHETL NVVEEKKRAE VGKDESVITE EMNGKEMSPG HGPGETRKVE PVAHKDSTSL
SSESSSSSSE SEEDVGEYQP HHRVTEGTIR EEQEECDEEL EEEPGQGAKV VEREAAVPDA
VPDRQAGASV LPVETEAQEH VVAQKLPGEK GAHGGTAEQD PREEAEEDPH RVNGEVPHLD
LDGLPEIICC SEPPVVKTEM VTISDASQRT EISTKEVPIV QTETKTITYE SPQIDGGAGG
DSGVLLTAQT ITSESASTTT TTHITKTVKG GISETRIEKR IVITGDAALD HDQALAQAIR
EAREQHPDMS VTRVVVHKET ELAEEGEE
