E41LB_MOUSE
ID E41LB_MOUSE Reviewed; 527 AA.
AC Q9JMC8; A2ALK7;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Band 4.1-like protein 4B;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 4B {ECO:0000312|MGI:MGI:1859149};
DE AltName: Full=Protein EHM2;
GN Name=Epb41l4b {ECO:0000312|MGI:MGI:1859149};
GN Synonyms=Ehm2 {ECO:0000312|MGI:MGI:1859149},
GN Epb4.1l4b {ECO:0000312|MGI:MGI:1859149},
GN Lulu2 {ECO:0000250|UniProtKB:Q9H329};
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 TISSUE SPECIFICITY.
RX PubMed=10783258; DOI=10.1006/geno.2000.6154;
RA Shimizu K., Nagamachi Y., Tani M., Kimura K., Shiroishi T., Wakana S.,
RA Yokota J.;
RT "Molecular cloning of a novel NF2/ERM/4.1 superfamily gene, Ehm2, that is
RT expressed in high-metastatic K1735 murine melanoma cells.";
RL Genomics 65:113-120(2000).
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 FUNCTION, INTERACTION WITH ARHGEF18, PHOSPHORYLATION, AND MUTAGENESIS OF
RP SER-385; SER-414; SER-419 AND THR-424.
RX PubMed=22006950; DOI=10.1083/jcb.201104118;
RA Nakajima H., Tanoue T.;
RT "Lulu2 regulates the circumferential actomyosin tensile system in
RT epithelial cells through p114RhoGEF.";
RL J. Cell Biol. 195:245-261(2011).
CC -!- FUNCTION: Up-regulates the activity of the Rho guanine nucleotide
CC exchange factor ARHGEF18 (PubMed:22006950). Involved in the regulation
CC of the circumferential actomyosin belt in epithelial cells
CC (PubMed:22006950). Promotes cellular adhesion, migration and motility
CC in vitro and may play a role in wound healing (By similarity). May have
CC a role in mediating cytoskeletal changes associated with steroid-
CC induced cell differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q9H329, ECO:0000269|PubMed:22006950}.
CC -!- SUBUNIT: Interacts (via FERM domain) with ARHGEF18 (via C-terminus);
CC the interaction activates ARHGEF18. {ECO:0000269|PubMed:22006950}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H329}. Cell
CC junction, tight junction {ECO:0000250|UniProtKB:Q9H329}.
CC Note=Accumulates along apical cell-cell boundaries and is also detected
CC in the cytoplasm in a punctate manner. {ECO:0000250|UniProtKB:Q9H329}.
CC -!- TISSUE SPECIFICITY: Expressed in mouse liver cells, with lower amounts
CC in lung, kidney and in 7- to 17-day embryos. Expression not detected in
CC adult mouse heart, brain, spleen, skeletal muscle or testis.
CC {ECO:0000269|PubMed:10783258}.
CC -!- PTM: May be negatively regulated by phosphorylation.
CC {ECO:0000269|PubMed:22006950}.
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DR EMBL; AB032366; BAA96078.1; -; mRNA.
DR EMBL; AL805921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51180.1; -.
DR RefSeq; NP_062300.2; NM_019427.2.
DR AlphaFoldDB; Q9JMC8; -.
DR SMR; Q9JMC8; -.
DR STRING; 10090.ENSMUSP00000030142; -.
DR iPTMnet; Q9JMC8; -.
DR PhosphoSitePlus; Q9JMC8; -.
DR jPOST; Q9JMC8; -.
DR MaxQB; Q9JMC8; -.
DR PaxDb; Q9JMC8; -.
DR PeptideAtlas; Q9JMC8; -.
DR PRIDE; Q9JMC8; -.
DR ProteomicsDB; 277541; -.
DR Antibodypedia; 29426; 81 antibodies from 22 providers.
DR Ensembl; ENSMUST00000030142; ENSMUSP00000030142; ENSMUSG00000028434.
DR GeneID; 54357; -.
DR KEGG; mmu:54357; -.
DR UCSC; uc008sxy.2; mouse.
DR CTD; 54566; -.
DR MGI; MGI:1859149; Epb41l4b.
DR VEuPathDB; HostDB:ENSMUSG00000028434; -.
DR eggNOG; KOG3530; Eukaryota.
DR GeneTree; ENSGT00940000158331; -.
DR HOGENOM; CLU_003623_1_0_1; -.
DR InParanoid; Q9JMC8; -.
DR OMA; SNHSLCK; -.
DR OrthoDB; 241659at2759; -.
DR TreeFam; TF319780; -.
DR BioGRID-ORCS; 54357; 3 hits in 39 CRISPR screens.
DR ChiTaRS; Epb41l4b; mouse.
DR PRO; PR:Q9JMC8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JMC8; protein.
DR Bgee; ENSMUSG00000028434; Expressed in pyloric antrum and 230 other tissues.
DR ExpressionAtlas; Q9JMC8; baseline and differential.
DR Genevisible; Q9JMC8; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:MGI.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030698; Band4.1-like4B.
DR InterPro; IPR019749; Band_41_domain.
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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280:SF18; PTHR23280:SF18; 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 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; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cytoplasm; Phosphoprotein; Reference proteome;
KW Tight junction.
FT CHAIN 1..527
FT /note="Band 4.1-like protein 4B"
FT /id="PRO_0000219405"
FT DOMAIN 85..369
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 23..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 385
FT /note="S->A: Abolishes in vitro phosphorylation."
FT /evidence="ECO:0000269|PubMed:22006950"
FT MUTAGEN 414
FT /note="S->A: Abolishes in vitro phosphorylation."
FT /evidence="ECO:0000269|PubMed:22006950"
FT MUTAGEN 419
FT /note="S->A: Abolishes in vitro phosphorylation."
FT /evidence="ECO:0000269|PubMed:22006950"
FT MUTAGEN 424
FT /note="T->A: Abolishes in vitro phosphorylation."
FT /evidence="ECO:0000269|PubMed:22006950"
FT CONFLICT 431
FT /note="V -> I (in Ref. 1; BAA96078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59564 MW; 8F6A93BEB107B64C CRC64;
MLRFLRRTFG RRSMQRYARG AAGRGAAGLG DERDGGPRGG PAAAASSSVL PAAPGGSVFP
AGGGPLLTGG AAVHISASGA AKATLYCRVF LLDGTEVSVD LPKHAKGQDL FDQIVYHLDL
VETDYFGLQF LDSAQVTHWL DHAKPIKKQM KVGPAYALHF RVKYYSSEPN NLREEFTRYL
FVLQLRHDIL SGKLKCPYET AVELAALCLQ AELGECELPE HTPELVSEFR FIPNQTEAME
FDIFQRWKEY RGKSPAQAEL SYLNKAKWLE MYGVDMHVVR GRDGCEYSLG LTPTGILIFE
GANKIGLFFW PKITKMDFKK SKLTLVVVED DDQGREQEHT FVFRLDSART CKHLWKCAVE
HHAFFRLRTP SNSKSARSDF IRLGSRFRFS GRTEYQATHG SRLRRTSTFE RKPSKRYPSR
RHSTFKASNP VIAAQLCSKA NPEVHNYQPQ YHPDVHPSQP RWRPHSPNVS NHSICKQNKP
CFQDDRPHWK TSASGDGSHF DYVQDQNQRN LGGAYSVTYR DKLMTAL
