E41LB_HUMAN
ID E41LB_HUMAN Reviewed; 900 AA.
AC Q9H329; Q5T4G5; Q5T4G6; Q9H328; Q9P2V3;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Band 4.1-like protein 4B;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 4B {ECO:0000312|HGNC:HGNC:19818};
DE AltName: Full=FERM-containing protein CG1;
DE AltName: Full=Protein EHM2;
GN Name=EPB41L4B {ECO:0000312|HGNC:HGNC:19818};
GN Synonyms=EHM2 {ECO:0000312|HGNC:HGNC:19818},
GN LULU2 {ECO:0000303|PubMed:22006950};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT THR-816.
RX PubMed=10603000; DOI=10.1007/s003350010017;
RA Chadwick B.P., Leyne M., Gill S., Liebert C.B., Mull J., Mezey E.,
RA Robbins C.M., Pinkett H.W., Makalowska I., Maayan C., Blumenfeld A.,
RA Axelrod F.B., Brownstein M., Gusella J.F., Slaugenhaupt S.A.;
RT "Cloning, mapping, and expression of a novel brain-specific transcript in
RT the familial dysautonomia candidate region on chromosome 9q31.";
RL Mamm. Genome 11:81-83(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14521927; DOI=10.1016/j.bbrc.2003.08.147;
RA Chauhan S., Pandey R., Way J.F., Sroka T.C., Demetriou M.C., Kunz S.,
RA Cress A.E., Mount D.W., Miesfeld R.L.;
RT "Androgen regulation of the human FERM domain encoding gene EHM2 in a cell
RT model of steroid-induced differentiation.";
RL Biochem. Biophys. Res. Commun. 310:421-432(2003).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23664528; DOI=10.1016/j.jdermsci.2013.04.008;
RA Bosanquet D.C., Ye L., Harding K.G., Jiang W.G.;
RT "Expressed in high metastatic cells (Ehm2) is a positive regulator of
RT keratinocyte adhesion and motility: The implication for wound healing.";
RL J. Dermatol. Sci. 71:115-121(2013).
CC -!- FUNCTION: Up-regulates the activity of the Rho guanine nucleotide
CC exchange factor ARHGEF18 (By similarity). Involved in the regulation of
CC 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 (PubMed:23664528). May
CC have a role in mediating cytoskeletal changes associated with steroid-
CC induced cell differentiation (PubMed:14521927).
CC {ECO:0000250|UniProtKB:Q9JMC8, ECO:0000269|PubMed:14521927,
CC ECO:0000269|PubMed:22006950, ECO:0000269|PubMed:23664528}.
CC -!- SUBUNIT: Interacts (via FERM domain) with ARHGEF18 (via C-terminus);
CC the interaction activates ARHGEF18. {ECO:0000250|UniProtKB:Q9JMC8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22006950}. Cell
CC junction, tight junction {ECO:0000269|PubMed:22006950}.
CC Note=Accumulates along apical cell-cell boundaries and is also detected
CC in the cytoplasm in a punctate manner. {ECO:0000269|PubMed:22006950}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H329-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H329-2; Sequence=VSP_007202, VSP_007203;
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in acute wounds than
CC chronic wounds with increased expression in healing wounds, especially
CC at the leading wound edge (PubMed:23664528). Isoform 1 is highly
CC expressed in brain. Isoform 2 is highly expressed in testis with lower
CC levels in prostate and breast (PubMed:14521927).
CC {ECO:0000269|PubMed:14521927, ECO:0000269|PubMed:23664528}.
CC -!- INDUCTION: By the androgen dihydrotestosterone (DHT).
CC {ECO:0000269|PubMed:14521927}.
CC -!- PTM: May be negatively regulated by phosphorylation.
CC {ECO:0000250|UniProtKB:Q9JMC8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG43366.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG43368.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF153416; AAG43366.1; ALT_FRAME; mRNA.
DR EMBL; AF153418; AAG43368.1; ALT_FRAME; mRNA.
DR EMBL; AB032179; BAA96079.2; -; mRNA.
DR EMBL; AL359963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS43859.1; -. [Q9H329-1]
DR CCDS; CCDS43860.1; -. [Q9H329-2]
DR RefSeq; NP_060894.2; NM_018424.3. [Q9H329-2]
DR RefSeq; NP_061987.3; NM_019114.4. [Q9H329-1]
DR AlphaFoldDB; Q9H329; -.
DR SMR; Q9H329; -.
DR BioGRID; 120044; 100.
DR IntAct; Q9H329; 18.
DR MINT; Q9H329; -.
DR STRING; 9606.ENSP00000363694; -.
DR iPTMnet; Q9H329; -.
DR PhosphoSitePlus; Q9H329; -.
DR BioMuta; EPB41L4B; -.
DR DMDM; 209572611; -.
DR EPD; Q9H329; -.
DR jPOST; Q9H329; -.
DR MassIVE; Q9H329; -.
DR MaxQB; Q9H329; -.
DR PaxDb; Q9H329; -.
DR PeptideAtlas; Q9H329; -.
DR PRIDE; Q9H329; -.
DR ProteomicsDB; 80657; -. [Q9H329-1]
DR ProteomicsDB; 80658; -. [Q9H329-2]
DR Antibodypedia; 29426; 81 antibodies from 22 providers.
DR DNASU; 54566; -.
DR Ensembl; ENST00000374557.4; ENSP00000363685.3; ENSG00000095203.15. [Q9H329-2]
DR Ensembl; ENST00000374566.8; ENSP00000363694.3; ENSG00000095203.15. [Q9H329-1]
DR GeneID; 54566; -.
DR KEGG; hsa:54566; -.
DR MANE-Select; ENST00000374566.8; ENSP00000363694.3; NM_019114.5; NP_061987.3.
DR UCSC; uc004bdz.3; human. [Q9H329-1]
DR CTD; 54566; -.
DR DisGeNET; 54566; -.
DR GeneCards; EPB41L4B; -.
DR HGNC; HGNC:19818; EPB41L4B.
DR HPA; ENSG00000095203; Tissue enhanced (liver, pancreas).
DR MIM; 610340; gene.
DR neXtProt; NX_Q9H329; -.
DR OpenTargets; ENSG00000095203; -.
DR PharmGKB; PA134986250; -.
DR VEuPathDB; HostDB:ENSG00000095203; -.
DR eggNOG; KOG3530; Eukaryota.
DR GeneTree; ENSGT00940000158331; -.
DR HOGENOM; CLU_003623_5_0_1; -.
DR InParanoid; Q9H329; -.
DR OMA; IYTPEAC; -.
DR OrthoDB; 241659at2759; -.
DR PhylomeDB; Q9H329; -.
DR TreeFam; TF319780; -.
DR PathwayCommons; Q9H329; -.
DR SignaLink; Q9H329; -.
DR SIGNOR; Q9H329; -.
DR BioGRID-ORCS; 54566; 5 hits in 1069 CRISPR screens.
DR ChiTaRS; EPB41L4B; human.
DR GenomeRNAi; 54566; -.
DR Pharos; Q9H329; Tbio.
DR PRO; PR:Q9H329; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H329; protein.
DR Bgee; ENSG00000095203; Expressed in secondary oocyte and 166 other tissues.
DR Genevisible; Q9H329; HS.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0031032; P:actomyosin structure organization; IDA:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IMP:UniProtKB.
DR GO; GO:0042060; P:wound healing; IDA:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell junction; Cytoplasm; Phosphoprotein;
KW Reference proteome; Tight junction.
FT CHAIN 1..900
FT /note="Band 4.1-like protein 4B"
FT /id="PRO_0000219404"
FT DOMAIN 85..369
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 23..48
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 492..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 470..518
FT /note="SYPLPSPVLSSSDRLPFGIEENGGTPFLTAASGRHHHQHQHQHQHQHHS ->
FT RPSFQDDRSHWKASASGDDSHFDYVHDQNQKNLGGMQSMMYRDKLMTAL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10603000,
FT ECO:0000303|PubMed:10783258"
FT /id="VSP_007202"
FT VAR_SEQ 519..900
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10603000,
FT ECO:0000303|PubMed:10783258"
FT /id="VSP_007203"
FT VARIANT 816
FT /note="N -> T (in dbSNP:rs3750450)"
FT /evidence="ECO:0000269|PubMed:10603000"
FT /id="VAR_048356"
FT CONFLICT 73
FT /note="V -> M (in Ref. 2; BAA96079)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="E -> R (in Ref. 1; AAG43366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 99712 MW; 9A4BD658DBE65BDE CRC64;
MLRFLRRTFG RRSMQRYARG AAGRGAAGLG DERDGGPRGG PAAAASSSAL PAAPGGSVFP
AGGGPLLTGG AAVHISAAGA AKATLYCRVF LLDGTEVSVD LPKHAKGQDL FDQIVYHLDL
VETDYFGLQF LDSAQVAHWL DHAKPIKKQM KIGPAYALHF RVKYYSSEPN NLREEFTRYL
FVLQLRHDIL SGKLKCPYET AVELAALCLQ AELGECELPE HTPELVSEFR FIPNQTEAME
FDIFQRWKEC RGKSPAQAEL SYLNKAKWLE MYGVDMHVVR GRDGCEYSLG LTPTGILIFE
GANKIGLFFW PKITKMDFKK SKLTLVVVED DDQGREQEHT FVFRLDSART CKHLWKCAVE
HHAFFRLRTP GNSKSNRSDF IRLGSRFRFS GRTEYQATHG SRLRRTSTFE RKPSKRYPSR
RHSTFKASNP VIAAQLCSKT NPEVHNYQPQ YHPNIHPSQP RWHPHSPNVS YPLPSPVLSS
SDRLPFGIEE NGGTPFLTAA SGRHHHQHQH QHQHQHHSNY SLSLTLENKE GPLRSPNSSS
KSLTKLSPGT PALFSEAAAH LKKLELETVK AAGPWPPLHI NINKAEEKKV SEKTLQTPLL
PSPVADHVKC NILKAQLENA SRVNIQGGKE ESPFVNINKK SSLQDASVRS PIPIRVETAQ
PAVEKPEIKP PRVRKLTRQY SFDEDDLPPD LAEAVGVTTS TTTNTTTAAT QVSVPLPSPK
VQNVSSPHKS EGKGLLSPGA KSPSDRGGAF TLEPGDLLMD FTEATPLAEP ASNPHCAHSR
CSPPLSLPMK EETTGVCMYP PIKTRLIKTF PVDTMNPFPD TFTTGPQFTA DFRDSKLQCC
PGPTSPLIPA ATLRPLTETV STVQTIYTTR KPVSLAASAE TLRQELEREK MMKRLLMTEL
