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Q9WV92 (E41L3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Band 4.1-like protein 3
Alternative name(s):
4.1B
Differentially expressed in adenocarcinoma of the lung protein 1
Short name=DAL-1
Short name=DAL1P
Short name=mDAL-1

Cleaved into the following chain:

  1. Band 4.1-like protein 3, N-terminally processed
Gene names
Name:Epb41l3
Synonyms:Dal1, Epb4.1l3, Kiaa0987
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length929 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N-methyltransferases, including PRMT3 and PRMT5 By similarity.

Subunit structure

Interacts (via FERM domain) with CADM1. Interacts with PRMT3, PRMT5 and PRMT6 By similarity. Isoform 2 (heart-specific) has the complete spectrin--actin-binding (SAB) domain and fully interacts with spectrin and actin. Ref.1

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm By similarity. Cell junction. Note: Detected in the cytoplasm of actively dividing cells. Ref.1

Tissue specificity

Detected in brain (at protein level). Highest expression in brain, lower in testis, adrenal gland, heart and kidney. Also present in muscle and epithelial cells. Isoform 1 is expressed in brain, isoform 2 is expressed in heart and isoform 3 is mostly expressed in kidney but also in heart and brain. Isoform 6 seems to be most abundant in kidney while isoform 4 and isoform 5 are predominantly expressed in heart and brain. Ref.1

Miscellaneous

The complete SAB domain is present only in the heart-specific isoforms (isoform 2 and isoform 5)

Sequence similarities

Contains 1 FERM domain.

Sequence caution

The sequence AAD51365.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseTumor suppressor
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cortical actin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

cortical cytoskeleton organization

Traceable author statement PubMed 21966409. Source: BHF-UCL

cytoskeletal anchoring at plasma membrane

Traceable author statement PubMed 21966409. Source: BHF-UCL

myelin maintenance

Inferred from mutant phenotype PubMed 21966409. Source: BHF-UCL

neuron projection morphogenesis

Inferred from mutant phenotype PubMed 21966409. Source: BHF-UCL

paranodal junction assembly

Inferred from mutant phenotype PubMed 21966409. Source: BHF-UCL

protein localization to juxtaparanode region of axon

Inferred from mutant phenotype PubMed 21966409. Source: BHF-UCL

protein localization to paranode region of axon

Inferred from mutant phenotype PubMed 21966409. Source: BHF-UCL

protein localization to plasma membrane

Inferred from mutant phenotype PubMed 21966409. Source: BHF-UCL

regulation of cell shape

Inferred from mutant phenotype PubMed 21966409. Source: BHF-UCL

   Cellular_componentcell-cell junction

Inferred from sequence or structural similarity. Source: HGNC

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of membrane

Inferred from electronic annotation. Source: InterPro

juxtaparanode region of axon

Inferred from direct assay PubMed 12975355PubMed 16551741PubMed 21966409. Source: BHF-UCL

paranode region of axon

Inferred from direct assay PubMed 12975355PubMed 16551741PubMed 21966409. Source: BHF-UCL

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionstructural constituent of cytoskeleton

Traceable author statement PubMed 21966409. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q9WV92-1)

Also known as: 4.1B-brain;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9WV92-2)

Also known as: 4.1B-heart;

The sequence of this isoform differs from the canonical sequence as follows:
     547-558: Missing.
     559-559: D → NSLIKRIKGENVYVKHSNLMLED
Isoform 3 (identifier: Q9WV92-3)

Also known as: 4.1B-kidney;

The sequence of this isoform differs from the canonical sequence as follows:
     547-558: Missing.
Isoform 4 (identifier: Q9WV92-4)

Also known as: 4.1b-brain;

The sequence of this isoform differs from the canonical sequence as follows:
     894-929: ALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED → E
Isoform 5 (identifier: Q9WV92-5)

Also known as: 4.1B-heart;

The sequence of this isoform differs from the canonical sequence as follows:
     547-558: Missing.
     559-559: D → NSLIKRIKGENVYVKHSNLMLED
     894-929: ALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED → E
Isoform 6 (identifier: Q9WV92-6)

Also known as: 4.1B-kidney;

The sequence of this isoform differs from the canonical sequence as follows:
     547-558: Missing.
     894-929: ALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED → E
Isoform 7 (identifier: Q9WV92-7)

The sequence of this isoform differs from the canonical sequence as follows:
     455-472: Missing.
     547-558: Missing.
     623-663: Missing.
     894-929: ALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED → E
Note: Inferred from the cDNA sequence of Ref.2.
Isoform 8 (identifier: Q9WV92-8)

The sequence of this isoform differs from the canonical sequence as follows:
     455-472: Missing.
     528-528: K → KSPPGHGAAD...NDPSDSSEEE
     894-929: ALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED → E

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 929929Band 4.1-like protein 3
PRO_0000219400
Initiator methionine11Removed; alternate By similarity
Chain2 – 929928Band 4.1-like protein 3, N-terminally processed
PRO_0000423195

Regions

Domain118 – 399282FERM
Region402 – 528127Hydrophilic
Region559 – 60244Spectrin--actin-binding
Region777 – 929153C-terminal (CTD)

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylthreonine; in Band 4.1-like protein 3, N-terminally processed By similarity
Modified residue961Phosphoserine Ref.7 Ref.10
Modified residue4861Phosphoserine By similarity
Modified residue4951Phosphothreonine By similarity
Modified residue8041Phosphoserine By similarity
Modified residue9231Phosphothreonine Ref.7

Natural variations

Alternative sequence455 – 47218Missing in isoform 7 and isoform 8.
VSP_000487
Alternative sequence5281K → KSPPGHGAADSCPPSPPSAH PDPPPPTELRRRCKEKERAE PSSLESEAQGKAYLGDQDVA FSYRQPAGKGTTLFSFSLQL PESFPSLLDEDGYLSFPNLS ETNLLPQSWQHFLPIRSPSL LPCFLFIFFFLLSASFSVPY ALTLSFPLALCLCYLEPKAA SLSASLDNDPSDSSEEE in isoform 8.
VSP_023063
Alternative sequence547 – 55812Missing in isoform 2, isoform 3, isoform 5, isoform 6 and isoform 7.
VSP_000490
Alternative sequence5591D → NSLIKRIKGENVYVKHSNLM LED in isoform 2 and isoform 5.
VSP_000489
Alternative sequence623 – 66341Missing in isoform 7.
VSP_000488
Alternative sequence894 – 92936ALAQA…EDGED → E in isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_000491

Experimental info

Sequence conflict6 – 105GSDSE → RIRLR in AAD51365. Ref.2
Sequence conflict281Q → R in AAD51365. Ref.2
Sequence conflict2881A → V in AAD51365. Ref.2
Sequence conflict3061V → G in AAD51365. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (4.1B-brain) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: F4975FF405DA44AE

FASTA929103,338
        10         20         30         40         50         60 
MTTESGSDSE SKPDQEAEPQ EAAGPQGQAG AQPGPEPAGG NGSLNGEKQQ PALEQFPEAA 

        70         80         90        100        110        120 
AHSTPVKREI GDKDRDFAAA AAKQLEYQQF EDDKLSQRSS SSKLSRSPLK IVKRPKSMQC 

       130        140        150        160        170        180 
KVTLLDGSEY GCDVDKRSRG QVLFDKVCEH LNLLEKDYFG LTYRDAENQK NWLDPAKEIK 

       190        200        210        220        230        240 
KQIRSGAWHF SFNVKFYPPD PAQLSEDITR YYLCLQLRDD IVSGRLPCSF VTLALLGSYT 

       250        260        270        280        290        300 
VQSELGDYDP DECGNDYISE FRFAPNHTKE LEDKVIELHK SHRGMTPAEA EMHFLENAKK 

       310        320        330        340        350        360 
LSMYGVDLHH AKDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKVLKISY KRNNFYIKIR 

       370        380        390        400        410        420 
PGEFEQFEST IGFKLPNHRA AKRLWKVCVE HHTFFRLLLP EAPPKKFLTL GSKFRYSGRT 

       430        440        450        460        470        480 
QAQTRRASAL IDRPAPYFER SSSKRYTMSR SLDGASVSEN HEIYMKDSVS AAEVGTGQYA 

       490        500        510        520        530        540 
TTKGISQTNL ITTVTPEKKA EEERVEEEDR RKKAEEATPV TALRHEGKTD SERTDTAADG 

       550        560        570        580        590        600 
ETSATESDQE EDAEIKAQDL DKTQDELMKH QTNISELKRT FLETSTETAL TNEWEKRLST 

       610        620        630        640        650        660 
SPVRLAARQE DAPMIEPLVP EETKQSSGEK LMDGSEILSL LESARKPTEF IGGVSSTTQS 

       670        680        690        700        710        720 
WVQKLETKTE PVEAEVESTP HPQPLSTEKV LQETILVEER HVMSVHASGD ASHTARDEVD 

       730        740        750        760        770        780 
AAESTPTDRR HTGKGKEGSS VTEAAKEQRG EEVDQSAPEQ EQPATVSHEE EQASTIRTSE 

       790        800        810        820        830        840 
GLEQKSHFES STVRVESTSV GSISPGGAKL EISTKEVPVV HTETKTITYE SSQVDPGADL 

       850        860        870        880        890        900 
EPGVLMSAQT ITSETTSTTT TTHITKTVKG GISETRIEKR IVITGDADID HDQALAQAIK 

       910        920 
EAKEQHPDMS VTKVVVHKET EITPEDGED 

« Hide

Isoform 2 (4.1B-heart) [UniParc].

Checksum: 389443CDEF2CC2A5
Show »

FASTA939104,561
Isoform 3 (4.1B-kidney) [UniParc].

Checksum: D0EF7EA95EDA3C24
Show »

FASTA917101,993
Isoform 4 (4.1b-brain) [UniParc].

Checksum: 2E5E5915A9568B81
Show »

FASTA89499,510
Isoform 5 (4.1B-heart) [UniParc].

Checksum: 12419E015BB8DD08
Show »

FASTA904100,734
Isoform 6 (4.1B-kidney) [UniParc].

Checksum: 94CC9620418FDF2C
Show »

FASTA88298,166
Isoform 7 [UniParc].

Checksum: 2F78D9ADA3DC0674
Show »

FASTA82391,850
Isoform 8 [UniParc].

Checksum: 3D9A917D79B9E7F5
Show »

FASTA1,052116,785

References

« Hide 'large scale' references
[1]"Molecular and functional characterization of protein 4.1B, a novel member of the protein 4.1 family with high level, focal expression in brain."
Parra M., Gascard P., Walensky L.D., Gimm J.A., Blackshaw S., Chan N., Takakuwa Y., Berger T., Lee G., Chasis J.A., Snyder S.H., Mohandas N., Conboy J.G.
J. Biol. Chem. 275:3247-3255(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), SUBUNIT, SUBCELLULAR LOCATION, ACTIN-BINDING, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Mouse DAL-1 (mDAL-1) cDNA sequence."
Azam M., Andrabi S., Lin L., Newsham I., Chishti A.H.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-929 (ISOFORM 7).
Strain: BALB/c.
Tissue: Brain.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-929 (ISOFORM 8).
Tissue: Fetal brain.
[4]Marra M., Hillier L., Kucaba T., Martin J., Beck C., Wylie T., Underwood K., Steptoe M., Theising B., Allen M., Bowers Y., Person B., Swaller T., Gibbons M., Pape D., Harvey N., Schurk R., Ritter E. expand/collapse author list , Kohn S., Shin T., Jackson Y., Cardenas M., McCann R., Waterston R., Wilson R.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 719-929 (ISOFORMS 4/5/6/7).
[5]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[6]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-923, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF152247 mRNA. Translation: AAD38048.1.
AF177146 mRNA. Translation: AAD51365.1. Different initiation.
AK173080 mRNA. Translation: BAD32358.1.
RefSeqNP_038841.1. NM_013813.1.
UniGeneMm.131135.

3D structure databases

ProteinModelPortalQ9WV92.
SMRQ9WV92. Positions 114-445.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199461. 2 interactions.
IntActQ9WV92. 7 interactions.
MINTMINT-4093843.

PTM databases

PhosphoSiteQ9WV92.

Proteomic databases

PaxDbQ9WV92.
PRIDEQ9WV92.

Protocols and materials databases

DNASU13823.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080208; ENSMUSP00000079098; ENSMUSG00000024044. [Q9WV92-1]
ENSMUST00000112680; ENSMUSP00000108300; ENSMUSG00000024044. [Q9WV92-2]
GeneID13823.
KEGGmmu:13823.
UCSCuc008dkp.1. mouse. [Q9WV92-1]
uc008dkq.1. mouse. [Q9WV92-7]
uc008dkr.1. mouse. [Q9WV92-8]

Organism-specific databases

CTD13823.
MGIMGI:103008. Epb4.1l3.
RougeSearch...

Phylogenomic databases

eggNOGNOG242913.
GeneTreeENSGT00750000117241.
HOGENOMHOG000228840.
HOVERGENHBG007777.
KOK06107.
OMASTDTAIT.
OrthoDBEOG7Z69BP.
PhylomeDBQ9WV92.
TreeFamTF351626.

Gene expression databases

ArrayExpressQ9WV92.
BgeeQ9WV92.
CleanExMM_EPB4.1L3.
GenevestigatorQ9WV92.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR008379. Band_4.1_C.
IPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR021187. Band_41_protein.
IPR000798. Ez/rad/moesin_like.
IPR014847. FERM-adjacent.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR007477. SAB_dom.
[Graphical view]
PfamPF05902. 4_1_CTD. 1 hit.
PF08736. FA. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF04382. SAB. 1 hit.
[Graphical view]
PIRSFPIRSF002304. Membrane_skeletal_4_1. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284624.
PROQ9WV92.
SOURCESearch...

Entry information

Entry nameE41L3_MOUSE
AccessionPrimary (citable) accession number: Q9WV92
Secondary accession number(s): Q69ZT8, Q9R102
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot