LOCUS       NP_906273                858 aa            linear   ROD 02-MAY-2024
DEFINITION  protein 4.1 isoform 1 [Mus musculus].
ACCESSION   NP_906273 XP_194176
VERSION     NP_906273.3
DBSOURCE    REFSEQ: accession NM_183428.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Lu,Y., Fan,D., Wang,W., Gao,X., Li,H., Guo,S., Zhao,L., Guo,Y.,
            Li,B., Zhong,Y., Zhang,B., Liu,J., Dai,L., Kang,Q. and Ji,Z.
  TITLE     The protein 4.1R downregulates VEGFA in M2 macrophages to inhibit
            colon cancer metastasis
  JOURNAL   Exp Cell Res 409 (1), 112896 (2021)
   PUBMED   34717920
  REMARK    GeneRIF: The protein 4.1R downregulates VEGFA in M2 macrophages to
            inhibit colon cancer metastasis.
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Huang,S.C., Vu,L.V., Yu,F.H., Nguyen,D.T. and Benz,E.J. Jr.
  TITLE     Multifunctional protein 4.1R regulates the asymmetric segregation
            of Numb during terminal erythroid maturation
  JOURNAL   J Biol Chem 297 (3), 101051 (2021)
   PUBMED   34364872
  REMARK    GeneRIF: Multifunctional protein 4.1R regulates the asymmetric
            segregation of Numb during terminal erythroid maturation.
REFERENCE   4  (residues 1 to 858)
  AUTHORS   Li,B., Zhang,X., Lu,Y., Zhao,L., Guo,Y., Guo,S., Kang,Q., Liu,J.,
            Dai,L., Zhang,L., Fan,D. and Ji,Z.
  TITLE     Protein 4.1R affects photodynamic therapy for B16 melanoma by
            regulating the transport of 5-aminolevulinic acid
  JOURNAL   Exp Cell Res 399 (2), 112465 (2021)
   PUBMED   33385415
  REMARK    GeneRIF: Protein 4.1R affects photodynamic therapy for B16 melanoma
            by regulating the transport of 5-aminolevulinic acid.
REFERENCE   5  (residues 1 to 858)
  AUTHORS   Ding,C., Guo,Y., Liang,T., Liu,J., Yang,L., Wang,T., Liu,X. and
            Kang,Q.
  TITLE     Protein 4.1R negatively regulates P815 cells proliferation by
            inhibiting C-Kit-mediated signal transduction
  JOURNAL   Exp Cell Res 398 (2), 112403 (2021)
   PUBMED   33271128
  REMARK    GeneRIF: Protein 4.1R negatively regulates P815 cells proliferation
            by inhibiting C-Kit-mediated signal transduction.
REFERENCE   6  (residues 1 to 858)
  AUTHORS   Winardi,R., Discher,D., Kelley,C., Zon,L., Mays,K., Mohandas,N. and
            Conboy,J.G.
  TITLE     Evolutionarily conserved alternative pre-mRNA splicing regulates
            structure and function of the spectrin-actin binding domain of
            erythroid protein 4.1
  JOURNAL   Blood 86 (11), 4315-4322 (1995)
   PUBMED   7492792
REFERENCE   7  (residues 1 to 858)
  AUTHORS   Takeuchi,K., Kawashima,A., Nagafuchi,A. and Tsukita,S.
  TITLE     Structural diversity of band 4.1 superfamily members
  JOURNAL   J Cell Sci 107 (Pt 7), 1921-1928 (1994)
   PUBMED   7983158
REFERENCE   8  (residues 1 to 858)
  AUTHORS   Bahary,N., Zorich,G., Pachter,J.E., Leibel,R.L. and Friedman,J.M.
  TITLE     Molecular genetic linkage maps of mouse chromosomes 4 and 6
  JOURNAL   Genomics 11 (1), 33-47 (1991)
   PUBMED   1684952
REFERENCE   9  (residues 1 to 858)
  AUTHORS   Conboy,J., Kan,Y.W., Shohet,S.B. and Mohandas,N.
  TITLE     Molecular cloning of protein 4.1, a major structural element of the
            human erythrocyte membrane skeleton
  JOURNAL   Proc Natl Acad Sci U S A 83 (24), 9512-9516 (1986)
   PUBMED   3467321
REFERENCE   10 (residues 1 to 858)
  AUTHORS   Conboy,J., Mohandas,N., Tchernia,G. and Kan,Y.W.
  TITLE     Molecular basis of hereditary elliptocytosis due to protein 4.1
            deficiency
  JOURNAL   N Engl J Med 315 (11), 680-685 (1986)
   PUBMED   3755799
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL669981.11, CB723734.1, CN537562.1, CN526385.1, CB526050.1 and
            AK220462.1.
            
            On Jun 19, 2008 this sequence version replaced NP_906273.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq was created from transcript and genomic
            sequence data because transcript sequence consistent with the
            reference genome assembly was not available for all regions of the
            RefSeq transcript, The extent of this transcript is supported by
            transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164138,
                              SAMN01164142 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            RefSeq Select criteria           :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 64.54 cM"
     Protein         1..858
                     /product="protein 4.1 isoform 1"
                     /note="protein 4.1; P4.1; band 4.1; Protein 4.1R;
                     erythrocyte protein band 4.1"
                     /calculated_mol_wt=95780
     Region          1..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48193.2)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Region          155..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48193.2)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Region          212..402
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:17947660; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Region          397..490
                     /region_name="FERM_C_4_1_family"
                     /note="FERM domain C-lobe of Protein 4.1 family; cd13184"
                     /db_xref="CDD:270005"
     Site            order(406,423,425,431)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270005"
     Site            order(435,440..443,478,482,485..486)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            478..489
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Region          495..608
                     /region_name="Hydrophilic"
                     /note="propagated from UniProtKB/Swiss-Prot (P48193.2)"
     Region          500..543
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Region          518..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48193.2)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (P48193.2)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Region          609..707
                     /region_name="Spectrin--actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P48193.2)"
     Site            654
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Region          661..709
                     /region_name="SAB"
                     /note="SAB domain; pfam04382"
                     /db_xref="CDD:461285"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Site            706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Region          710..858
                     /region_name="C-terminal (CTD)"
                     /note="propagated from UniProtKB/Swiss-Prot (P48193.2)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     Region          747..854
                     /region_name="4_1_CTD"
                     /note="4.1 protein C-terminal domain (CTD); pfam05902"
                     /db_xref="CDD:461774"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11171; propagated from
                     UniProtKB/Swiss-Prot (P48193.2)"
     CDS             1..858
                     /gene="Epb41"
                     /gene_synonym="4.1R; D4Ertd442e; Elp-1; Elp1; Epb4.1;
                     mKIAA4056"
                     /coded_by="NM_183428.3:1478..4054"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS18717.1"
                     /db_xref="GeneID:269587"
                     /db_xref="MGI:MGI:95401"
ORIGIN      
        1 mttekslaae aensqhqqqk eegegatnsg qqetqleeas qaaaaegsdq geqklkasng
       61 dtpthedltk nkertsesrg lsrllssflk rpksqvseee grevesekek geggqkeiel
      121 gnsldediil kapiaapepe lktdpsldlh slssietqpa qeehredpds etkegegiee
      181 csgtevkedp esraerepea sqkpvrrhrn mhckvslldd tvyecvvekh akgqdllkrv
      241 cehlnlleed yfglalwdsa tsktwldsak eikkqvrgvp wnftfnvkfy ppdpaqlted
      301 itryylclql rqdivagrlp csfatlallg sytiqselgd ydpelhgmdy vsdfklapnq
      361 tkeleekvme lhksyrsmtp aqadleflen akklsmygvd lhkakdlegv diilgvcssg
      421 llvykdklri nrfpwpkvlk isykrssffi kirpgeqehy estigfklps yraakklwkv
      481 cvehhtffrl tstdtipksk flalgskfry sgrtqaqtrq asalidrpap hfertaskra
      541 srsldgaaaa estdrsprpt sapaiaqsqv tegpgapikk tpkeavkvee krgeepaepa
      601 epepteawkv ekthtevtvp tsngdqtqkl agkgedlirm rkkkrerldg eniyirhsnl
      661 mledldksqe eikkhhasis elkknfmesv peprpsewdk rlsthspfrt lningqvptg
      721 dgpplvktqt vtisdtanav kseiptkdvp ivhtetktit yeaaqtedsn gdldpgvllt
      781 aqtitsetts sttttqitkt vkggisetri ekrivitgda didhdqvlvq aikeakeqhp
      841 dmsvtkvvvh qeteisee
//
