ID   EPB41_MOUSE             Reviewed;         858 AA.
AC   P48193; A2A843; Q5DTQ8; Q68FF1; Q6NVF5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Protein 4.1;
DE            Short=P4.1;
DE   AltName: Full=4.1R;
DE   AltName: Full=Band 4.1;
DE   AltName: Full=Erythrocyte membrane protein band 4.1 {ECO:0000312|MGI:MGI:95401};
GN   Name=Epb41 {ECO:0000312|MGI:MGI:95401};
GN   Synonyms=Epb4.1 {ECO:0000312|MGI:MGI:95401}, Kiaa4056;
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] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC   STRAIN=BALB/cJ;
RX   PubMed=8429050; DOI=10.1016/s0021-9258(18)53759-5;
RA   Huang J.-P., Tang C.-J.C., Kou G.-H., Marchesi V.T., Benz E.J. Jr.,
RA   Tang T.K.;
RT   "Genomic structure of the locus encoding protein 4.1. Structural basis for
RT   complex combinational patterns of tissue-specific alternative RNA
RT   splicing.";
RL   J. Biol. Chem. 268:3758-3766(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 709-713, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   CHARACTERIZATION OF CARBOXY-TERMINAL DOMAIN.
RX   PubMed=11432737; DOI=10.1046/j.1432-1327.2001.02276.x;
RA   Scott C., Phillips G.W., Baines A.J.;
RT   "Properties of the C-terminal domain of 4.1 proteins.";
RL   Eur. J. Biochem. 268:3709-3717(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Mast cell;
RX   PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541 AND SER-543, AND
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-541; SER-543;
RP   SER-556; SER-658 AND SER-668, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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).
RN   [10]
RP   INTERACTION WITH ATP2B1.
RX   PubMed=23460639; DOI=10.1074/jbc.m112.436659;
RA   Liu C., Weng H., Chen L., Yang S., Wang H., Debnath G., Guo X., Wu L.,
RA   Mohandas N., An X.;
RT   "Impaired intestinal calcium absorption in protein 4.1R-deficient mice due
RT   to altered expression of plasma membrane calcium ATPase 1b (PMCA1b).";
RL   J. Biol. Chem. 288:11407-11415(2013).
CC   -!- FUNCTION: Protein 4.1 is a major structural element of the erythrocyte
CC       membrane skeleton. It plays a key role in regulating membrane physical
CC       properties of mechanical stability and deformability by stabilizing
CC       spectrin-actin interaction. Recruits DLG1 to membranes. Required for
CC       dynein-dynactin complex and NUMA1 recruitment at the mitotic cell
CC       cortex during anaphase. {ECO:0000250|UniProtKB:P11171}.
CC   -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower
CC       affinity to band III protein. Associates with the nuclear mitotic
CC       apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate
CC       with contractile apparatus and tight junctions. Interacts with NUMA1;
CC       this interaction is negatively regulated by CDK1 during metaphase and
CC       promotes anaphase-specific localization of NUMA1 in symmetrically
CC       dividing cells. Interacts with ATP2B1; regulates small intestinal
CC       calcium absorption through regulation of membrane expression of ATP2B1
CC       (PubMed:23460639). {ECO:0000250|UniProtKB:P11171,
CC       ECO:0000269|PubMed:23460639}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11171}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P11171}. Cytoplasm, cell
CC       cortex {ECO:0000250|UniProtKB:P11171}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=A number of isoforms are produced.;
CC       Name=1;
CC         IsoId=P48193-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P48193-2; Sequence=VSP_012874;
CC   -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in the C-
CC       terminal domain. {ECO:0000250}.
CC   -!- PTM: Phosphorylated at multiple sites by different protein kinases and
CC       each phosphorylation event selectively modulates the protein's
CC       functions.
CC   -!- PTM: Phosphorylation on Tyr-654 reduces the ability of 4.1 to promote
CC       the assembly of the spectrin/actin/4.1 ternary complex.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90280.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L00919; AAA37122.1; -; mRNA.
DR   EMBL; L00919; AAA37123.1; -; mRNA.
DR   EMBL; AK220462; BAD90280.1; ALT_INIT; mRNA.
DR   EMBL; AL607088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL669981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC068138; AAH68138.1; -; mRNA.
DR   EMBL; BC079875; AAH79875.1; -; mRNA.
DR   CCDS; CCDS18717.1; -. [P48193-1]
DR   CCDS; CCDS51317.1; -. [P48193-2]
DR   PIR; A46613; A46613.
DR   RefSeq; NP_001122078.1; NM_001128606.1. [P48193-2]
DR   RefSeq; NP_001122079.1; NM_001128607.1.
DR   RefSeq; NP_906273.3; NM_183428.3. [P48193-1]
DR   AlphaFoldDB; P48193; -.
DR   BMRB; P48193; -.
DR   SMR; P48193; -.
DR   BioGRID; 234673; 10.
DR   STRING; 10090.ENSMUSP00000030739; -.
DR   GlyGen; P48193; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P48193; -.
DR   PhosphoSitePlus; P48193; -.
DR   EPD; P48193; -.
DR   jPOST; P48193; -.
DR   MaxQB; P48193; -.
DR   PaxDb; 10090-ENSMUSP00000101595; -.
DR   PeptideAtlas; P48193; -.
DR   ProteomicsDB; 285570; -. [P48193-1]
DR   ProteomicsDB; 285571; -. [P48193-2]
DR   Antibodypedia; 30998; 399 antibodies from 30 providers.
DR   DNASU; 269587; -.
DR   Ensembl; ENSMUST00000030739.11; ENSMUSP00000030739.5; ENSMUSG00000028906.18. [P48193-1]
DR   Ensembl; ENSMUST00000054917.12; ENSMUSP00000060375.6; ENSMUSG00000028906.18. [P48193-2]
DR   Ensembl; ENSMUST00000084253.10; ENSMUSP00000081274.4; ENSMUSG00000028906.18. [P48193-2]
DR   Ensembl; ENSMUST00000105972.8; ENSMUSP00000101592.2; ENSMUSG00000028906.18. [P48193-1]
DR   Ensembl; ENSMUST00000105981.9; ENSMUSP00000101601.3; ENSMUSG00000028906.18. [P48193-1]
DR   GeneID; 269587; -.
DR   KEGG; mmu:269587; -.
DR   UCSC; uc008val.3; mouse. [P48193-2]
DR   UCSC; uc008vam.3; mouse. [P48193-1]
DR   AGR; MGI:95401; -.
DR   CTD; 2035; -.
DR   MGI; MGI:95401; Epb41.
DR   VEuPathDB; HostDB:ENSMUSG00000028906; -.
DR   eggNOG; KOG3527; Eukaryota.
DR   GeneTree; ENSGT00940000157833; -.
DR   InParanoid; P48193; -.
DR   OMA; TYEAAQX; -.
DR   OrthoDB; 5391231at2759; -.
DR   Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR   BioGRID-ORCS; 269587; 2 hits in 44 CRISPR screens.
DR   ChiTaRS; Epb41; mouse.
DR   PRO; PR:P48193; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P48193; Protein.
DR   Bgee; ENSMUSG00000028906; Expressed in blood and 248 other cell types or tissues.
DR   ExpressionAtlas; P48193; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; ISO:MGI.
DR   GO; GO:0003779; F:actin binding; ISS:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR   GO; GO:0030507; F:spectrin binding; ISS:MGI.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
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:0065003; P:protein-containing complex assembly; ISO:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IMP:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:MGI.
DR   GO; GO:1904478; P:regulation of intestinal absorption; IMP:UniProtKB.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13184; FERM_C_4_1_family; 1.
DR   CDD; cd17105; FERM_F1_EPB41; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR021187; EPB4.1_FERM_F1.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FA.
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; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF12; PROTEIN 4.1; 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   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 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; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   Genevisible; P48193; MM.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Calmodulin-binding; Cell cycle;
KW   Cell division; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Glycoprotein; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW   Transport.
FT   CHAIN           1..858
FT                   /note="Protein 4.1"
FT                   /id="PRO_0000219391"
FT   DOMAIN          211..492
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   REGION          1..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..608
FT                   /note="Hydrophilic"
FT   REGION          518..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..707
FT                   /note="Spectrin--actin-binding"
FT   REGION          710..858
FT                   /note="C-terminal (CTD)"
FT   COMPBIAS        1..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..613
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         62
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         192
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         223
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17947660"
FT   MOD_RES         379
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         541
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         556
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         654
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         658
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         668
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         703
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         706
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         730
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   MOD_RES         853
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P11171"
FT   VAR_SEQ         610..663
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_012874"
FT   CONFLICT        1..3
FT                   /note="MTT -> EPLKGREPRRARTRPGPARPGPCQVPVLCSP (in Ref. 4;
FT                   AAH68138)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        8
FT                   /note="A -> V (in Ref. 1; AAA37123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232..233
FT                   /note="KG -> NL (in Ref. 1; AAA37122)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="Y -> S (in Ref. 1; AAA37122)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        576
FT                   /note="A -> R (in Ref. 1; AAA37122)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   858 AA;  95911 MW;  7CF1CD52D790D1FD CRC64;
     MTTEKSLAAE AENSQHQQQK EEGEGATNSG QQETQLEEAS QAAAAEGSDQ GEQKLKASNG
     DTPTHEDLTK NKERTSESRG LSRLLSSFLK RPKSQVSEEE GREVESEKEK GEGGQKEIEL
     GNSLDEDIIL KAPIAAPEPE LKTDPSLDLH SLSSIETQPA QEEHREDPDS ETKEGEGIEE
     CSGTEVKEDP ESRAEREPEA SQKPVRRHRN MHCKVSLLDD TVYECVVEKH AKGQDLLKRV
     CEHLNLLEED YFGLALWDSA TSKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED
     ITRYYLCLQL RQDIVAGRLP CSFATLALLG SYTIQSELGD YDPELHGMDY VSDFKLAPNQ
     TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG
     LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI KIRPGEQEHY ESTIGFKLPS YRAAKKLWKV
     CVEHHTFFRL TSTDTIPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA
     SRSLDGAAAA ESTDRSPRPT SAPAIAQSQV TEGPGAPIKK TPKEAVKVEE KRGEEPAEPA
     EPEPTEAWKV EKTHTEVTVP TSNGDQTQKL AGKGEDLIRM RKKKRERLDG ENIYIRHSNL
     MLEDLDKSQE EIKKHHASIS ELKKNFMESV PEPRPSEWDK RLSTHSPFRT LNINGQVPTG
     DGPPLVKTQT VTISDTANAV KSEIPTKDVP IVHTETKTIT YEAAQTEDSN GDLDPGVLLT
     AQTITSETTS STTTTQITKT VKGGISETRI EKRIVITGDA DIDHDQVLVQ AIKEAKEQHP
     DMSVTKVVVH QETEISEE
//