LIMA1_MOUSE
ID LIMA1_MOUSE Reviewed; 753 AA.
AC Q9ERG0; Q8K2H0; Q9ERG1;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=LIM domain and actin-binding protein 1;
DE AltName: Full=Epithelial protein lost in neoplasm;
DE Short=mEPLIN;
GN Name=Lima1; Synonyms=D15Ertd366e, Eplin {ECO:0000303|PubMed:11179679};
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] (ISOFORMS ALPHA AND BETA).
RX PubMed=11179679; DOI=10.1016/s0378-1119(00)00540-0;
RA Maul R.S., Sachi Gerbin C., Chang D.D.;
RT "Characterization of mouse epithelial protein lost in neoplasm (EPLIN) and
RT comparison of mammalian and zebrafish EPLIN.";
RL Gene 262:155-160(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION AT SER-360; SER-602 AND SER-692 BY MAPK1/MAPK3, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF SER-360; SER-602 AND SER-692, AND INTERACTION WITH
RP F-ACTIN.
RX PubMed=17875928; DOI=10.1128/mcb.00661-07;
RA Han M.Y., Kosako H., Watanabe T., Hattori S.;
RT "Extracellular signal-regulated kinase/mitogen-activated protein kinase
RT regulates actin organization and cell motility by phosphorylating the actin
RT cross-linking protein EPLIN.";
RL Mol. Cell. Biol. 27:8190-8204(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-230; SER-360;
RP SER-485 AND SER-488, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-488, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-225; SER-230;
RP SER-242; SER-467; SER-485; SER-488; SER-615; SER-720 AND SER-735, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-437, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE,
RP INTERACTION WITH NPC1L1 AND MYO5B, MUTAGENESIS OF 164-CYS--GLY-166,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH F-ACTIN.
RX PubMed=29880681; DOI=10.1126/science.aao6575;
RA Zhang Y.Y., Fu Z.Y., Wei J., Qi W., Baituola G., Luo J., Meng Y.J.,
RA Guo S.Y., Yin H., Jiang S.Y., Li Y.F., Miao H.H., Liu Y., Wang Y., Li B.L.,
RA Ma Y.T., Song B.L.;
RT "A LIMA1 variant promotes low plasma LDL cholesterol and decreases
RT intestinal cholesterol absorption.";
RL Science 360:1087-1092(2018).
CC -!- FUNCTION: Actin-binding protein involved in actin cytoskeleton
CC regulation and dynamics. Increases the number and size of actin stress
CC fibers and inhibits membrane ruffling. Inhibits actin filament
CC depolymerization. Bundles actin filaments, delays filament nucleation
CC and reduces formation of branched filaments (By similarity). Plays a
CC role in cholesterol homeostasis. Influences plasma cholesterol levels
CC through regulation of intestinal cholesterol absorption. May act as a
CC scaffold protein by regulating NPC1L1 transportation, an essential
CC protein for cholesterol absorption, to the plasma membrane by
CC recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake
CC (PubMed:29880681). {ECO:0000250|UniProtKB:Q9UHB6,
CC ECO:0000269|PubMed:29880681}.
CC -!- SUBUNIT: Interacts with NPC1L1; bridges NPC1L1 with MYO5B
CC (PubMed:29880681). Interacts with MYO5B; bridges MYO5B with NPC1L1
CC (PubMed:29880681). Interacts with PXN; this complex stabilizes actin
CC dynamics (By similarity). Binds to G-actin and F-actin
CC (PubMed:17875928) (By similarity). {ECO:0000250|UniProtKB:Q9UHB6,
CC ECO:0000269|PubMed:17875928, ECO:0000269|PubMed:29880681}.
CC -!- INTERACTION:
CC Q9ERG0-2; P35221: CTNNA1; Xeno; NbExp=2; IntAct=EBI-15677021, EBI-701918;
CC Q9ERG0-2; P35221-1: CTNNA1; Xeno; NbExp=2; IntAct=EBI-15677021, EBI-7053242;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9UHB6}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:17875928}. Cell membrane
CC {ECO:0000269|PubMed:29880681}. Cell projection, ruffle
CC {ECO:0000269|PubMed:17875928}. Note=Expressed mainly in the brush
CC border membrane of the small intestine and colocalizes with NPC1L1 and
CC MYO5B (PubMed:29880681). Colocalizes with PXN at focal adhesions in
CC mesangial cells (By similarity). Colocalizes with actin stress fibers
CC in quiescent cells. PDGF stimulation induced disassembly of stress
CC fibers and formation of peripheral and dorsal ruffles, where LIMA1 is
CC relocalized (PubMed:17875928). {ECO:0000250|UniProtKB:Q9UHB6,
CC ECO:0000269|PubMed:17875928, ECO:0000269|PubMed:29880681}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Beta;
CC IsoId=Q9ERG0-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=Q9ERG0-2; Sequence=VSP_003118;
CC -!- TISSUE SPECIFICITY: Highly expressed in the small intestine, including
CC the duodenum, jejunum, and ileum. Low expression in the liver and very
CC low expressed in the heart, spleen, lung, brain, and pancreas
CC (PubMed:29880681). Isoform Alpha is highly expressed in embryos from
CC day 7-11 and in adult spleen and lung. Isoform Beta expression is
CC highest in adult kidney, testis, lung and liver, intermediate in heart,
CC brain, spleen, skeletal muscle and low in embryos.
CC {ECO:0000269|PubMed:29880681}.
CC -!- DOMAIN: Contains at least 2 actin-binding domains, one on each side of
CC the LIM domain. Both domains bind actin monomers and filaments. The C-
CC terminal domain binds filaments more efficiently than the N-terminus
CC (By similarity). {ECO:0000250|UniProtKB:Q9UHB6}.
CC -!- PTM: Phosphorylation of the C-terminal region by MAPK1/MAPK3 reduces
CC its association with F-actin and contributes to actin filament
CC reorganization and enhances cell motility.
CC {ECO:0000269|PubMed:17875928}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display reduced dietary
CC cholesterol absorption. {ECO:0000269|PubMed:29880681}.
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DR EMBL; AF307844; AAG31147.1; -; mRNA.
DR EMBL; AF307845; AAG31148.1; -; mRNA.
DR EMBL; BC031490; AAH31490.1; -; mRNA.
DR EMBL; CH466550; EDL04110.1; -; Genomic_DNA.
DR CCDS; CCDS37206.1; -. [Q9ERG0-2]
DR CCDS; CCDS49729.1; -. [Q9ERG0-1]
DR RefSeq; NP_001107017.1; NM_001113545.1. [Q9ERG0-1]
DR AlphaFoldDB; Q9ERG0; -.
DR SMR; Q9ERG0; -.
DR BioGRID; 211164; 138.
DR DIP; DIP-29634N; -.
DR ELM; Q9ERG0; -.
DR IntAct; Q9ERG0; 136.
DR STRING; 10090.ENSMUSP00000073371; -.
DR iPTMnet; Q9ERG0; -.
DR PhosphoSitePlus; Q9ERG0; -.
DR SwissPalm; Q9ERG0; -.
DR jPOST; Q9ERG0; -.
DR MaxQB; Q9ERG0; -.
DR PaxDb; Q9ERG0; -.
DR PeptideAtlas; Q9ERG0; -.
DR PRIDE; Q9ERG0; -.
DR ProteomicsDB; 286199; -. [Q9ERG0-1]
DR ProteomicsDB; 286200; -. [Q9ERG0-2]
DR Antibodypedia; 14200; 337 antibodies from 33 providers.
DR DNASU; 65970; -.
DR Ensembl; ENSMUST00000073691; ENSMUSP00000073371; ENSMUSG00000023022. [Q9ERG0-1]
DR Ensembl; ENSMUST00000109024; ENSMUSP00000104652; ENSMUSG00000023022. [Q9ERG0-2]
DR GeneID; 65970; -.
DR KEGG; mmu:65970; -.
DR UCSC; uc007xqh.3; mouse. [Q9ERG0-1]
DR CTD; 51474; -.
DR MGI; MGI:1920992; Lima1.
DR VEuPathDB; HostDB:ENSMUSG00000023022; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000158313; -.
DR HOGENOM; CLU_021314_0_0_1; -.
DR InParanoid; Q9ERG0; -.
DR OMA; PEVCISH; -.
DR PhylomeDB; Q9ERG0; -.
DR TreeFam; TF350273; -.
DR BioGRID-ORCS; 65970; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Lima1; mouse.
DR PRO; PR:Q9ERG0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9ERG0; protein.
DR Bgee; ENSMUSG00000023022; Expressed in undifferentiated genital tubercle and 253 other tissues.
DR ExpressionAtlas; Q9ERG0; baseline and differential.
DR Genevisible; Q9ERG0; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IMP:UniProtKB.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0031529; P:ruffle organization; IMP:UniProtKB.
DR InterPro; IPR028740; EPLIN.
DR InterPro; IPR045268; LIMA-like.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24206; PTHR24206; 2.
DR PANTHER; PTHR24206:SF57; PTHR24206:SF57; 2.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative promoter usage; Cell membrane;
KW Cell projection; Cholesterol metabolism; Cytoplasm; Cytoskeleton;
KW LIM domain; Lipid metabolism; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Steroid metabolism; Sterol metabolism; Zinc.
FT CHAIN 1..753
FT /note="LIM domain and actin-binding protein 1"
FT /id="PRO_0000075731"
FT DOMAIN 386..446
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 46..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..511
FT /note="Required for interaction with MYO5B"
FT /evidence="ECO:0000269|PubMed:29880681"
FT REGION 505..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..166
FT /note="Required for interaction with NPC1L1"
FT /evidence="ECO:0000269|PubMed:29880681"
FT COMPBIAS 46..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17875928,
FT ECO:0007744|PubMed:17242355"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 437
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17875928"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB6"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17875928"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..160
FT /note="Missing (in isoform Alpha)"
FT /evidence="ECO:0000303|PubMed:11179679"
FT /id="VSP_003118"
FT MUTAGEN 164..166
FT /note="CLG->AAA: Decreases interaction with NPC1L1."
FT /evidence="ECO:0000269|PubMed:29880681"
FT MUTAGEN 360
FT /note="S->A: Abolished phosphorylation by MAPK1/MAPK3."
FT /evidence="ECO:0000269|PubMed:17875928"
FT MUTAGEN 602
FT /note="S->A: Reduced phosphorylation by MAPK1/MAPK3."
FT /evidence="ECO:0000269|PubMed:17875928"
FT MUTAGEN 692
FT /note="S->A: Reduced phosphorylation by MAPK1/MAPK3."
FT /evidence="ECO:0000269|PubMed:17875928"
FT CONFLICT 216
FT /note="S -> N (in Ref. 1; AAG31148)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="T -> A (in Ref. 1; AAG31147)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="P -> S (in Ref. 1; AAG31147)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="V -> A (in Ref. 1; AAG31147)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="G -> S (in Ref. 1; AAG31147)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="A -> T (in Ref. 1; AAG31147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 753 AA; 84060 MW; 79F98E47C100CF22 CRC64;
MESTPFNRRQ WTSLSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEEANM ERKKNNPESL
PQHFRRGTLS VLKKKWENPV AGAEFHTDSL PNSSSEGGHT ADYPPAEVTD KPAPGVRADR
EEHTQPKPRF GSRPEAVIQS RYPRSENSHD FKAQATESQK MENCLGDSRH EAEKPETSEN
TETSGKIEKY NVPLNRLKMM FEKGEHNQTK SLWTQSRNAG GRRLSENNCS LDDWEIGAGH
LSSSAFNSEK NESKRNLELP RLSETSIKDR MAKYQAAVSK QSSPASYTNE LKTSESKTHK
WEQKENVPPG PEACSVHQEG SKVSTTENSL VALSVPAEDD TCNSQVKSEA QQPMHPKPLS
PDARTSSLPE SSPSKTAKKF QAPAKESCVE CQKTVYPMER LLANQQVFHI SCFRCSYCNN
KLSLGTYASL HGRIYCKPHF NQLFKSKGNY DEGFGHKQHK DLWASKSDNE ETLGRPAQPP
NAGESPHSPG VEDAPIAKVG VLAASMEAKA SSQREREDKP AETKKLRIAW PPPAELGGSG
SALEEGIKVS KPKWPPEDDV CKTEAPEDVD LDLKKLRRSS SLKERSRPFT VAASFRTSSI
KSPKASSPSL RKGWSESEQS EEFGGGIATM ERKQTENARP SGEKENVGKS RWQGEEVPRS
KDRSSFELES ENFMENGANI AEDDNHVHAQ QSPLEPEAPG WSGFVDTTAA KEFTTQNQKS
QDVGFWEGEV VRELSVEEQI KRNRYYDEDE DEE
