ANXA2_MOUSE
ID ANXA2_MOUSE Reviewed; 339 AA.
AC P07356;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Annexin A2;
DE AltName: Full=Annexin II;
DE AltName: Full=Annexin-2;
DE AltName: Full=Calpactin I heavy chain;
DE AltName: Full=Calpactin-1 heavy chain;
DE AltName: Full=Chromobindin-8;
DE AltName: Full=Lipocortin II;
DE AltName: Full=Placental anticoagulant protein IV;
DE Short=PAP-IV;
DE AltName: Full=Protein I;
DE AltName: Full=p36;
GN Name=Anxa2; Synonyms=Anx2, Cal1h;
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].
RX PubMed=3013423; DOI=10.1016/0092-8674(86)90737-3;
RA Saris C.J.M., Tack B.F., Kristensen T., Glenney J.R. Jr., Hunter T.;
RT "The cDNA sequence for the protein-tyrosine kinase substrate p36 (calpactin
RT I heavy chain) reveals a multidomain protein with internal repeats.";
RL Cell 46:201-212(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16 AND 322-339.
RX PubMed=2138915; DOI=10.1021/bi00457a019;
RA Amiguet P., D'Eustachio P., Kristensen T., Wetsel R.A., Saris C.J.M.,
RA Hunter T., Chaplin D.D., Tack B.F.;
RT "Structure and chromosome assignment of the murine p36 (calpactin I heavy
RT chain) gene.";
RL Biochemistry 29:1226-1232(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX PubMed=8634333; DOI=10.1016/0167-4781(95)00238-3;
RA Fey M.F., Moffat G.J., Vik D.P., Meisenhelder J., Saris C.J., Hunter T.,
RA Tack B.F.;
RT "Complete structure of the murine p36 (annexin II) gene. Identification of
RT mRNAs for both the murine and the human gene with alternatively spliced 5'
RT noncoding exons.";
RL Biochim. Biophys. Acta 1306:160-170(1996).
RN [5]
RP INTERACTION WITH DYSF.
RX PubMed=14506282; DOI=10.1074/jbc.m307247200;
RA Lennon N.J., Kho A., Bacskai B.J., Perlmutter S.L., Hyman B.T.,
RA Brown R.H. Jr.;
RT "Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal
RT wound-healing.";
RL J. Biol. Chem. 278:50466-50473(2003).
RN [6]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, 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 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 INTERACTION WITH APPL2 AND APPL1.
RX PubMed=21645192; DOI=10.1111/j.1600-0854.2011.01226.x;
RA Urbanska A., Sadowski L., Kalaidzidis Y., Miaczynska M.;
RT "Biochemical characterization of APPL endosomes: the role of annexin A2 in
RT APPL membrane recruitment.";
RL Traffic 12:1227-1241(2011).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22848640; DOI=10.1371/journal.pone.0041865;
RA Seidah N.G., Poirier S., Denis M., Parker R., Miao B., Mapelli C., Prat A.,
RA Wassef H., Davignon J., Hajjar K.A., Mayer G.;
RT "Annexin A2 is a natural extrahepatic inhibitor of the PCSK9-induced LDL
RT receptor degradation.";
RL PLoS ONE 7:E41865-E41865(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-49; LYS-152 AND LYS-227, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Calcium-regulated membrane-binding protein whose affinity for
CC calcium is greatly enhanced by anionic phospholipids. It binds two
CC calcium ions with high affinity. May be involved in heat-stress
CC response (By similarity). Inhibits PCSK9-enhanced LDLR degradation,
CC probably reduces PCSK9 protein levels via a translational mechanism but
CC also competes with LDLR for binding with PCSK9 (PubMed:22848640).
CC {ECO:0000250|UniProtKB:P07355, ECO:0000269|PubMed:22848640}.
CC -!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2
CC heavy chains of ANXA2/p36 (By similarity). Interacts with ATP1B1 (By
CC similarity). Interacts with DYSF (PubMed:14506282). Interacts with
CC COCH. Interacts (via repeat Annexin 1) with PCSK9 (via the C-terminal
CC domain); the interaction inhibits the degradation of LDLR. Interacts
CC with CEACAM1 (via the cytoplasmic domain); this interaction is
CC regulated by phosphorylation of CEACAM1 (By similarity). Interacts with
CC APPL2 and APPL1; targets APPL2 to endosomes and acting in parallel to
CC RAB5A (PubMed:21645192). Interacts with S100A4 (By similarity).
CC {ECO:0000250|UniProtKB:A2SW69, ECO:0000250|UniProtKB:P07355,
CC ECO:0000250|UniProtKB:Q6TEQ7, ECO:0000269|PubMed:14506282,
CC ECO:0000269|PubMed:21645192}.
CC -!- INTERACTION:
CC P07356; P08207: S100a10; NbExp=2; IntAct=EBI-738510, EBI-643986;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the lamina
CC beneath the plasma membrane.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- DISRUPTION PHENOTYPE: Animals show a 40% increase of LDL-cholesterol
CC levels in plasma. {ECO:0000269|PubMed:22848640}.
CC -!- MISCELLANEOUS: It may cross-link plasma membrane phospholipids with
CC actin and the cytoskeleton and be involved with exocytosis.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Red velvet - Issue 86 of
CC September 2007;
CC URL="https://web.expasy.org/spotlight/back_issues/086";
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DR EMBL; M14044; AAA37360.1; -; mRNA.
DR EMBL; BC003327; AAH03327.1; -; mRNA.
DR EMBL; BC005763; AAH05763.1; -; mRNA.
DR EMBL; M33321; AAA37361.1; -; Genomic_DNA.
DR EMBL; M33322; AAA37362.1; -; Genomic_DNA.
DR EMBL; D10024; BAA00914.1; -; mRNA.
DR EMBL; S82177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23316.1; -.
DR PIR; A23943; LUMS36.
DR RefSeq; NP_031611.1; NM_007585.3.
DR RefSeq; XP_006510859.1; XM_006510796.2.
DR PDB; 4HRE; X-ray; 2.79 A; A/B/C/D=1-339.
DR PDBsum; 4HRE; -.
DR AlphaFoldDB; P07356; -.
DR SMR; P07356; -.
DR BioGRID; 198448; 40.
DR ComplexPortal; CPX-141; ANXA2-PCSK9 complex.
DR ComplexPortal; CPX-898; Annexin A2 - S100-A10 complex.
DR ComplexPortal; CPX-899; SMARCA3 - Annexin A2 - S100-A10 complex.
DR ComplexPortal; CPX-905; AHNAK - Annexin A2 - S100-A10 complex.
DR CORUM; P07356; -.
DR IntAct; P07356; 23.
DR MINT; P07356; -.
DR STRING; 10090.ENSMUSP00000034756; -.
DR TCDB; 9.A.48.1.1; the unconventional protein secretion (ups) system.
DR iPTMnet; P07356; -.
DR PhosphoSitePlus; P07356; -.
DR SwissPalm; P07356; -.
DR REPRODUCTION-2DPAGE; IPI00468203; -.
DR REPRODUCTION-2DPAGE; P07356; -.
DR SWISS-2DPAGE; P07356; -.
DR CPTAC; non-CPTAC-3634; -.
DR EPD; P07356; -.
DR jPOST; P07356; -.
DR PaxDb; P07356; -.
DR PeptideAtlas; P07356; -.
DR PRIDE; P07356; -.
DR ProteomicsDB; 281892; -.
DR Antibodypedia; 3808; 872 antibodies from 46 providers.
DR DNASU; 12306; -.
DR Ensembl; ENSMUST00000034756; ENSMUSP00000034756; ENSMUSG00000032231.
DR GeneID; 12306; -.
DR KEGG; mmu:12306; -.
DR UCSC; uc009qng.1; mouse.
DR CTD; 302; -.
DR MGI; MGI:88246; Anxa2.
DR VEuPathDB; HostDB:ENSMUSG00000032231; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000154257; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; P07356; -.
DR OMA; EVDLMRI; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P07356; -.
DR TreeFam; TF105452; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
DR BioGRID-ORCS; 12306; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Anxa2; mouse.
DR PRO; PR:P07356; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P07356; protein.
DR Bgee; ENSMUSG00000032231; Expressed in substantia propria of cornea and 256 other tissues.
DR ExpressionAtlas; P07356; baseline and differential.
DR Genevisible; P07356; MM.
DR GO; GO:1990665; C:AnxA2-p11 complex; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0044354; C:macropinosome; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IDA:BHF-UCL.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990667; C:PCSK9-AnxA2 complex; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0098797; C:plasma membrane protein complex; IPI:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0044730; F:bone sialoprotein binding; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0044548; F:S100 protein binding; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0046790; F:virion binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0007589; P:body fluid secretion; ISO:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0042730; P:fibrinolysis; IMP:MGI.
DR GO; GO:0001765; P:membrane raft assembly; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IMP:BHF-UCL.
DR GO; GO:0002091; P:negative regulation of receptor internalization; IEA:Ensembl.
DR GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR GO; GO:0051099; P:positive regulation of binding; IMP:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; IC:ComplexPortal.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:1905581; P:positive regulation of low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:1905597; P:positive regulation of low-density lipoprotein particle receptor binding; IMP:BHF-UCL.
DR GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IMP:BHF-UCL.
DR GO; GO:1905686; P:positive regulation of plasma membrane repair; IC:ComplexPortal.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IMP:BHF-UCL.
DR GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0044090; P:positive regulation of vacuole organization; IEA:Ensembl.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IDA:ComplexPortal.
DR GO; GO:0006900; P:vesicle budding from membrane; IEA:Ensembl.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR002389; ANX2.
DR PANTHER; PTHR10502:SF18; PTHR10502:SF18; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00198; ANNEXINII.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 4.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Annexin; Basement membrane; Calcium;
KW Calcium/phospholipid-binding; Extracellular matrix; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P04272"
FT CHAIN 2..339
FT /note="Annexin A2"
FT /id="PRO_0000067471"
FT REPEAT 33..104
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 105..176
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 189..261
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 265..336
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REGION 2..24
FT /note="S100A10-binding site"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P04272"
FT MOD_RES 24
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT MOD_RES 26
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT MOD_RES 49
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT MOD_RES 199
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 227
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07355"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:4HRE"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:4HRE"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:4HRE"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:4HRE"
FT HELIX 325..335
FT /evidence="ECO:0007829|PDB:4HRE"
SQ SEQUENCE 339 AA; 38676 MW; 4407E572097FB2C0 CRC64;
MSTVHEILCK LSLEGDHSTP PSAYGSVKPY TNFDAERDAL NIETAVKTKG VDEVTIVNIL
TNRSNVQRQD IAFAYQRRTK KELPSALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG
LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA
EDGSVIDYEL IDQDARELYD AGVKRKGTDV PKWISIMTER SVCHLQKVFE RYKSYSPYDM
LESIKKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD
