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Annexin A6 (67 kDa calelectrin) (Annexin VI) (Annexin-6) (Calphobindin-II) (CPB-II) (Chromobindin-20) (Lipocortin VI) (Protein III) (p68) (p70)

 ANXA6_HUMAN             Reviewed;         673 AA.
P08133; B7Z8A7; D3DQH4; E9PGK1; Q6ZT79;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 192.
RecName: Full=Annexin A6;
AltName: Full=67 kDa calelectrin;
AltName: Full=Annexin VI;
AltName: Full=Annexin-6;
AltName: Full=Calphobindin-II;
Short=CPB-II;
AltName: Full=Chromobindin-20;
AltName: Full=Lipocortin VI;
AltName: Full=Protein III;
AltName: Full=p68;
AltName: Full=p70;
Name=ANXA6; Synonyms=ANX6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3258820;
Crompton M.R., Owens R.J., Totty N.F., Moss S.E., Waterfield M.D.,
Crumpton M.J.;
"Primary structure of the human, membrane-associated Ca2+-binding
protein p68 a novel member of a protein family.";
EMBO J. 7:21-27(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
PubMed=2963335; DOI=10.1073/pnas.85.3.664;
Suedhof T.C., Slaughter C.A., Leznicki I., Barjon P., Reynolds G.A.;
"Human 67-kDa calelectrin contains a duplication of four repeats found
in 35-kDa lipocortins.";
Proc. Natl. Acad. Sci. U.S.A. 85:664-668(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2528541;
Iwasaki A., Suda M., Watanabe M., Nakao H., Hattori Y., Nagoya T.,
Saino Y., Shidara Y., Maki M.;
"Structure and expression of cDNA for calphobindin II, a human
placental coagulation inhibitor.";
J. Biochem. 106:43-49(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-673.
PubMed=2139657; DOI=10.1093/oxfordjournals.jbchem.a123009;
Yoshizaki H., Mizoguchi T., Arai K., Shiratsuchi M., Shidara Y.,
Maki M.;
"Structure and properties of calphobindin II, an anticoagulant protein
from human placenta.";
J. Biochem. 107:43-50(1990).
[9]
PROTEIN SEQUENCE OF 485-499.
TISSUE=Adipocyte;
PubMed=15242332; DOI=10.1042/BJ20040647;
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific
fragmentation of polymerase I and transcript release factor (PTRF) at
the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-68; LYS-75; LYS-81;
LYS-306; LYS-370; LYS-418; LYS-483 AND LYS-620, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; TYR-30 AND SER-537,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
PubMed=8709144; DOI=10.1006/jmbi.1996.0426;
Benz J., Bergner A., Hofmann A., Demange P., Goettig P., Liemann S.,
Huber R., Voges D.;
"The structure of recombinant human annexin VI in crystals and
membrane-bound.";
J. Mol. Biol. 260:638-643(1996).
-!- FUNCTION: May associate with CD21. May regulate the release of
Ca(2+) from intracellular stores.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
{ECO:0000269|PubMed:17081065}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P08133-1; Sequence=Displayed;
Name=2;
IsoId=P08133-2; Sequence=VSP_045480;
Note=No experimental confirmation available.;
-!- INDUCTION: By Epstein-Barr virus (EBV).
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- PTM: Phosphorylated in response to growth factor stimulation.
-!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
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EMBL; Y00097; CAA68286.1; -; mRNA.
EMBL; J03578; AAA35656.1; -; mRNA.
EMBL; D00510; BAA00400.1; -; mRNA.
EMBL; AK126836; BAC86715.1; ALT_SEQ; mRNA.
EMBL; AK303078; BAH13893.1; -; mRNA.
EMBL; AC008641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW61684.1; -; Genomic_DNA.
EMBL; CH471062; EAW61686.1; -; Genomic_DNA.
EMBL; BC017046; AAH17046.1; -; mRNA.
CCDS; CCDS47315.1; -. [P08133-1]
CCDS; CCDS54941.1; -. [P08133-2]
PIR; JU0032; AQHU68.
RefSeq; NP_001146.2; NM_001155.4. [P08133-1]
RefSeq; NP_001180473.1; NM_001193544.1. [P08133-2]
UniGene; Hs.412117; -.
PDB; 1M9I; X-ray; 2.65 A; A=2-673.
PDBsum; 1M9I; -.
ProteinModelPortal; P08133; -.
SMR; P08133; -.
BioGrid; 106806; 38.
CORUM; P08133; -.
IntAct; P08133; 14.
MINT; MINT-4999263; -.
STRING; 9606.ENSP00000346550; -.
TCDB; 1.A.31.1.2; the annexin (annexin) family.
iPTMnet; P08133; -.
PhosphoSitePlus; P08133; -.
SwissPalm; P08133; -.
BioMuta; ANXA6; -.
REPRODUCTION-2DPAGE; IPI00221226; -.
UCD-2DPAGE; P08133; -.
EPD; P08133; -.
MaxQB; P08133; -.
PaxDb; P08133; -.
PeptideAtlas; P08133; -.
PRIDE; P08133; -.
DNASU; 309; -.
Ensembl; ENST00000354546; ENSP00000346550; ENSG00000197043. [P08133-1]
Ensembl; ENST00000523714; ENSP00000430517; ENSG00000197043. [P08133-2]
GeneID; 309; -.
KEGG; hsa:309; -.
UCSC; uc003ltl.3; human. [P08133-1]
CTD; 309; -.
DisGeNET; 309; -.
EuPathDB; HostDB:ENSG00000197043.13; -.
GeneCards; ANXA6; -.
HGNC; HGNC:544; ANXA6.
HPA; CAB005077; -.
HPA; HPA002462; -.
HPA; HPA009650; -.
MIM; 114070; gene.
neXtProt; NX_P08133; -.
OpenTargets; ENSG00000197043; -.
PharmGKB; PA24834; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P08133; -.
KO; K17094; -.
OMA; REIFRTK; -.
OrthoDB; EOG091G0H6H; -.
PhylomeDB; P08133; -.
TreeFam; TF105452; -.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
ChiTaRS; ANXA6; human.
EvolutionaryTrace; P08133; -.
GeneWiki; ANXA6; -.
GenomeRNAi; 309; -.
PRO; PR:P08133; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000197043; -.
CleanEx; HS_ANXA6; -.
ExpressionAtlas; P08133; baseline and differential.
Genevisible; P08133; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
GO; GO:0015276; F:ligand-gated ion channel activity; IMP:UniProtKB.
GO; GO:0008289; F:lipid binding; IMP:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IMP:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; IMP:UniProtKB.
GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IMP:UniProtKB.
GO; GO:0006937; P:regulation of muscle contraction; IEA:Ensembl.
Gene3D; 1.10.220.10; -; 8.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002393; ANX6.
PANTHER; PTHR10502:SF19; PTHR10502:SF19; 2.
Pfam; PF00191; Annexin; 8.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00202; ANNEXINVI.
SMART; SM00335; ANX; 8.
PROSITE; PS00223; ANNEXIN; 8.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Annexin; Calcium;
Calcium/phospholipid-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:2139657}.
CHAIN 2 673 Annexin A6.
/FTId=PRO_0000067494.
REPEAT 29 89 Annexin 1.
REPEAT 101 161 Annexin 2.
REPEAT 185 245 Annexin 3.
REPEAT 260 320 Annexin 4.
REPEAT 372 432 Annexin 5.
REPEAT 444 504 Annexin 6.
REPEAT 533 593 Annexin 7.
REPEAT 608 668 Annexin 8.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 30 30 Phosphotyrosine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 63 63 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 68 68 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 75 75 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 81 81 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 201 201 Phosphotyrosine.
{ECO:0000250|UniProtKB:P14824}.
MOD_RES 306 306 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 370 370 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 418 418 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000250|UniProtKB:P48037}.
MOD_RES 483 483 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 537 537 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 620 620 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 32 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045480.
CONFLICT 221 221 T -> A (in Ref. 4; BAH13893).
{ECO:0000305}.
CONFLICT 226 227 IE -> MK (in Ref. 2; AAA35656).
{ECO:0000305}.
CONFLICT 248 248 C -> R (in Ref. 4; BAC86715).
{ECO:0000305}.
CONFLICT 555 555 S -> T (in Ref. 2; AAA35656).
{ECO:0000305}.
CONFLICT 619 619 E -> D (in Ref. 1; CAA68286).
{ECO:0000305}.
HELIX 22 32 {ECO:0000244|PDB:1M9I}.
STRAND 34 37 {ECO:0000244|PDB:1M9I}.
HELIX 40 47 {ECO:0000244|PDB:1M9I}.
HELIX 52 66 {ECO:0000244|PDB:1M9I}.
HELIX 70 77 {ECO:0000244|PDB:1M9I}.
HELIX 80 90 {ECO:0000244|PDB:1M9I}.
HELIX 93 105 {ECO:0000244|PDB:1M9I}.
STRAND 106 109 {ECO:0000244|PDB:1M9I}.
HELIX 112 121 {ECO:0000244|PDB:1M9I}.
HELIX 124 137 {ECO:0000244|PDB:1M9I}.
HELIX 142 149 {ECO:0000244|PDB:1M9I}.
HELIX 152 163 {ECO:0000244|PDB:1M9I}.
HELIX 174 187 {ECO:0000244|PDB:1M9I}.
TURN 188 190 {ECO:0000244|PDB:1M9I}.
STRAND 191 193 {ECO:0000244|PDB:1M9I}.
HELIX 196 205 {ECO:0000244|PDB:1M9I}.
HELIX 208 221 {ECO:0000244|PDB:1M9I}.
STRAND 222 224 {ECO:0000244|PDB:1M9I}.
HELIX 226 230 {ECO:0000244|PDB:1M9I}.
TURN 231 233 {ECO:0000244|PDB:1M9I}.
HELIX 236 262 {ECO:0000244|PDB:1M9I}.
STRAND 264 268 {ECO:0000244|PDB:1M9I}.
HELIX 271 280 {ECO:0000244|PDB:1M9I}.
TURN 281 285 {ECO:0000244|PDB:1M9I}.
HELIX 286 296 {ECO:0000244|PDB:1M9I}.
STRAND 297 299 {ECO:0000244|PDB:1M9I}.
HELIX 301 306 {ECO:0000244|PDB:1M9I}.
HELIX 311 321 {ECO:0000244|PDB:1M9I}.
HELIX 333 348 {ECO:0000244|PDB:1M9I}.
HELIX 365 376 {ECO:0000244|PDB:1M9I}.
STRAND 377 380 {ECO:0000244|PDB:1M9I}.
HELIX 383 391 {ECO:0000244|PDB:1M9I}.
HELIX 395 409 {ECO:0000244|PDB:1M9I}.
HELIX 413 420 {ECO:0000244|PDB:1M9I}.
HELIX 424 433 {ECO:0000244|PDB:1M9I}.
HELIX 436 448 {ECO:0000244|PDB:1M9I}.
STRAND 449 452 {ECO:0000244|PDB:1M9I}.
HELIX 455 464 {ECO:0000244|PDB:1M9I}.
HELIX 467 481 {ECO:0000244|PDB:1M9I}.
HELIX 485 492 {ECO:0000244|PDB:1M9I}.
HELIX 495 504 {ECO:0000244|PDB:1M9I}.
HELIX 516 530 {ECO:0000244|PDB:1M9I}.
HELIX 535 537 {ECO:0000244|PDB:1M9I}.
HELIX 546 553 {ECO:0000244|PDB:1M9I}.
HELIX 556 568 {ECO:0000244|PDB:1M9I}.
STRAND 569 572 {ECO:0000244|PDB:1M9I}.
HELIX 574 581 {ECO:0000244|PDB:1M9I}.
HELIX 584 611 {ECO:0000244|PDB:1M9I}.
STRAND 613 616 {ECO:0000244|PDB:1M9I}.
HELIX 619 628 {ECO:0000244|PDB:1M9I}.
TURN 630 633 {ECO:0000244|PDB:1M9I}.
HELIX 634 645 {ECO:0000244|PDB:1M9I}.
HELIX 649 656 {ECO:0000244|PDB:1M9I}.
HELIX 659 668 {ECO:0000244|PDB:1M9I}.
SEQUENCE 673 AA; 75873 MW; 90F47474F7F6D7B6 CRC64;
MAKPAQGAKY RGSIHDFPGF DPNQDAEALY TAMKGFGSDK EAILDIITSR SNRQRQEVCQ
SYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYCDAKE IKDAISGIGT DEKCLIEILA
SRTNEQMHQL VAAYKDAYER DLEADIIGDT SGHFQKMLVV LLQGTREEDD VVSEDLVQQD
VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK
LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS
LYSMIKNDTS GEYKKTLLKL SGGDDDAAGQ FFPEAAQVAY QMWELSAVAR VELKGTVRPA
NDFNPDADAK ALRKAMKGLG TDEDTIIDII THRSNVQRQQ IRQTFKSHFG RDLMTDLKSE
ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI RAINEAYKED
YHKSLEDALS SDTSGHFRRI LISLATGHRE EGGENLDQAR EDAQVAAEIL EIADTPSGDK
TSLETRFMTI LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDAF VAIVQSVKNK
PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGD
FLKALLALCG GED


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