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Agglutinin-like protein 9 (Adhesin 9)

 ALS9_CANAL              Reviewed;        1890 AA.
A0A1D8PQ86; Q7ZA78; Q7ZA79;
15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
18-JAN-2017, sequence version 1.
22-NOV-2017, entry version 8.
RecName: Full=Agglutinin-like protein 9;
AltName: Full=Adhesin 9;
Flags: Precursor;
Name=ALS9; Synonyms=ALS11; OrderedLocusNames=CAALFM_C603710WA;
ORFNames=orf19.13164, orf19.5742;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=14523127; DOI=10.1099/mic.0.26495-0;
Zhao X., Pujol C., Soll D.R., Hoyer L.L.;
"Allelic variation in the contiguous loci encoding Candida albicans
ALS5, ALS1 and ALS9.";
Microbiology 149:2947-2960(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[3]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[5]
PREDICTION OF GPI-ANCHOR.
PubMed=12845604; DOI=10.1002/yea.1007;
De Groot P.W., Hellingwerf K.J., Klis F.M.;
"Genome-wide identification of fungal GPI proteins.";
Yeast 20:781-796(2003).
[6]
FUNCTION, AND DOMAIN.
PubMed=15128742; DOI=10.1074/jbc.M401929200;
Sheppard D.C., Yeaman M.R., Welch W.H., Phan Q.T., Fu Y.,
Ibrahim A.S., Filler S.G., Zhang M., Waring A.J., Edwards J.E. Jr.;
"Functional and structural diversity in the Als protein family of
Candida albicans.";
J. Biol. Chem. 279:30480-30489(2004).
[7]
FUNCTION.
PubMed=17510860; DOI=10.1080/13693780701299333;
Klotz S.A., Gaur N.K., De Armond R., Sheppard D., Khardori N.,
Edwards J.E. Jr., Lipke P.N., El-Azizi M.;
"Candida albicans Als proteins mediate aggregation with bacteria and
yeasts.";
Med. Mycol. 45:363-370(2007).
[8]
FUNCTION.
PubMed=17600078; DOI=10.1099/mic.0.2006/005017-0;
Zhao X., Oh S.H., Hoyer L.L.;
"Unequal contribution of ALS9 alleles to adhesion between Candida
albicans and human vascular endothelial cells.";
Microbiology 153:2342-2350(2007).
[9]
FUNCTION.
PubMed=22321066; DOI=10.1111/j.1574-695X.2012.00941.x;
Aoki W., Kitahara N., Miura N., Morisaka H., Kuroda K., Ueda M.;
"Profiling of adhesive properties of the agglutinin-like sequence
(ALS) protein family, a virulent attribute of Candida albicans.";
FEMS Immunol. Med. Microbiol. 65:121-124(2012).
[10]
FUNCTION.
PubMed=22429754; DOI=10.1111/j.1439-0507.2012.02188.x;
Monroy-Perez E., Sainz-Espunes T., Paniagua-Contreras G.,
Negrete-Abascal E., Rodriguez-Moctezuma J.R., Vaca S.;
"Frequency and expression of ALS and HWP1 genotypes in Candida
albicans strains isolated from Mexican patients suffering from vaginal
candidosis.";
Mycoses 55:E151-E157(2012).
[11] {ECO:0000244|PDB:2Y7L, ECO:0000244|PDB:2Y7M, ECO:0000244|PDB:2Y7N}
X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 18-328, AND DISULFIDE BONDS.
PubMed=21896717; DOI=10.1073/pnas.1103496108;
Salgado P.S., Yan R., Taylor J.D., Burchell L., Jones R., Hoyer L.L.,
Matthews S.J., Simpson P.J., Cota E.;
"Structural basis for the broad specificity to host-cell ligands by
the pathogenic fungus Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 108:15775-15779(2011).
-!- FUNCTION: Cell surface adhesion protein which mediates both yeast-
to-host tissue adherence and yeast aggregation. Plays an important
role in the pathogenesis of C.albicans infections
(PubMed:17510860, PubMed:22321066, PubMed:22429754). Allele ALS9-2
contributes to endothelial cell adhesion, whereas ALS9-1 does not
(PubMed:17600078). {ECO:0000269|PubMed:17510860,
ECO:0000269|PubMed:17600078, ECO:0000269|PubMed:22321066,
ECO:0000269|PubMed:22429754}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
Secreted, cell wall. Note=Identified as covalently-linked GPI-
modified cell wall protein (GPI-CWP) in the outer cell wall layer.
{ECO:0000305|PubMed:12845604}.
-!- DOMAIN: Each ALS protein has a similar three-domain structure,
including a N-ter domain of 433-436 amino acids that is 55-90
percent identical across the family and which mediates adherence
to various materials; a central domain of variable numbers of
tandemly repeated copies of a 36 amino acid motif; and a C-ter;
domain that is relatively variable in length and sequence across
the family. {ECO:0000269|PubMed:15128742}.
-!- PTM: N-glycosylated and O-glycosylated.
-!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
reticulum and serves to target the protein to the cell surface.
There, the glucosamine-inositol phospholipid moiety is cleaved off
and the GPI-modified mannoprotein is covalently attached via its
lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer
cell wall layer. {ECO:0000305|PubMed:12845604}.
-!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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EMBL; AY269422; AAP34370.1; -; Genomic_DNA.
EMBL; AY269423; AAP34371.1; -; Genomic_DNA.
EMBL; CP017628; AOW30298.1; -; Genomic_DNA.
RefSeq; XP_718078.2; XM_712985.2.
PDB; 2Y7L; X-ray; 1.49 A; A=18-328.
PDB; 2Y7M; X-ray; 1.98 A; A=18-328.
PDB; 2Y7N; X-ray; 2.00 A; A=18-328.
PDB; 2Y7O; X-ray; 1.75 A; A=18-328.
PDB; 2YLH; X-ray; 1.70 A; A=18-328.
PDBsum; 2Y7L; -.
PDBsum; 2Y7M; -.
PDBsum; 2Y7N; -.
PDBsum; 2Y7O; -.
PDBsum; 2YLH; -.
SMR; A0A1D8PQ86; -.
EnsemblFungi; AOW30298; AOW30298; CAALFM_C603710WA.
GeneID; 3640281; -.
KEGG; cal:CAALFM_C603710WA; -.
CGD; CAL0000194750; ALS9.
Proteomes; UP000000559; Chromosome 6.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0007155; P:cell adhesion; IDA:CGD.
GO; GO:0043710; P:cell adhesion involved in multi-species biofilm formation; IMP:CGD.
GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
InterPro; IPR008966; Adhesion_dom_sf.
InterPro; IPR008440; Agglutinin-like_ALS_rpt.
InterPro; IPR024672; Agglutinin-like_N.
InterPro; IPR033504; ALS.
PANTHER; PTHR33793; PTHR33793; 6.
Pfam; PF05792; Candida_ALS; 19.
Pfam; PF11766; Candida_ALS_N; 1.
SMART; SM01056; Candida_ALS_N; 1.
SUPFAM; SSF49401; SSF49401; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell membrane; Cell wall;
Complete proteome; Disulfide bond; Glycoprotein; GPI-anchor;
Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal;
Virulence.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 1867 Agglutinin-like protein 9.
/FTId=PRO_0000439168.
PROPEP 1868 1890 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000439169.
REPEAT 400 431 ALS 1.
REPEAT 437 468 ALS 2.
REPEAT 473 504 ALS 3.
REPEAT 509 540 ALS 4.
REPEAT 545 576 ALS 5.
REPEAT 581 612 ALS 6.
REPEAT 617 648 ALS 7.
REPEAT 653 684 ALS 8.
REPEAT 689 720 ALS 9.
REPEAT 725 756 ALS 10.
REPEAT 761 792 ALS 11.
REPEAT 797 828 ALS 12.
REPEAT 833 864 ALS 13.
REPEAT 869 900 ALS 14.
REPEAT 905 936 ALS 15.
REPEAT 941 972 ALS 16.
REPEAT 977 1008 ALS 17.
REPEAT 1013 1044 ALS 18.
REPEAT 1049 1077 ALS 19.
COMPBIAS 329 1606 Thr-rich. {ECO:0000255|PROSITE-
ProRule:PRU00017}.
COMPBIAS 1092 1871 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
LIPID 1867 1867 GPI-anchor amidated aspartate.
{ECO:0000255}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1175 1175 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1475 1475 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1818 1818 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1821 1821 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 73 150 {ECO:0000244|PDB:2Y7L,
ECO:0000244|PDB:2Y7M,
ECO:0000244|PDB:2Y7N,
ECO:0000269|PubMed:21896717}.
DISULFID 96 112 {ECO:0000244|PDB:2Y7L,
ECO:0000244|PDB:2Y7M,
ECO:0000244|PDB:2Y7N,
ECO:0000269|PubMed:21896717}.
DISULFID 205 297 {ECO:0000244|PDB:2Y7L,
ECO:0000244|PDB:2Y7M,
ECO:0000244|PDB:2Y7N,
ECO:0000269|PubMed:21896717}.
DISULFID 226 255 {ECO:0000244|PDB:2Y7L,
ECO:0000244|PDB:2Y7M,
ECO:0000244|PDB:2Y7N,
ECO:0000269|PubMed:21896717}.
VARIANT 6 11 LLLLLY -> ILLFIS (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 28 42 DSLTWTRSVEYVYKG -> NSLTWANAANYGYQT (in
allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 39 39 V -> A (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 49 49 T -> N (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 63 63 A -> P (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 71 71 M -> L (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 80 80 S -> T (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 122 124 DKA -> ARV (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 132 133 IT -> FS (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 146 146 T -> A (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 161 161 M -> T (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 166 190 KISTTVDFDASPVSPSGYITSSRII -> EISTSVDFQASP
ISSSGYIASARVV (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 196 196 A -> L (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 202 202 S -> V (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 218 218 T -> A (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 220 220 Q -> N (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 229 229 I -> V (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 250 250 T -> S (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 256 265 SSSGIIVEYE -> TSTSITVEFQ (in allele ALS9-
2). {ECO:0000269|PubMed:14523127}.
VARIANT 281 286 SENVEQ -> AENIDK (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 298 298 K -> E (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 312 312 W -> T (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 322 322 N -> D (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 325 325 I -> V (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 331 331 K -> R (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 335 335 A -> D (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 348 348 T -> S (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 357 357 V -> I (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 371 374 IGIS -> VGVT (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 380 380 F -> L (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 382 382 A -> G (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 400 400 T -> A (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 404 404 T -> N (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 410 410 V -> I (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 417 417 S -> T (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 423 423 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 429 470 QIPSPDPTTTITEFWSESFASTTTVTNPPDGTNSVIIKEPY
N -> ELPSPA (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 453 453 V -> I (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 489 489 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 501 501 V -> I (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 525 525 V -> I (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 561 561 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 577 577 Y -> H (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 607 607 V -> F (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 609 609 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 633 633 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 645 645 V -> I (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 669 669 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 679 679 V -> I (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 682 682 K -> M (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 685 685 Y -> F (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 712 712 T -> R (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 718 718 K -> M (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 753 753 V -> I (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 781 781 P -> L (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 789 932 Missing (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 789 789 V -> I (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 813 813 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 820 820 T -> R (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 826 826 K -> M (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 849 849 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 882 882 T -> S (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 885 885 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 921 921 I -> V (in allele ALS9-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 944 944 T -> N (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 948 948 S -> Y (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 993 993 V -> I (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1029 1029 V -> I (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1045 1045 Y -> H (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1065 1065 V -> I (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1077 1077 I -> V (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1081 1081 Y -> H (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1108 1134 KTFYSSEAQSSLEIDSSNTFMTSISVS -> TIFHSSEPHY
SSDFDSSDSFVTLISVT (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1149 1149 A -> T (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1155 1164 ISSYSLSTSF -> LSSYTWSSGL (in allele ALS9-
2). {ECO:0000269|PubMed:14523127}.
VARIANT 1170 1170 L -> F (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1180 1183 SSPS -> NLPT (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1189 1227 MYSSVTSAVTSIDNDREVPTSTTTYLHSKLYSESISTVI
-> VYSSTASAVASTDGDSVVPSSTNLVTQSISSSETYCID
ISGCSSVRQSSSVMVTPSNSGRIIISDSAYLTTTYSHSESD
LESIVTVV (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1238 1238 L -> S (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1242 1242 N -> D (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1248 1257 STVSEESLHY -> TTVSDDNSYS (in allele ALS9-
2). {ECO:0000269|PubMed:14523127}.
VARIANT 1301 1301 M -> V (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1308 1308 S -> N (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1429 1429 M -> L (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1488 1488 T -> TTAESIATKTIVSETPVTKVLSSKSLAANASPSEPT
SKKE (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1799 1799 D -> G (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1859 1859 K -> N (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1861 1861 V -> I (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1875 1875 L -> H (in allele ALS9-2).
{ECO:0000269|PubMed:14523127}.
CONFLICT 537 537 I -> V (in Ref. 1; AAP34370/AAP34371).
{ECO:0000305}.
CONFLICT 705 705 I -> V (in Ref. 1; AAP34370/AAP34371).
{ECO:0000305}.
CONFLICT 741 741 I -> V (in Ref. 1; AAP34370/AAP34371).
{ECO:0000305}.
CONFLICT 1886 1886 F -> L (in Ref. 1; AAP34370/AAP34371).
{ECO:0000305}.
STRAND 24 32 {ECO:0000244|PDB:2Y7L}.
STRAND 36 38 {ECO:0000244|PDB:2Y7L}.
STRAND 48 57 {ECO:0000244|PDB:2Y7L}.
TURN 58 60 {ECO:0000244|PDB:2Y7L}.
STRAND 66 72 {ECO:0000244|PDB:2Y7L}.
STRAND 74 80 {ECO:0000244|PDB:2Y7L}.
STRAND 82 88 {ECO:0000244|PDB:2Y7L}.
STRAND 91 99 {ECO:0000244|PDB:2Y7L}.
TURN 102 104 {ECO:0000244|PDB:2Y7L}.
STRAND 106 114 {ECO:0000244|PDB:2Y7L}.
STRAND 122 134 {ECO:0000244|PDB:2Y7L}.
STRAND 139 141 {ECO:0000244|PDB:2Y7L}.
HELIX 142 147 {ECO:0000244|PDB:2Y7L}.
STRAND 153 162 {ECO:0000244|PDB:2Y7L}.
STRAND 165 173 {ECO:0000244|PDB:2Y7L}.
STRAND 184 190 {ECO:0000244|PDB:2Y7L}.
HELIX 191 193 {ECO:0000244|PDB:2Y7L}.
STRAND 195 201 {ECO:0000244|PDB:2Y7L}.
STRAND 209 218 {ECO:0000244|PDB:2Y7L}.
STRAND 222 237 {ECO:0000244|PDB:2Y7L}.
STRAND 251 255 {ECO:0000244|PDB:2Y7L}.
STRAND 257 264 {ECO:0000244|PDB:2Y7L}.
STRAND 271 283 {ECO:0000244|PDB:2Y7L}.
STRAND 286 291 {ECO:0000244|PDB:2Y7L}.
STRAND 294 297 {ECO:0000244|PDB:2Y7L}.
STRAND 302 304 {ECO:0000244|PDB:2Y7L}.
STRAND 307 312 {ECO:0000244|PDB:2Y7L}.
STRAND 320 326 {ECO:0000244|PDB:2Y7L}.
SEQUENCE 1890 AA; 201290 MW; 3E394E9A31CFF950 CRC64;
MLPQFLLLLL YLTVSTAKTI TGVFNSFDSL TWTRSVEYVY KGPETPTWTA VLGWSLNSTT
ADAGDTFTLI MPCVFKFITS QTSVDLTADG VSYATCDFNA GEEFTTFSSL SCTVNSVSVS
YDKASGTVKL PITFNVGGTG SSVDLTDSKC FTAGKNTVTF MDGDTKISTT VDFDASPVSP
SGYITSSRII PSLNKASSLF VSPQCENGYT SGIMGFVTSQ GATIDCSNIN IGISKGLNDW
NFPVSSESFT YTKTCSSSGI IVEYENVPAG YRPFVDAYIS SENVEQYTLT YANEYTCKNG
NTVVDPFTLT WWGYKNSEAD SNGDIIVVTT KTVTASTTAV TTLPFNPTVD KTETIEVLQP
IPTTTITTSY IGISTSYETF TATIGGTATV IVDTPYHITT TVTTFWTGSV TTTTTYSNPT
GSIDTVIVQI PSPDPTTTIT EFWSESFAST TTVTNPPDGT NSVIIKEPYN PTVTTTEFWS
ESFASTTTIT NPPDGTNSVI VKEPYNPTVT TTEFWSESFA STTTVTNPPD GTNSVIIKEP
YNPTVTTTEF WSESFASTTT ITNPPDGTNS VIVKEPYNPT VTTTEFWSES FASTTTVTNP
PDGTNSVIIK EPYNPTVTTT EFWSESFAST TTITNPPDGT NSVIVKEPYN PTVTTTEFWS
ESFASTTTIT NPPDGTNSVI VKEPYNPTVT TTEFWSESFA STTTITNPPD GTNSVIVKEP
YNPTVTTTEF WSESFASTTT ITNPPDGTNS VIVKEPYNPT VTTTEFWSES FASTTTVTNP
PDGTNSVIVK EPYNPTVTTT EFWSESFAST TTITNPPDGT NSVIVKEPYN PTVTTTEFWS
ESFASTTTIT NPPDGTNSVI VKEPYNPTVT TTEFWSESFA STTTITNPPD GTNSVIIKEP
YNPTVTTTEF WSESFASTTT ITNPPDGTNS VIIKEPYNPT VTTTEFWSES FASTTTVTNP
PDGTNSVIIK EPYNPTVTTT EFWSESFAST TTVTNPPDGT NSVIIKEPYN PTVTTTEFWS
ESFASTTTVT NPPDGTNSVI VKEPYNPTVT TTEFWSESFA STTTVTNPPD GTNSVIIKEP
YNPTVTTTEF WSESFASTTP SVSSFESKTF YSSEAQSSLE IDSSNTFMTS ISVSTASSYD
ESSTIVSSAF PTLHISSYSL STSFVPPVTL PRYVNTTISS SPSFESSSMY SSVTSAVTSI
DNDREVPTST TTYLHSKLYS ESISTVIQTK SSDWSLSLGN SNKPESASTV SEESLHYLST
PGPSSSEYSI SFTSEKEGHV SSYVPRVSYT SSVKVSISST MSSENGMSAT HTFGISTNTI
PSSTETSIKS ATVTTPVSES TNTGMSIFMS TTTESKTTDI TTETSVSGEV NLGSATVKVS
SSEFISKGTV TRIMPTELTN SESTFTASPS FVLTSTESSV IETPATIEMS SRSSSYSVPL
SKLRSEGETT RVIPTSSTAT GSTVIGSPSS VSTSNESIIT GSSSFVSTTA ETISTRSIVT
ESIVAGSPSL VLTTTVLDTT ETTITETSIV GESSSRSLTF KASSLSKGEI TGTVTPEMSV
STSKATTGTT SEVSIKESLT TKVPTFTSTT IKPETSETQH SESRTTQIPY SETKGSQLST
ANSQVSQTGS SKSSIFESAI SKDESTFVSA TVKSITTPAV TQYQTSLPNP AVSVSEESGK
KSSIIESQTE NSATQHSIYF DSIETSTLSN TLANTLVSGA MKNSETTSEL TTSDKAIGFS
TTTETSIPGA TNSALSPSVD SGKSSMLGWS GGIVSTVSTS TRLEDSTATS SSITAANQDS
LNPSTVSKYP HGSETIDNGS NGSSHSSSAL ASTISASHSI KFSAHQTTLS QSLISSSTKT
VIASTYDGSG SVIKLHSWFY GLVTIFFLFI


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