ALS9_CANAL
ID ALS9_CANAL Reviewed; 1890 AA.
AC A0A1D8PQ86; Q7ZA78; Q7ZA79;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Agglutinin-like protein 9;
DE AltName: Full=Adhesin 9;
DE Flags: Precursor;
GN Name=ALS9; Synonyms=ALS11; OrderedLocusNames=CAALFM_C603710WA;
GN ORFNames=orf19.13164, orf19.5742;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=14523127; DOI=10.1099/mic.0.26495-0;
RA Zhao X., Pujol C., Soll D.R., Hoyer L.L.;
RT "Allelic variation in the contiguous loci encoding Candida albicans ALS5,
RT ALS1 and ALS9.";
RL Microbiology 149:2947-2960(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=15128742; DOI=10.1074/jbc.m401929200;
RA Sheppard D.C., Yeaman M.R., Welch W.H., Phan Q.T., Fu Y., Ibrahim A.S.,
RA Filler S.G., Zhang M., Waring A.J., Edwards J.E. Jr.;
RT "Functional and structural diversity in the Als protein family of Candida
RT albicans.";
RL J. Biol. Chem. 279:30480-30489(2004).
RN [7]
RP FUNCTION.
RX PubMed=17510860; DOI=10.1080/13693780701299333;
RA Klotz S.A., Gaur N.K., De Armond R., Sheppard D., Khardori N.,
RA Edwards J.E. Jr., Lipke P.N., El-Azizi M.;
RT "Candida albicans Als proteins mediate aggregation with bacteria and
RT yeasts.";
RL Med. Mycol. 45:363-370(2007).
RN [8]
RP FUNCTION.
RX PubMed=17600078; DOI=10.1099/mic.0.2006/005017-0;
RA Zhao X., Oh S.H., Hoyer L.L.;
RT "Unequal contribution of ALS9 alleles to adhesion between Candida albicans
RT and human vascular endothelial cells.";
RL Microbiology 153:2342-2350(2007).
RN [9]
RP FUNCTION.
RX PubMed=22321066; DOI=10.1111/j.1574-695x.2012.00941.x;
RA Aoki W., Kitahara N., Miura N., Morisaka H., Kuroda K., Ueda M.;
RT "Profiling of adhesive properties of the agglutinin-like sequence (ALS)
RT protein family, a virulent attribute of Candida albicans.";
RL FEMS Immunol. Med. Microbiol. 65:121-124(2012).
RN [10]
RP FUNCTION.
RX PubMed=22429754; DOI=10.1111/j.1439-0507.2012.02188.x;
RA Monroy-Perez E., Sainz-Espunes T., Paniagua-Contreras G.,
RA Negrete-Abascal E., Rodriguez-Moctezuma J.R., Vaca S.;
RT "Frequency and expression of ALS and HWP1 genotypes in Candida albicans
RT strains isolated from Mexican patients suffering from vaginal candidosis.";
RL Mycoses 55:E151-E157(2012).
RN [11] {ECO:0007744|PDB:2Y7L, ECO:0007744|PDB:2Y7M, ECO:0007744|PDB:2Y7N}
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 18-328, AND DISULFIDE BONDS.
RX PubMed=21896717; DOI=10.1073/pnas.1103496108;
RA Salgado P.S., Yan R., Taylor J.D., Burchell L., Jones R., Hoyer L.L.,
RA Matthews S.J., Simpson P.J., Cota E.;
RT "Structural basis for the broad specificity to host-cell ligands by the
RT pathogenic fungus Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:15775-15779(2011).
CC -!- FUNCTION: Cell surface adhesion protein which mediates both yeast-to-
CC host tissue adherence and yeast aggregation. Plays an important role in
CC the pathogenesis of C.albicans infections (PubMed:17510860,
CC PubMed:22321066, PubMed:22429754). Allele ALS9-2 contributes to
CC endothelial cell adhesion, whereas ALS9-1 does not (PubMed:17600078).
CC {ECO:0000269|PubMed:17510860, ECO:0000269|PubMed:17600078,
CC ECO:0000269|PubMed:22321066, ECO:0000269|PubMed:22429754}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Secreted, cell wall. Note=Identified as covalently-linked GPI-modified
CC cell wall protein (GPI-CWP) in the outer cell wall layer.
CC {ECO:0000305|PubMed:12845604}.
CC -!- DOMAIN: Each ALS protein has a similar three-domain structure,
CC including a N-ter domain of 433-436 amino acids that is 55-90 percent
CC identical across the family and which mediates adherence to various
CC materials; a central domain of variable numbers of tandemly repeated
CC copies of a 36 amino acid motif; and a C-ter; domain that is relatively
CC variable in length and sequence across the family.
CC {ECO:0000269|PubMed:15128742}.
CC -!- PTM: N-glycosylated and O-glycosylated.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC {ECO:0000305|PubMed:12845604}.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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DR EMBL; AY269422; AAP34370.1; -; Genomic_DNA.
DR EMBL; AY269423; AAP34371.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30298.1; -; Genomic_DNA.
DR RefSeq; XP_718078.2; XM_712985.2.
DR PDB; 2Y7L; X-ray; 1.49 A; A=18-328.
DR PDB; 2Y7M; X-ray; 1.98 A; A=18-328.
DR PDB; 2Y7N; X-ray; 2.00 A; A=18-328.
DR PDB; 2Y7O; X-ray; 1.75 A; A=18-328.
DR PDB; 2YLH; X-ray; 1.70 A; A=18-328.
DR PDBsum; 2Y7L; -.
DR PDBsum; 2Y7M; -.
DR PDBsum; 2Y7N; -.
DR PDBsum; 2Y7O; -.
DR PDBsum; 2YLH; -.
DR AlphaFoldDB; A0A1D8PQ86; -.
DR SMR; A0A1D8PQ86; -.
DR GeneID; 3640281; -.
DR KEGG; cal:CAALFM_C603710WA; -.
DR CGD; CAL0000194750; ALS9.
DR VEuPathDB; FungiDB:C6_03710W_A; -.
DR OrthoDB; 1428896at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IDA:CGD.
DR GO; GO:0043710; P:cell adhesion involved in multi-species biofilm formation; IMP:CGD.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR Gene3D; 2.60.40.1280; -; 1.
DR Gene3D; 2.60.40.2430; -; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR008440; Agglutinin-like_ALS_rpt.
DR InterPro; IPR024672; Agglutinin-like_N.
DR InterPro; IPR043063; Agglutinin-like_N_N2.
DR InterPro; IPR033504; ALS.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR PANTHER; PTHR33793; PTHR33793; 7.
DR Pfam; PF05792; Candida_ALS; 19.
DR Pfam; PF11766; Candida_ALS_N; 1.
DR SMART; SM01056; Candida_ALS_N; 1.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Cell wall; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1867
FT /note="Agglutinin-like protein 9"
FT /id="PRO_0000439168"
FT PROPEP 1868..1890
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439169"
FT REPEAT 400..431
FT /note="ALS 1"
FT REPEAT 437..468
FT /note="ALS 2"
FT REPEAT 473..504
FT /note="ALS 3"
FT REPEAT 509..540
FT /note="ALS 4"
FT REPEAT 545..576
FT /note="ALS 5"
FT REPEAT 581..612
FT /note="ALS 6"
FT REPEAT 617..648
FT /note="ALS 7"
FT REPEAT 653..684
FT /note="ALS 8"
FT REPEAT 689..720
FT /note="ALS 9"
FT REPEAT 725..756
FT /note="ALS 10"
FT REPEAT 761..792
FT /note="ALS 11"
FT REPEAT 797..828
FT /note="ALS 12"
FT REPEAT 833..864
FT /note="ALS 13"
FT REPEAT 869..900
FT /note="ALS 14"
FT REPEAT 905..936
FT /note="ALS 15"
FT REPEAT 941..972
FT /note="ALS 16"
FT REPEAT 977..1008
FT /note="ALS 17"
FT REPEAT 1013..1044
FT /note="ALS 18"
FT REPEAT 1049..1077
FT /note="ALS 19"
FT REGION 1237..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1867
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 73..150
FT /evidence="ECO:0000269|PubMed:21896717,
FT ECO:0007744|PDB:2Y7L, ECO:0007744|PDB:2Y7M,
FT ECO:0007744|PDB:2Y7N"
FT DISULFID 96..112
FT /evidence="ECO:0000269|PubMed:21896717,
FT ECO:0007744|PDB:2Y7L, ECO:0007744|PDB:2Y7M,
FT ECO:0007744|PDB:2Y7N"
FT DISULFID 205..297
FT /evidence="ECO:0000269|PubMed:21896717,
FT ECO:0007744|PDB:2Y7L, ECO:0007744|PDB:2Y7M,
FT ECO:0007744|PDB:2Y7N"
FT DISULFID 226..255
FT /evidence="ECO:0000269|PubMed:21896717,
FT ECO:0007744|PDB:2Y7L, ECO:0007744|PDB:2Y7M,
FT ECO:0007744|PDB:2Y7N"
FT VARIANT 6..11
FT /note="LLLLLY -> ILLFIS (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 28..42
FT /note="DSLTWTRSVEYVYKG -> NSLTWANAANYGYQT (in allele ALS9-
FT 1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 39
FT /note="V -> A (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 49
FT /note="T -> N (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 63
FT /note="A -> P (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 71
FT /note="M -> L (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 80
FT /note="S -> T (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 122..124
FT /note="DKA -> ARV (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 132..133
FT /note="IT -> FS (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 146
FT /note="T -> A (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 161
FT /note="M -> T (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 166..190
FT /note="KISTTVDFDASPVSPSGYITSSRII -> EISTSVDFQASPISSSGYIASAR
FT VV (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 196
FT /note="A -> L (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 202
FT /note="S -> V (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 218
FT /note="T -> A (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 220
FT /note="Q -> N (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 229
FT /note="I -> V (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 250
FT /note="T -> S (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 256..265
FT /note="SSSGIIVEYE -> TSTSITVEFQ (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 281..286
FT /note="SENVEQ -> AENIDK (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 298
FT /note="K -> E (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 312
FT /note="W -> T (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 322
FT /note="N -> D (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 325
FT /note="I -> V (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 331
FT /note="K -> R (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 335
FT /note="A -> D (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 348
FT /note="T -> S (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 357
FT /note="V -> I (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 371..374
FT /note="IGIS -> VGVT (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 380
FT /note="F -> L (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 382
FT /note="A -> G (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 400
FT /note="T -> A (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 404
FT /note="T -> N (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 410
FT /note="V -> I (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 417
FT /note="S -> T (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 423
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 429..470
FT /note="QIPSPDPTTTITEFWSESFASTTTVTNPPDGTNSVIIKEPYN -> ELPSPA
FT (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 453
FT /note="V -> I (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 489
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 501
FT /note="V -> I (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 525
FT /note="V -> I (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 561
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 577
FT /note="Y -> H (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 607
FT /note="V -> F (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 609
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 633
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 645
FT /note="V -> I (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 669
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 679
FT /note="V -> I (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 682
FT /note="K -> M (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 685
FT /note="Y -> F (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 712
FT /note="T -> R (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 718
FT /note="K -> M (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 753
FT /note="V -> I (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 781
FT /note="P -> L (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 789..932
FT /note="Missing (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 789
FT /note="V -> I (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 813
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 820
FT /note="T -> R (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 826
FT /note="K -> M (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 849
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 882
FT /note="T -> S (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 885
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 921
FT /note="I -> V (in allele ALS9-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 944
FT /note="T -> N (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 948
FT /note="S -> Y (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 993
FT /note="V -> I (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1029
FT /note="V -> I (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1045
FT /note="Y -> H (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1065
FT /note="V -> I (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1077
FT /note="I -> V (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1081
FT /note="Y -> H (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1108..1134
FT /note="KTFYSSEAQSSLEIDSSNTFMTSISVS -> TIFHSSEPHYSSDFDSSDSFV
FT TLISVT (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1149
FT /note="A -> T (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1155..1164
FT /note="ISSYSLSTSF -> LSSYTWSSGL (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1170
FT /note="L -> F (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1180..1183
FT /note="SSPS -> NLPT (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1189..1227
FT /note="MYSSVTSAVTSIDNDREVPTSTTTYLHSKLYSESISTVI -> VYSSTASAV
FT ASTDGDSVVPSSTNLVTQSISSSETYCIDISGCSSVRQSSSVMVTPSNSGRIIISDSAY
FT LTTTYSHSESDLESIVTVV (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1238
FT /note="L -> S (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1242
FT /note="N -> D (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1248..1257
FT /note="STVSEESLHY -> TTVSDDNSYS (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1301
FT /note="M -> V (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1308
FT /note="S -> N (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1429
FT /note="M -> L (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1488
FT /note="T -> TTAESIATKTIVSETPVTKVLSSKSLAANASPSEPTSKKE (in
FT allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1799
FT /note="D -> G (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1859
FT /note="K -> N (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1861
FT /note="V -> I (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1875
FT /note="L -> H (in allele ALS9-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT CONFLICT 537
FT /note="I -> V (in Ref. 1; AAP34370/AAP34371)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="I -> V (in Ref. 1; AAP34370/AAP34371)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="I -> V (in Ref. 1; AAP34370/AAP34371)"
FT /evidence="ECO:0000305"
FT CONFLICT 1886
FT /note="F -> L (in Ref. 1; AAP34370/AAP34371)"
FT /evidence="ECO:0000305"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:2Y7L"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:2Y7L"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 122..134
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2Y7L"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:2Y7L"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 222..237
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 271..283
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:2Y7L"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:2Y7L"
SQ 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
