ALS4_CANAL
ID ALS4_CANAL Reviewed; 2100 AA.
AC A0A1D8PQB9; Q9HFX4;
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 4;
DE AltName: Full=Adhesin 4;
DE Flags: Precursor;
GN Name=ALS4; Synonyms=ALS12; OrderedLocusNames=CAALFM_C604130CA;
GN ORFNames=orf19.4555, orf19.4556;
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 [MRNA], AND VARIANTS.
RC STRAIN=SC5314 / ATCC MYA-2876;
RA Chen X., Chen J.-Y.;
RT "ALS4 (agglutinin-like sequence) of Candida albicans.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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 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=15870470; DOI=10.1099/mic.0.27763-0;
RA Zhao X., Oh S.H., Yeater K.M., Hoyer L.L.;
RT "Analysis of the Candida albicans Als2p and Als4p adhesins suggests the
RT potential for compensatory function within the Als family.";
RL Microbiology 151:1619-1630(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22106872; DOI=10.1111/j.1574-695x.2011.00914.x;
RA Coleman D.A., Oh S.H., Manfra-Maretta S.L., Hoyer L.L.;
RT "A monoclonal antibody specific for Candida albicans Als4 demonstrates
RT overlapping localization of Als family proteins on the fungal cell surface
RT and highlights differences between Als localization in vitro and in vivo.";
RL FEMS Immunol. Med. Microbiol. 64:321-333(2012).
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).
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.
CC {ECO:0000269|PubMed:22321066, ECO:0000269|PubMed:22429754}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:12845604}. Secreted, cell wall
CC {ECO:0000269|PubMed:22106872}. Note=Identified as covalently-linked
CC GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer
CC (Probable). Covers the surface of yeast-form cells (PubMed:22106872).
CC {ECO:0000269|PubMed:22106872, 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:0000305|PubMed:15128742}.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000305}.
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; AF272027; AAG25054.1; -; mRNA.
DR EMBL; CP017628; AOW30333.1; -; Genomic_DNA.
DR RefSeq; XP_710425.2; XM_705333.2.
DR AlphaFoldDB; A0A1D8PQB9; -.
DR SMR; A0A1D8PQB9; -.
DR STRING; 237561.A0A1D8PQB9; -.
DR GeneID; 3647972; -.
DR KEGG; cal:CAALFM_C604130CA; -.
DR CGD; CAL0000174423; ALS4.
DR VEuPathDB; FungiDB:C6_04130C_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; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD.
DR GO; GO:0043710; P:cell adhesion involved in multi-species biofilm formation; IBA:GO_Central.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IDA:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
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; 38.
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 Cell adhesion; Cell membrane; Cell wall; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Repeat; Secreted;
KW Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..2078
FT /note="Agglutinin-like protein 4"
FT /id="PRO_0000439166"
FT PROPEP 2079..2100
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439167"
FT REPEAT 365..396
FT /note="ALS 1"
FT REPEAT 401..432
FT /note="ALS 2"
FT REPEAT 438..469
FT /note="ALS 3"
FT REPEAT 474..505
FT /note="ALS 4"
FT REPEAT 510..541
FT /note="ALS 5"
FT REPEAT 546..577
FT /note="ALS 6"
FT REPEAT 582..613
FT /note="ALS 7"
FT REPEAT 618..649
FT /note="ALS 8"
FT REPEAT 654..685
FT /note="ALS 9"
FT REPEAT 690..721
FT /note="ALS 10"
FT REPEAT 726..757
FT /note="ALS 11"
FT REPEAT 762..793
FT /note="ALS 12"
FT REPEAT 798..829
FT /note="ALS 13"
FT REPEAT 834..865
FT /note="ALS 14"
FT REPEAT 870..901
FT /note="ALS 15"
FT REPEAT 906..937
FT /note="ALS 16"
FT REPEAT 942..973
FT /note="ALS 17"
FT REPEAT 978..1009
FT /note="ALS 18"
FT REPEAT 1014..1045
FT /note="ALS 19"
FT REPEAT 1050..1078
FT /note="ALS 20"
FT REPEAT 1086..1117
FT /note="ALS 21"
FT REPEAT 1122..1153
FT /note="ALS 22"
FT REPEAT 1158..1189
FT /note="ALS 23"
FT REPEAT 1194..1225
FT /note="ALS 24"
FT REPEAT 1230..1261
FT /note="ALS 25"
FT REPEAT 1266..1297
FT /note="ALS 26"
FT REPEAT 1302..1333
FT /note="ALS 27"
FT REPEAT 1338..1369
FT /note="ALS 28"
FT REPEAT 1374..1405
FT /note="ALS 29"
FT REPEAT 1410..1441
FT /note="ALS 30"
FT REPEAT 1446..1477
FT /note="ALS 31"
FT REPEAT 1482..1513
FT /note="ALS 32"
FT REPEAT 1518..1549
FT /note="ALS 33"
FT REPEAT 1554..1585
FT /note="ALS 34"
FT REPEAT 1590..1621
FT /note="ALS 35"
FT REPEAT 1626..1657
FT /note="ALS 36"
FT REPEAT 1662..1693
FT /note="ALS 37"
FT REPEAT 1698..1726
FT /note="ALS 38"
FT REGION 1770..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1843..2064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1843..1884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1895..2064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2078
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1850
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2014
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2036
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 73..150
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 96..112
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 205..298
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 227..256
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT VARIANT 169
FT /note="T -> A (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 484
FT /note="Y -> F (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 520
FT /note="Y -> F (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 592
FT /note="Y -> F (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 664
FT /note="F -> Y (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 736..742
FT /note="FATTTTV -> YVTTSTI (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 751
FT /note="S -> T (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 760
FT /note="P -> Y (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 772
FT /note="F -> Y (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 852
FT /note="G -> A (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 867
FT /note="N -> S (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 888
FT /note="S -> A (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 895..1110
FT /note="Missing (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1168
FT /note="F -> Y (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1255
FT /note="T -> S (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1336..1695
FT /note="Missing (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1789
FT /note="T -> P (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1806
FT /note="K -> E (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1837
FT /note="T -> P (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1842
FT /note="T -> P (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1844
FT /note="T -> P (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1947
FT /note="V -> A (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1969
FT /note="S -> G (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 1975
FT /note="G -> R (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 2011
FT /note="Missing (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 2016
FT /note="S -> F (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 2022
FT /note="I -> T (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 2046
FT /note="D -> G (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 2053
FT /note="I -> T (in allele ALS4-2)"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 2100 AA; 220888 MW; 1AEC27572CA0E400 CRC64;
MLLQFLLLSL CVSVATAKVI TGIFDSFNSL TWTNAASYSY RGPANPTWTA VIGWSLDGAT
ASAGDTFTLD MPCVFKFITD QTSIDLVADG RTYATCNLNS AEEFTTFSSV SCTVTTTMTA
DTKAIGTVTL PFSFSVGGSG SDVDLANSQC FTAGINTVTF NDGDTSISTT VDFEKSTVAS
SDRILLSRIL PSLSQAVSLF LPQECANGYT SGTMGFSTAG TGATIDCSTV HVGISNGLND
WNYPISSESF SYTKTCTSTS VLVTYQNVPA GYRPFVDAYV SATRVSSYAM RYTNIYACVG
AASVDDSFTH TWSGYSNSQA GSNGITIVVT TRTVTDSTTA VTTLPFNSES DKTKTIEILQ
PIPTTTITTS YVGVTTSYST KTAPIGETAT VIVDVPYHTT TTVTSEWTGT ITTTTTRTNP
TDSIDTVVVQ VPSPNPTVTT TEYWSQSYAT TTTVTAPPGG TDSVIIREPP NPTVTTTEYW
SQSYATTTTV TAPPGGTDSV IIREPPNPTV TTTEYWSQSY ATTTTVTAPP GGTDSVIIRE
PPNPTVTTTE YWSQSYATTT TVTAPPGGTD SVIIREPPNP TVTTTEYWSQ SYATTTTVTA
PPGGTDSVII REPPNPTVTT TEYWSQSFAT TTTVTAPPGG TDSVIIREPP NPTVTTTEYW
SQSFATTTTV TAPPGGTDSV IIREPPNPTV TTTEYWSQSY ATTTTVTAPP GGTDSVIIRE
PPNPTVTTTE YWSQSFATTT TVTAPPGGTD SVIIREPPNP TVTTTEYWSQ SFATTTTVTA
PPGGTDSVII REPPNPTVTT TEYWSQSYAT TTTVTAPPGG TDTVIIREPP NYTVTTTEYW
SQSYATTTTV TGPPGGTDTV IIREPPNPTV TTTEYWSQSY ATTTTVTSPP GGTDIVIIRE
PPNPTVTTTE YWSQSYATTT TVTAPPGGTD SVIIREPPNP TVTTTEYWSQ SYATTTTVTA
PPGGTDSVII REPPNPTVTT TEYWSQSYAT TTTVTAPPGG TDSVIIREPP NPTVTTTEYW
SQSFATTTTV TAPPGGTDSV IIREPPNPTV TTTEYWSQSY ATTTTVTAPP GGTDTVIIRE
PPNYTVTTTE YWSQSYATTT TVTGPPGGTD TVIIREPPNP TVTTTEYWSQ SYATTTTVTS
PPGGTDIVII REPPNPTVTT TEYWSQSFAT TTTVTAPPGG TDSVIIREPP NPTVTTTEYW
SQSYATTTTV TAPPGGTDSV IIREPPNPTV TTTEYWSQSY ATTTTVTAPP GGTDTVIIRE
PPNPTVTTTE YWSQSYATTT TVTAPPGGTD SVIIREPPNP TVTTTEYWSQ SYATTTTVTA
PPGGTDTVII REPPNYTVTT TEYWSQSYAT TTTVTAPPGG TDTVIIREPP SPTVTTTEYW
SQSYATTTTV TAPPGGTATV IIKEPPNYTV TTTEYWSQSY ATTTTITAPP GGTDTVIIRE
PPNYTVTTTE YWSQSYATTT TVTAPPGGTD TVIIREPPNY TVTTTEYWSQ SYATTTTVTG
PPGGTDTVII REPPSPTVTT TEYWSQSYAT TTTVTAPPGG TATVIIREPP NYTVTTTEYW
SQSYATTTTI TAPPGGTDTV IIREPPNYTV TTTEYWSQSY ATTTTVTGPP GGTDTVIIRE
PPNYTVTTTE YWSQSYATTT TVTGPPGGTD TVIIREPPNY TVTTTEYWSQ SYATTTTVTG
PPGGTDTVII REPPNPTVTT TEYWSQSYAT TLTITAPPGG TNSVIIRVHS STNDESSEST
FSTLSVPSFS GSISIVSTVS RPHYVNSTVT HLPSSSSKPV DIPSSDVVTS TNDNSLTSLT
GSENGKTSVA ISTTFCDDEN GCQTSIPQGS VVRTTATTTA TTTTIIGDNN GSGKSKSGEL
SSTGSVTTNT ATPDVPSTKV PSNPGAPGTG VPPPLAPSTE TQTTNNVPGS PNIPATGTTD
IIRESTTVSH TVTGNGNTGV PMNPNPVLTT STSLTGATNS ATNPSHETSV NTGSGGSTNI
VTPPSSATAT VVIPGTDNGA TTKGQDTAGG GNSNGSTATT NIQGGNNEPG NQPGTNTTGE
PVGTTDTQSV ESISQPTTLS QQTTSSLIST PLASTFDGSG SIVQHSGWLY VLLTAISIFF
