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Agglutinin-like protein 5 (Adhesin 5)

 ALS5_CANAL              Reviewed;        1347 AA.
Q5A8T7; A0A1D8PQ81; Q5A8L3; Q874K9; Q874L0;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 2.
05-JUL-2017, entry version 78.
RecName: Full=Agglutinin-like protein 5;
AltName: Full=Adhesin 5;
Flags: Precursor;
Name=ALS5; Synonyms=ALA1, ALS99; OrderedLocusNames=CAALFM_C603690WA;
ORFNames=CaO19.13158, CaO19.5736;
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]
FUNCTION.
PubMed=9393828;
Gaur N.K., Klotz S.A.;
"Expression, cloning, and characterization of a Candida albicans gene,
ALA1, that confers adherence properties upon Saccharomyces cerevisiae
for extracellular matrix proteins.";
Infect. Immun. 65:5289-5294(1997).
[6]
FUNCTION.
PubMed=10531265;
Gaur N.K., Klotz S.A., Henderson R.L.;
"Overexpression of the Candida albicans ALA1 gene in Saccharomyces
cerevisiae results in aggregation following attachment of yeast cells
to extracellular matrix proteins, adherence properties similar to
those of Candida albicans.";
Infect. Immun. 67:6040-6047(1999).
[7]
FUNCTION.
PubMed=12200964; DOI=10.1080/15419060212187;
Gaur N.K., Smith R.L., Klotz S.A.;
"Candida albicans and Saccharomyces cerevisiae expressing ALA1/ALS5
adhere to accessible threonine, serine, or alanine patches.";
Cell Commun. Adhes. 9:45-57(2002).
[8]
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).
[9]
FUNCTION.
PubMed=15039323; DOI=10.1128/IAI.72.4.2029-2034.2004;
Klotz S.A., Gaur N.K., Lake D.F., Chan V., Rauceo J., Lipke P.N.;
"Degenerate peptide recognition by Candida albicans adhesins Als5p and
Als1p.";
Infect. Immun. 72:2029-2034(2004).
[10]
FUNCTION.
PubMed=15321986; DOI=10.1128/IAI.72.9.4948-4955.2004;
Rauceo J.M., Gaur N.K., Lee K.G., Edwards J.E., Klotz S.A.,
Lipke P.N.;
"Global cell surface conformational shift mediated by a Candida
albicans adhesin.";
Infect. Immun. 72:4948-4955(2004).
[11]
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).
[12]
INDUCTION.
PubMed=15731087; DOI=10.1128/IAI.73.3.1852-1855.2005;
Green C.B., Zhao X., Hoyer L.L.;
"Use of green fluorescent protein and reverse transcription-PCR to
monitor Candida albicans agglutinin-like sequence gene expression in a
murine model of disseminated candidiasis.";
Infect. Immun. 73:1852-1855(2005).
[13]
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).
[14]
SUBUNIT.
PubMed=18083824; DOI=10.1128/EC.00309-07;
Otoo H.N., Lee K.G., Qiu W., Lipke P.N.;
"Candida albicans Als adhesins have conserved amyloid-forming
sequences.";
Eukaryot. Cell 7:776-782(2008).
[15]
INDUCTION.
PubMed=20398368; DOI=10.1186/1471-2180-10-114;
Nailis H., Kucharikova S., Ricicova M., Van Dijck P., Deforce D.,
Nelis H., Coenye T.;
"Real-time PCR expression profiling of genes encoding potential
virulence factors in Candida albicans biofilms: identification of
model-dependent and -independent gene expression.";
BMC Microbiol. 10:114-114(2010).
[16]
DOMAIN, AND SUBUNIT.
PubMed=19820118; DOI=10.1128/EC.00235-09;
Frank A.T., Ramsook C.B., Otoo H.N., Tan C., Soybelman G.,
Rauceo J.M., Gaur N.K., Klotz S.A., Lipke P.N.;
"Structure and function of glycosylated tandem repeats from Candida
albicans Als adhesins.";
Eukaryot. Cell 9:405-414(2010).
[17]
SUBCELLULAR LOCATION.
PubMed=21059927; DOI=10.1073/pnas.1013893107;
Alsteens D., Garcia M.C., Lipke P.N., Dufrene Y.F.;
"Force-induced formation and propagation of adhesion nanodomains in
living fungal cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:20744-20749(2010).
[18]
FUNCTION, AND MUTAGENESIS OF VAL-326.
PubMed=21408122; DOI=10.1371/journal.pone.0017632;
Garcia M.C., Lee J.T., Ramsook C.B., Alsteens D., Dufrene Y.F.,
Lipke P.N.;
"A role for amyloid in cell aggregation and biofilm formation.";
PLoS ONE 6:E17632-E17632(2011).
[19]
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).
[20]
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).
-!- 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. Forms amyloid
structures, essential for cell-cell association and cell-substrate
adhesion to polystyrene. {ECO:0000269|PubMed:10531265,
ECO:0000269|PubMed:12200964, ECO:0000269|PubMed:15039323,
ECO:0000269|PubMed:15128742, ECO:0000269|PubMed:15321986,
ECO:0000269|PubMed:17510860, ECO:0000269|PubMed:21408122,
ECO:0000269|PubMed:22321066, ECO:0000269|PubMed:22429754,
ECO:0000269|PubMed:9393828}.
-!- SUBUNIT: Forms homodimers through the tandem repeats. Aggregates
in amyloid-like structures, with self-propagating secondary-
structure changes, amyloid-characteristic dye binding, and induced
birefringence. {ECO:0000269|PubMed:18083824,
ECO:0000269|PubMed:19820118}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
{ECO:0000305|PubMed:12845604}. Secreted, cell wall
{ECO:0000269|PubMed:21059927}. Note=Identified as covalently-
linked GPI-modified cell wall protein (GPI-CWP) in the outer cell
wall layer. {ECO:0000305|PubMed:12845604}.
-!- INDUCTION: Highly expressed in biofilms and during candidiasis
infection dissemination. {ECO:0000269|PubMed:15731087,
ECO:0000269|PubMed:20398368}.
-!- 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,
ECO:0000269|PubMed:19820118}.
-!- 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; AY227439; AAO72528.1; -; Genomic_DNA.
EMBL; AY227440; AAO72529.1; -; Genomic_DNA.
EMBL; CP017628; AOW30296.1; -; Genomic_DNA.
RefSeq; XP_718074.2; XM_712981.2.
ProteinModelPortal; Q5A8T7; -.
SMR; Q5A8T7; -.
PRIDE; Q5A8T7; -.
GeneID; 3640277; -.
KEGG; cal:CAALFM_C603690WA; -.
CGD; CAL0000191115; ALS5.
InParanoid; Q5A8T7; -.
OrthoDB; EOG092C0UQK; -.
PRO; PR:Q5A8T7; -.
Proteomes; UP000000559; Chromosome 6.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001968; F:fibronectin binding; IDA:CGD.
GO; GO:0042277; F:peptide binding; IDA:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IDA:CGD.
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:0007160; P:cell-matrix adhesion; IDA:CGD.
GO; GO:0030260; P:entry into host cell; IDA:CGD.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0016337; P:single organismal cell-cell adhesion; IDA:CGD.
Gene3D; 2.60.40.1280; -; 1.
InterPro; IPR008966; Adhesion_dom.
InterPro; IPR008440; Agglutinin-like_ALS_rpt.
InterPro; IPR024672; Agglutinin-like_N.
InterPro; IPR033504; ALS.
InterPro; IPR011252; Fibrogen-bd_dom1.
PANTHER; PTHR33793; PTHR33793; 1.
Pfam; PF05792; Candida_ALS; 6.
Pfam; PF11766; Candida_ALS_N; 1.
SMART; SM01056; Candida_ALS_N; 1.
SUPFAM; SSF49401; SSF49401; 1.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Cell wall; Complete proteome;
Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
Reference proteome; Repeat; Secreted; Signal; Virulence.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1326 Agglutinin-like protein 5.
/FTId=PRO_0000420222.
PROPEP 1327 1347 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000420223.
REPEAT 365 396 ALS 1.
REPEAT 401 432 ALS 2.
REPEAT 438 469 ALS 3.
REPEAT 474 505 ALS 4.
REPEAT 510 541 ALS 5.
REPEAT 546 577 ALS 6.
COMPBIAS 330 569 Thr-rich. {ECO:0000255|PROSITE-
ProRule:PRU00017}.
COMPBIAS 581 1182 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
LIPID 1326 1326 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 593 593 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 723 723 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 847 847 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1229 1229 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1254 1254 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 73 150 {ECO:0000250|UniProtKB:A0A1D8PQ86}.
DISULFID 96 112 {ECO:0000250|UniProtKB:A0A1D8PQ86}.
DISULFID 205 298 {ECO:0000250|UniProtKB:A0A1D8PQ86}.
DISULFID 227 256 {ECO:0000250|UniProtKB:A0A1D8PQ86}.
VARIANT 2 2 I -> L (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 311 311 K -> R (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 406 406 E -> K (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 481 481 S -> SESYATTETITTGPLGTDSVIIKEPHNPTVTTTVFW
S (in allele ALS5-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 492 492 N -> T (in allele ALS5-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 495 495 E -> L (in allele ALS5-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 502 503 VR -> IK (in allele ALS5-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 514 514 E -> K (in allele ALS5-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 526 526 V -> I (in allele ALS5-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 539 539 K -> R (in allele ALS5-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 542 542 H -> Y (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1167 1167 A -> T (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1202 1202 T -> N (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1267 1269 AQV -> SEA (in allele ALS5-1).
{ECO:0000269|PubMed:14523127}.
VARIANT 1271 1271 N -> S (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1273 1273 L -> S (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1278 1278 S -> L (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1283 1283 M -> T (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
VARIANT 1291 1291 I -> M (in allele ALS5-2).
{ECO:0000269|PubMed:14523127}.
MUTAGEN 326 326 V->N: Impairs amyloid formation and
decreases cell aggregation.
{ECO:0000269|PubMed:21408122}.
CONFLICT 538 538 I -> V (in Ref. 1; AAO72528/AAO72529).
{ECO:0000305}.
CONFLICT 841 841 T -> I (in Ref. 1; AAO72528/AAO72529).
{ECO:0000305}.
CONFLICT 911 911 M -> I (in Ref. 1; AAO72528/AAO72529).
{ECO:0000305}.
CONFLICT 975 975 S -> L (in Ref. 1; AAO72528/AAO72529).
{ECO:0000305}.
CONFLICT 1028 1028 M -> T (in Ref. 1; AAO72528/AAO72529).
{ECO:0000305}.
CONFLICT 1046 1046 T -> I (in Ref. 1; AAO72528/AAO72529).
{ECO:0000305}.
SEQUENCE 1347 AA; 141787 MW; 9AB66EDE24480F83 CRC64;
MIQQFTLLFL YLSFATAKAI TGIFNSIDSL TWSNAGNYAF KGPGYPTWNA VLGWSLDGTS
ANPGDTFILN MPCVFKFTAS QKSVDLTADG VKYATCQFYS GEEFTTFSSL KCTVNNNLRS
SIKALGTVTL PIAFNVGGTG SSVDLEDSKC FTAGTNTVTF NDGSKKLSIA VNFEKSTVDQ
SGYLTTSRFM PSLNKIATLY VAPQCENGYT SGTMGFSTSY GDVAIDCSNV HIGISKGVND
WNHPVTSESF SYTKSCSSFG ISITYQNVPA GYRPFIDAYI SPSDNNQYQL SYKNDYTCVD
DYWQHAPFTL KWTGYKNSDA GSNGIVIVAT TRTVTDSTTA VTTLPFNPSV DKTKTIEILQ
PIPTTTITTS YVGVTTSYST KTAPIGETAT VIVDVPYHTT TTVTSEWTGT ITTTTTRTNP
TDSIDTVVVQ VPLPNPTTTT TQFWSESFTS TTTITNSLKG TDSVIVREPH NPTVTTTEFW
SESYATTETI TNGPEGTDSV IVREPHNPTV TTTEFWSESY ATTETVTNKP EGTDSVIIKE
PHNPTVTTTE FWSESYATTE TITTGPLGTD SIVIHDPLEE SSSTTAIESS DSNISSSAQE
SSSSVEQSSS IVGLSSSSDI PLSSDMPSSS STGLTSSESS TVSSYDSDSS SSSELSTFSS
SESYSSSISD TTNFWDSSSS DLESTSITWS SSIDAQSSQS VQSVSNSIST SQETTSSSGE
ESNTSVTDIL VSSDASSILN SDISSYYPSS TISLSDDFPH TIAGEPDSRS SSSIASTVEI
SSDLVSLTSD PTSSFDSSSS LNSDSSSSPF SDESDISASS SFSTLVAPSF SLSSSSSLSL
TYPHYVNSTT YHASESESSS VASPSMASES ANDDTHTLSE STDTTSSIGT DSSTVTFCRR
DNGDGCIVTG MPSSSIDSEQ TSDVTTTSSF VASSTPTSAE QSITDNPNID SSQTSASSST
KSSVSVSDTV VNSISLSETS TLSSDDSTSS DTSISSTTNS DTGNINAGSS HTSTASIKES
SIQKTGVMLS SSYLSTKLSS TSDITTELIT TELITTELTT IEDNEPNTFT STPSSHSEIF
SSDNSVLSKQ VDRESTIKTS PTTDVTTVSS LSVHSTEAST ATLGENSFSN VASTPSNIAT
SLRSTSSSSN HATESSGTVK SEASAEAIPS PPTSTDNRLS YSTEEAKGIT YANSGSTNNL
ITESQVAAPT DSTSVLIENP VVTSTFDDNS SAAVDQPSKT KSIEESIMNP DSTNETNNGF
IATLSQAQVP NSLIHSESIS TTMAKTTDAS INGDSAASNS QPTTLIQQVA TSSYNQPLIT
TYAGSSSATK HPSWLLKFIS VALFFFL


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