ALS7_CANAL
ID ALS7_CANAL Reviewed; 1568 AA.
AC Q5A312; A0A1D8PKF8; Q7Z9Z1;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Agglutinin-like protein 7;
DE AltName: Full=Adhesin 7;
DE Flags: Precursor;
GN Name=ALS7; Synonyms=ALS94, ALS95, ALS96, ALS98;
GN OrderedLocusNames=CAALFM_C306320WA; ORFNames=CaO19.7400;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-471.
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 [5]
RP INDUCTION, AND FUNCTION.
RX PubMed=12952872; DOI=10.1101/gr.1024903;
RA Zhang N., Harrex A.L., Holland B.R., Fenton L.E., Cannon R.D., Schmid J.;
RT "Sixty alleles of the ALS7 open reading frame in Candida albicans: ALS7 is
RT a hypermutable contingency locus.";
RL Genome Res. 13:2005-2017(2003).
RN [6]
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 [7]
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 [8]
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 [9]
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:12952872, ECO:0000269|PubMed:15128742,
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 -!- INDUCTION: Highly expressed in biofilms and during candidiasis
CC infection dissemination. {ECO:0000269|PubMed:12952872}.
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: 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 -!- MISCELLANEOUS: ALS7 gene corresponds to a hypermutable contingency
CC locus meaning that the diversity of ALS7 proteins provide C.albicans
CC with a large and flexible repertoire of similar but non-identical
CC surface proteins which may be important not only for adhesion but also
CC for evasion of host defenses.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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DR EMBL; CP017625; AOW28639.1; -; Genomic_DNA.
DR EMBL; AY296650; AAP51179.1; -; Genomic_DNA.
DR RefSeq; XP_716065.2; XM_710972.2.
DR AlphaFoldDB; Q5A312; -.
DR SMR; Q5A312; -.
DR BioGRID; 1225328; 9.
DR GeneID; 3642234; -.
DR KEGG; cal:CAALFM_C306320WA; -.
DR CGD; CAL0000197652; ALS7.
DR VEuPathDB; FungiDB:C3_06320W_A; -.
DR eggNOG; ENOG502RGCG; Eukaryota.
DR HOGENOM; CLU_001779_0_0_1; -.
DR InParanoid; Q5A312; -.
DR OrthoDB; 1428896at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
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: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 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; 3.
DR Pfam; PF05792; Candida_ALS; 4.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1548
FT /note="Agglutinin-like protein 7"
FT /id="PRO_0000420226"
FT PROPEP 1549..1568
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420227"
FT REPEAT 403..434
FT /note="ALS 1"
FT REPEAT 441..471
FT /note="ALS 2"
FT REPEAT 476..507
FT /note="ALS 3"
FT REPEAT 512..543
FT /note="ALS 4"
FT REGION 546..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1548
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 851
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 988
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 74..151
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 97..113
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 206..299
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 228..257
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT CONFLICT 2
FT /note="K -> N (in Ref. 4; AAP51179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1568 AA; 167667 MW; E462A221F517FAF4 CRC64;
MKKLYLLYLL ASFTTVISKE VTGVFNQFNS LIWSYTYRAR YEEISTLTAK AQLEWALDGT
IASPGDTFTL VMPCVYKFMT YETSVQLTAN SIAYATCDFD AGEDTKSFSS LKCTVTDELT
EDTSVFGSVI LPIAFNVGGS GSKSTITDSK CFSSGYNTVT FFDGNNQLST TANFLPRREL
AFGLVVSQRL SMSLDTMTNF VMSTPCFMGY QSGKLGFTSN DDDFEIDCSS IHVGITNEIN
DWSMPVSSVP FDHTIRCTSR ALYIEFKTIP AGYRPFVDAI VQIPTTEPFF VKYTNEFACV
NGIYTSIPFT SFFSQPILYD EALAIGADLV RTTSTVIGSI TRTTTLPFIS RLQKTKTILV
LEPIPTTTVT TSHHGFDTWY YTKKATIGDT ATVFIDVPQH TATTLTTYWQ ESSTATTTYF
DDIDLVDTVI VKIPYPNPTI ITTQFWSGKY LTTETHKEPP LGTDSVIIKE PHNPTVTTTE
FWSESFATTE TITNNPEGTD SVIIKEPHNP TVTTTKFWSE SFATTETITT GPLGTDSIVI
HDPLEESSSS TAIESSDSNI SSSAQDSSSS VEQSFTSADE TSSIVELSSS SDIPSSSIGL
TSSESSTVSS YDSYSSSTSE SSIASSYDSY SSSSIESSTL SSSDRYSSSI SDTTSFWDSS
SSDLESTSIT WSSSIDAQSS HLVQSVSNSI STSQEISSSS SEESSTSATD ALVSSDASSI
LSSDTSSYYP SSTISPSDDF PHTIAGESDS QSFSFITSTV EISSDSVSLT SDPASSFDSS
SRLNSDSSSS PSTDQRDILT SSSFSTLIKS SESRESSSGT ILSEESSDSI PTTFSTRYWS
PSGMSSRHYT NSTETSVSDV VSSSVAGDET SESSVSVTSE SSESVTSESV ASESVTSESV
TAVSDISDLY TTSEEVSTSD SNSGMSSPIP SSEQRSSIPI MSSSDESSES RESSIGTILS
EESSDSIPTT FSTRYWSPSG MSSRHYTNST ETSVSDVVSS SVAGDETSES SVSVISESSE
SVTSESVASE SVTAVSDISD LYTTSEVVST SDSKIVPSTS VPSSEQRSSI PIMSSSDESS
ESRESSSGTI LSEENSDSIP TTFSTRYVSV SLTVGELSAL PSLPGKLSHL PSSLSETSIG
MTKSANLSPQ FFSTSVDSAL SYWASGSSSA DHQSSATCDV SESSVEGNLS AMALGMSNSD
DGLSEDTRSS SVAGKEEIEL TSTNSVGEIT LISYSSSSPT THDHGRVSKS MGAAPLSSLF
SVSVHAPLVT GLSDSDTFPS ENSNRSRSFK ESTDNTISIS RESLGNPYSS ISSPSDYDVK
SFTTSRELVS SESILPFSDV MDANDMPTSG SNLHSMVFSI SVLGEKFNAN IEKHKNTNGH
YSSMVFTYQS AGLEESDQRI AVTNTKFDQN KIDTTIDSNT FVTSLPFATT LNDQIDQAVP
IKIPASSTAG FVSDVLKPDY SKSVQAESVQ TDSTTYSEMM SSKRNKNSGF GTSSLNLKPT
ITVVTKSIDT KVNTMKEGGV SKQVSTTVTE QYDTSTYTPA SLLVSDNSGS VSKYSLWMMA
FYMLFGLF
