ALS6_CANAL
ID ALS6_CANAL Reviewed; 1366 AA.
AC Q5A2Z7; A0A1D8PKF9; B1PKX7; Q873Q8;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Agglutinin-like protein 6;
DE AltName: Full=Adhesin 6;
DE Flags: Precursor;
GN Name=ALS6; Synonyms=ALS97; OrderedLocusNames=CAALFM_C306190CA;
GN ORFNames=CaO19.7414;
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].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17625934; DOI=10.1016/j.fgb.2007.05.004;
RA Zhao X., Oh S.H., Jajko R., Diekema D.J., Pfaller M.A., Pujol C.,
RA Soll D.R., Hoyer L.L.;
RT "Analysis of ALS5 and ALS6 allelic variability in a geographically diverse
RT collection of Candida albicans isolates.";
RL Fungal Genet. Biol. 44:1298-1309(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=SC5314 / ATCC MYA-2876;
RA Zhao X., Oh S.-H., Hoyer L.L.;
RT "Candida albicans SC5314 ALS6 second allele.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10417199; DOI=10.1128/iai.67.8.4251-4255.1999;
RA Hoyer L.L., Clevenger J., Hecht J.E., Ehrhart E.J., Poulet F.M.;
RT "Detection of Als proteins on the cell wall of Candida albicans in murine
RT tissues.";
RL Infect. Immun. 67:4251-4255(1999).
RN [7]
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 [8]
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 [9]
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 [10]
RP INDUCTION.
RX PubMed=17164403; DOI=10.1074/mcp.m600210-mcp200;
RA Fernandez-Arenas E., Cabezon V., Bermejo C., Arroyo J., Nombela C.,
RA Diez-Orejas R., Gil C.;
RT "Integrated proteomics and genomics strategies bring new insight into
RT Candida albicans response upon macrophage interaction.";
RL Mol. Cell. Proteomics 6:460-478(2007).
RN [11]
RP INDUCTION.
RX PubMed=20398368; DOI=10.1186/1471-2180-10-114;
RA Nailis H., Kucharikova S., Ricicova M., Van Dijck P., Deforce D., Nelis H.,
RA Coenye T.;
RT "Real-time PCR expression profiling of genes encoding potential virulence
RT factors in Candida albicans biofilms: identification of model-dependent and
RT -independent gene expression.";
RL BMC Microbiol. 10:114-114(2010).
RN [12]
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).
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:15128742, ECO:0000269|PubMed:17510860,
CC ECO:0000269|PubMed:22321066}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10417199};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10417199}. Secreted, cell
CC wall {ECO:0000269|PubMed:10417199}. Note=Identified as covalently-
CC linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall
CC layer.
CC -!- INDUCTION: Highly expressed in biofilms and during candidiasis
CC infection dissemination. Induced upon interaction with host
CC macrophages. {ECO:0000269|PubMed:17164403,
CC ECO:0000269|PubMed:20398368}.
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 -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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DR EMBL; AY225310; AAO72081.1; -; Genomic_DNA.
DR EMBL; EU444081; ACA42971.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28626.1; -; Genomic_DNA.
DR RefSeq; XP_716079.2; XM_710986.2.
DR AlphaFoldDB; Q5A2Z7; -.
DR SMR; Q5A2Z7; -.
DR GeneID; 3642266; -.
DR KEGG; cal:CAALFM_C306190CA; -.
DR eggNOG; ENOG502RGCG; Eukaryota.
DR HOGENOM; CLU_257941_0_0_1; -.
DR InParanoid; Q5A2Z7; -.
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; 6.
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..1345
FT /note="Agglutinin-like protein 6"
FT /id="PRO_0000420224"
FT PROPEP 1346..1366
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420225"
FT REPEAT 368..399
FT /note="ALS 1"
FT REPEAT 404..435
FT /note="ALS 2"
FT REPEAT 441..472
FT /note="ALS 3"
FT REPEAT 477..508
FT /note="ALS 4"
FT REPEAT 513..544
FT /note="ALS 5"
FT REPEAT 549..580
FT /note="ALS 6"
FT REGION 449..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1345
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..151
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 97..113
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 206..301
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 228..257
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT VARIANT 70
FT /note="L -> S (in allele ALS6-2)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 856
FT /note="S -> L (in allele ALS6-2)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 907
FT /note="I -> V (in allele ALS6-2)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 1230
FT /note="D -> G (in allele ALS6-2)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 1238
FT /note="N -> S (in allele ALS6-2)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 1302
FT /note="M -> T (in allele ALS6-2)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 1310
FT /note="I -> M (in allele ALS6-2)"
FT /evidence="ECO:0000269|Ref.2"
FT CONFLICT 755
FT /note="S -> R (in Ref. 1; AAO72081)"
FT /evidence="ECO:0000305"
FT CONFLICT 763
FT /note="S -> F (in Ref. 1; AAO72081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1366 AA; 142767 MW; FC6F3A3A1D9E91C6 CRC64;
MKTVILLHLF FYCTIAMAKT ISGVFTSFNS LTYTNTGNYP YGGPGYPTWT AVLGWSLDGT
LASPGDTFTL VMPCVFKFIT TQTSVDLTAN GVKYATCTFH AGEDFTTFSS MSCVVNNGLS
SNIRAFGTVR LPISFNVGGT GSSVNIQDSK CFTAGTNTVT FTDGDHKIST TVNFPKTPQS
SSSLVYFARV IPSLDKLSSL VVASQCTAGY ASGVLGFSAT KDDVTIDCST IHVGITNGLN
SWNMPVSSES FSYTKTCTPN SFIITYENVP AGYRPFIDSY VKKSATATNG FNLNYTNIYN
CMDGKKGNDP LIYFWTSYTN SDAGSNGAAV VVTTRTVTDS TTAITTLPFD PTVDKTKTIE
VIEPIPTTTI TTSYVGISTS LSTKTATIGG TATVVVDVPY HTTTTITSIW TGSATTSSTY
TNPTDSIDTV VVQVPSPNPT VTTTQFWSGS VPTTETVTTG PQGTDSVIIK EPHNPTVTTT
EFWSESFATT ETVTNGPEGT DSVIVREPHN PTVTTTEFWS ESFATTETVT NGPEGTDSVI
VREPHNPTVT TTEFWSESFA TTETITTGPL GTDSIVIHDP LEESSSSTAI ESSDSNISSS
AQESSSSVEQ SLTSADETSS IVELSSSSDI PSSSIGLTSS ESSTVSSYDS YSSSTSESSI
ASSYDSYWSS SIESSTLSSS DRYSSSISDT TSFWDSSSSD LESTSITWSS SIDAQSSHLV
QSVSNSISTS QELSSSSSEE SSTSATDALV SSDASSILSS DTSSYYPSST ISPSDDFPHT
IAGESDSQSI SFITSTVEIS SDSVSLTSDP ASSFDSSSSL NSDSSSSPSS DQSDILTSSS
FSTLVVPSFS LSSSSSLSLT YPHYVNSTTY HASESESSSV ASPSMASESA NDDTHTLSES
TDTTSSIGTD SSTVTFCRRD NGDGCIVTGM PSSSIDSEQT SDVTTTSSFV ASSTPTSAEQ
SITDNPNIDS SQTSASSSTK LSVFVSDTVV NSISLSETST LSSDDSTSSD TSISSTTNSD
TGNINAGSSH TSTASIKESS IQKTGVMLSS SYLSTKLSST SDITTELITT ELTTTELTTI
EDNEPNTFTS TPSSHSEIFS SDNSVLSKQV DGESTVEIPP VTDTTTVSSV SVHSIEASTA
TLGENSFSKV ASAPVNTETS LRSTSSSSNH ATESSGTVKS EASAEAIPSP PTSTDNRLSY
STEEAKGSTY ANSGSTNNLM TESQVAAPTD STSVLTANPV VTSTFDDKSS AAVNQPSKTK
SIEESIGSLD SVNETNNGFI ATLSQSEAPN SLIHSESIST TMAKTTDASI NGDSAASNSQ
PTTLIQQVAT SSYNQPLITT YAGSSSATKH PSWLLKFISV ALFFFL
