ALS2_CANAX
ID ALS2_CANAX Reviewed; 874 AA.
AC Q9URQ0; A0A1D8PQE1; O74657; O74658; O74659; Q59QW1;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Agglutinin-like protein 2;
DE AltName: Full=Adhesin 2;
DE Flags: Precursor; Fragments;
GN Name=ALS2;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS, AND SUBCELLULAR LOCATION.
RC STRAIN=1161;
RX PubMed=9765564; DOI=10.1128/jb.180.20.5334-5343.1998;
RA Hoyer L.L., Payne T.L., Hecht J.E.;
RT "Identification of Candida albicans ALS2 and ALS4 and localization of als
RT proteins to the fungal cell surface.";
RL J. Bacteriol. 180:5334-5343(1998).
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:0000250|UniProtKB:P0CU38}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:9765564}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:P0CU38}. Note=Identified as covalently-linked
CC GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer.
CC {ECO:0000250|UniProtKB:P0CU38}.
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:0000250|UniProtKB:P0CU38}.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000250|UniProtKB:P0CU38}.
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:9765564}.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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DR EMBL; AH006927; AAC64235.1; -; Genomic_DNA.
DR EMBL; AH006927; AAC64236.1; -; Genomic_DNA.
DR EMBL; AH006928; AAC64237.1; -; Genomic_DNA.
DR EMBL; AH006928; AAC64238.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9URQ0; -.
DR SMR; Q9URQ0; -.
DR VEuPathDB; FungiDB:C6_03700W_A; -.
DR VEuPathDB; FungiDB:C6_04380W_A; -.
DR VEuPathDB; FungiDB:CAWG_04941; -.
DR VEuPathDB; FungiDB:CAWG_04967; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 2.
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 3: Inferred from homology;
KW Cell adhesion; Cell membrane; Cell wall; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..851
FT /note="Agglutinin-like protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5004334322"
FT PROPEP 852..874
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439164"
FT REPEAT 364..395
FT /note="ALS 1"
FT REPEAT 400..431
FT /note="ALS 2"
FT REPEAT 437..468
FT /note="ALS 3"
FT REPEAT 473..501
FT /note="ALS 4"
FT REGION 545..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 851
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 810
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..297
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 227..256
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT VARIANT 183
FT /note="Y -> F (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 412
FT /note="T -> A (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 438
FT /note="T -> S (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 470
FT /note="N -> S (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 501..504
FT /note="IRVH -> VRFR (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 530
FT /note="V -> I (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 533
FT /note="I -> T (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 649..651
FT /note="NVP -> GGS (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 661
FT /note="A -> E (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 663
FT /note="G -> S (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 687
FT /note="N -> D (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 726
FT /note="G -> S (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 729
FT /note="L -> S (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 785
FT /note="G -> GG (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 796
FT /note="T -> I (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 808
FT /note="G -> S (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 820
FT /note="G -> D (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 830
FT /note="Q -> P (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 859
FT /note="H -> Y (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 861
FT /note="G -> A (in allele ALS2-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT NON_CONS 468..469
SQ SEQUENCE 874 AA; 90770 MW; 9B9F7A3616658843 CRC64;
MLLQFLLLSL CVSVATAKVI TGVFNSFDSL TWTRAGNYAY KGPNRPTWNA VLGWSLDGTS
ANPGDTFTLN MPCVFKFITD QTSVDLTAEG VKYATCQFYS GEEFTTFSSL KCTVSNTLTS
SIKALGTVTL PISFNVGGTG SSVDLESSQC FKAGTNTVTF NDGDKKISID VDFEKTNEDA
SGYFIASRLI PSINKVSITY VAPQCANGYT SGAMGFIVLT GDTTIDCSNV HVGITKGLND
WNFPVSSDSL SYNKTCSSTG ISITYENVPA GYRPFFDVYT SVSGQNRQLR YTNDYACVGS
SLQSKPFNLR LRGYNNSEAN SNGFVIVATT RTVTDSTTAV TTLPFNPSVD KTKTIEILQP
IPTTTITTSY VGVTTSYSTK TAPIGETATV IVDVPYHTTT TVTSEWTGTI TTTTTRTNPT
DSIDTVVVQV PSPNPTVTTT EYWSQSYATT TTVTAPPGGT DSVIIREPPN PTVTTTEYWS
QSYATTLTIT APPGGTNSVI IRVHSSTNDE SSESTFSTLS VPSFSGSISV VSIISRPHYV
NSTVTHLPSS SSKPVDIPSS DAVTSTNDNS LTSLTGSENG KTSVAISTTF CDDENGCQTS
IPQGSVVRTT ATTTATTTTI IGDNNGSGKS KSGELSPTGS VTTNTATPNV PSTKVPSNPG
APGTGVPPPL APSTETQTTN NVPGSPNIPA TGTTDIIRES TTVSHTVTGN GNTGVPMNPN
PALTTGTSLT GATNSATNPS HETGVNTGSG GSTNIVTPPS SATATVVIPG TDNGATTKGQ
DTAGGNSNGS TATTNTQGGN NEPGNQPGTN TTGEPVGTTG TQSVELISQQ TTLSQQTTSS
LISTPLASTF DGSGSIVQHS GWLYVLLTAI SIFF
