ALS3_CANAX
ID ALS3_CANAX Reviewed; 1119 AA.
AC O74623;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Agglutinin-like protein 3;
DE AltName: Full=3D9 antigen;
DE AltName: Full=Adhesin 3;
DE Flags: Precursor;
GN Name=ALS3; Synonyms=ALD8;
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].
RC STRAIN=1161;
RX PubMed=9644209; DOI=10.1007/s002940050359;
RA Hoyer L.L., Payne T.L., Bell M., Myers A.M., Scherer S.;
RT "Candida albicans ALS3 and insights into the nature of the ALS gene
RT family.";
RL Curr. Genet. 33:451-459(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 biofilm formation and pathogenesis of C.albicans infections.
CC Necessary for C.albicans to bind to N-cadherin on endothelial cells and
CC E-cadherin on oral epithelial cells and subsequent endocytosis by these
CC cells. During disseminated infection, mediates initial trafficking to
CC the brain and renal cortex and contributes to fungal persistence in the
CC kidneys. {ECO:0000250|UniProtKB:Q59L12}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q59L12};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q59L12}. Secreted, cell
CC wall {ECO:0000250|UniProtKB:Q59L12}. Note=Covers the surface of the
CC germ tube. {ECO:0000250|UniProtKB:Q59L12}.
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:Q59L12}.
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:0000250|UniProtKB:Q59L12}.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U87956; AAC39486.1; -; Genomic_DNA.
DR PDB; 4LEE; X-ray; 3.00 A; A/B/C/D=18-330.
DR PDBsum; 4LEE; -.
DR AlphaFoldDB; O74623; -.
DR SMR; O74623; -.
DR VEuPathDB; FungiDB:CAWG_02004; -.
DR VEuPathDB; FungiDB:CAWG_02005; -.
DR VEuPathDB; FungiDB:CR_07070C_A; -.
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; 3.
DR Pfam; PF05792; Candida_ALS; 13.
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 3D-structure; Cell adhesion; Cell membrane; Cell wall; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1098
FT /note="Agglutinin-like protein 3"
FT /id="PRO_0000020693"
FT PROPEP 1099..1119
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420220"
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..827
FT /note="ALS 13"
FT REGION 892..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1098
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 987
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1061
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..150
FT /evidence="ECO:0000250|UniProtKB:Q59L12"
FT DISULFID 96..112
FT /evidence="ECO:0000250|UniProtKB:Q59L12"
FT DISULFID 205..298
FT /evidence="ECO:0000250|UniProtKB:Q59L12"
FT DISULFID 227..256
FT /evidence="ECO:0000250|UniProtKB:Q59L12"
SQ SEQUENCE 1119 AA; 119927 MW; 6A3FB3FC8C879A71 CRC64;
MLQQYTLLLI YLSVATAKTI TGVFNSFNSL TWSNAATYNY KGPGTPTWNA VLGWSLDGTS
ASPGDTFTLN MPCVFKFTTS QTSVDLTAHG VKYATCQFQA GEEFMTFSTL TCTVSNTLTP
SIKALGTVTL PLAFNVGGTG SSVDLEDSKC FTAGTNTVTF NDGGKKISIN VDFERSNVDP
KGYLTDSRVI PSLNKVSTLF VAPQCANGYT SGTMGFANTY GDVQIDCSNI HVGITKGLND
WNYPVSSESF SYTKTCSSNG IFITYKNVPA GYRPFVDAYI SATDVNSYTL SYANEYTCAG
GYWQRAPFTL RWTGYRNSDA GSNGIVIVAT TRTVTDSTTA VTTLPFDPNR DKTKTIEILK
PIPTTTITTS YVGVTTSYST KTAPIGETAT VIVDIPYHTT TTVTSKWTGT ITSTTTHTNP
TDSIDTVIVQ VPSPNPTVTT TEYWSQSFAT TTTITGPPGN TDTVLIREPP NHTVTTTEYW
SESYTTTSTF TAPPGGTDSV IIKEPPNPTV TTTEYWSESY TTTSTFTAPP GGTDSVIIKE
PPNHTVTTTE YWSQSYTTTT TVTAPPGGTD TVLVREPPNH TVTTTEYWSQ SYTTTTTVIA
PPGGTDSVII REPPNPTVTT TEYWSQSYAT TTTITAPPGE TDTVLIREPP NHTVTTTEYW
SQSYATTTTI TAPPGETDTV LIREPPNHTV TTTEYWSQSF ATTTTVTAPP GGTDTVIIRE
PPNHTVTTTE YWSQSYATTT TITAPPGETD TVLIREPPNH TVTTTEYWSQ SYATTTTIIA
PPGETDTVLI REPPNPTVTT TEYWSQSYTT ATTVTAPPGG TDTVIIYDTM SSSEISSFSR
PHYTNHTTLW STTWVIETKT ITETSCEGDK GCSWVSVSTR IVTIPNNIET PMVTNTVDST
TTESTSQSPS GIFSESGVSV ETESSTVTTA QTNPSVPTTE SEVVFTTKGN NENGPYESPS
TNVKSSMDEN SEFTTSTAAS TSTDIENETI ATTGSVEASS PIISSSADET TTVTTTAEST
SVIEQPTNNN GGGKAPSATS SPSTTTTANN DSVITGTTST NQSQSQSQYN SDTQQTTLSQ
QMTSSLVSLH MLTTFDGSGS VIQHSTWLCG LITLLSLFI
