ALS1_CANAX
ID ALS1_CANAX Reviewed; 1260 AA.
AC P46590;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Agglutinin-like protein 1;
DE AltName: Full=Adhesin 1;
DE Flags: Precursor;
GN Name=ALS1;
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=ATCC 11651 / B792 / 171D;
RX PubMed=7752895; DOI=10.1111/j.1365-2958.1995.tb02219.x;
RA Hoyer L.L., Scherer S., Shatzman A.R., Livi G.P.;
RT "Candida albicans ALS1: domains related to a Saccharomyces cerevisiae
RT sexual agglutinin separated by a repeating motif.";
RL Mol. Microbiol. 15:39-54(1995).
CC -!- FUNCTION: Major cell surface adhesion protein which mediates both
CC yeast-to-host tissue adherence and yeast aggregation. Acts as a
CC downstream effector of the EFG1 regulatory pathway. Required for
CC rapamycin-induced aggregation of C.albicans. Binds glycans and mediates
CC adherence to endothelial and epithelial cells, thereby playing an
CC important role in the pathogenesis of C.albicans infections.
CC {ECO:0000250|UniProtKB:Q5A8T4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5A8T4};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q5A8T4}. Secreted, cell
CC wall {ECO:0000250|UniProtKB:Q5A8T4}. Note=Identified as covalently-
CC linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall
CC layer. Covers the germ tube as well as the cell surface with the
CC exception of bud scars. {ECO:0000250|UniProtKB:Q5A8T4}.
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:Q5A8T4}.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000305}.
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:Q5A8T4}.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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DR EMBL; L25902; AAC41649.2; -; Genomic_DNA.
DR PIR; S60896; S60896.
DR AlphaFoldDB; P46590; -.
DR SMR; P46590; -.
DR VEuPathDB; FungiDB:C6_03700W_A; -.
DR VEuPathDB; FungiDB:CAWG_04941; -.
DR VEuPathDB; FungiDB:CAWG_05002; -.
DR PHI-base; PHI:198; -.
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; 12.
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..1260
FT /note="Agglutinin-like protein 1"
FT /id="PRO_0000020691"
FT REPEAT 433..468
FT /note="1-1"
FT REPEAT 469..504
FT /note="1-2"
FT REPEAT 505..540
FT /note="1-3"
FT REPEAT 541..576
FT /note="1-4"
FT REPEAT 577..612
FT /note="1-5"
FT REPEAT 613..648
FT /note="1-6"
FT REPEAT 649..684
FT /note="1-7"
FT REPEAT 685..720
FT /note="1-8"
FT REPEAT 721..756
FT /note="1-9"
FT REPEAT 757..792
FT /note="1-10"
FT REPEAT 983..1043
FT /note="2-1"
FT REPEAT 1092..1152
FT /note="2-2"
FT REGION 433..792
FT /note="10 X 36 AA tandem repeats"
FT REGION 896..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1152
FT /note="2 X 26 AA approximate repeats"
FT COMPBIAS 954..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 471
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 615
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 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 918
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1068
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..150
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 96..112
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 205..298
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 227..256
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
SQ SEQUENCE 1260 AA; 132641 MW; 763D1063A2354C24 CRC64;
MLQQFTLLFL YLSIASAKTI TGVFDSFNSL TWSNAANYAF KGPGYPTWNA VLGWSLDGTS
ANPGDTFTLN MPCVFKYTTS QTSVDLTADG VKYATCQFYS GEEFTTFSTL TCTVNDALKS
SIKAFGTVTL PIAFNVGGTG SSTDLEDSKC FTAGTNTVTF NDGDKDISID VEFEKSTVDP
SAYLYASRVM PSLNKVTTLF VAPQCENGYT SGTMGFSSSN GDVAIDCSNI HIGITKGLND
WNYPVSSESF SYTKTCTSNG IQIKYQNVPA GYRPFIDAYI SATDVNQYTL AYTNDYTCAG
SRSQSKPFTL RWTGYKNSDA GSNGIVIVAT TRTVTDSTTA VTTLPFNPSV DKTKTIEILQ
PIPTTTITTS YVGVTTSYST KTAPIGETAT VIVDVPYHTT TTVTSEWTGT ITTTTTRTNP
TDSIDTVVVQ VPSPNPTVST TEYWSQSFAT TTTVTAPPGG TDTVIIREPP NHTVTTTEYW
SQSFATTTTV TAPPGGTDSV IIREPPNPTV TTTEYWSQSF ATTTTVTAPP GGTDSVIIRE
PPNPTVTTTE YWSQSYATTT TVTAPPGGTD SVIIREPPNH TVTTTEYWSQ SYATTTTVTA
PPGGTDTVII REPPNHTVTT TEYWSQSFAT TTTVTGPPSG TDTVIIREPP NPTVTTTEYW
SQSYATTTTI TAPPGETDTV LIREPPNHTV TTTEYWSQSY ATTTTVTAPP GETDTVLIRE
PPNHTVTTTE YWSQSYATTT TVTAPPGGTD TVIIREPPNP TVTTTEYWSQ SFATTTTVTA
PPGGTDTVII YESMSSSKIS TSSNDITSII PSFSRPHYVN STTSDLSTFE SSSMNTPTSI
SSDGMLLSST TLVTESETTT ESICSDGKEC SRLSSSSGIV TNPDSNESSI VTSTVPTAST
MSDSLSSTDG ISATSSDNVS KSGVSVTTET SVTTIQTTPN PLSSSVTSLT QLSSIPSVSE
SESKVTFTSN GDNQSGTHDS QSTSTEIEIV TTSSTKVLPP VVSSNTDLTS EPTNTREQPT
TLSTTSNSIT EDITTSQPTG DNGDNTSSTN PVPTVATSTL ASASEEDNKS GSHESASTSL
KPSMGENSGL TTSTEIEATT TSPTEAPSPA VSSGTDVTTE PTDTREQPTT LSTTSKTNSE
SVATTQATNE NGGKSPSTDL TSSLTTGTSA STSANSELVT SGSVTGGAVA SASNDQSHST
SVTNSNSIVS NTPQTTLSQQ VTSSSPSTNT FIASTYDGSG SIIQHSTWLY GLITLLSLFI
