ALS5_CANAX
ID ALS5_CANAX Reviewed; 1419 AA.
AC O13368;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Agglutinin-like protein 5;
DE AltName: Full=Adhesin 5;
DE Flags: Precursor;
GN Name=ALS5; Synonyms=ALA1;
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], AND FUNCTION.
RX PubMed=9393828; DOI=10.1128/iai.65.12.5289-5294.1997;
RA Gaur N.K., Klotz S.A.;
RT "Expression, cloning, and characterization of a Candida albicans gene,
RT ALA1, that confers adherence properties upon Saccharomyces cerevisiae for
RT extracellular matrix proteins.";
RL Infect. Immun. 65:5289-5294(1997).
CC -!- FUNCTION: Cell surface adhesion protein which mediates both yeast-to-
CC host tissue adherence and yeast aggregation (PubMed:9393828). Plays an
CC important role in the pathogenesis of C.albicans infections. Forms
CC amyloid structures, essential for cell-cell association and cell-
CC substrate adhesion to polystyrene (By similarity).
CC {ECO:0000250|UniProtKB:Q5A8T7, ECO:0000269|PubMed:9393828}.
CC -!- SUBUNIT: Forms homodimers through the tandem repeats. Aggregates in
CC amyloid-like structures, with self-propagating secondary-structure
CC changes, amyloid-characteristic dye binding, and induced birefringence.
CC {ECO:0000250|UniProtKB:Q5A8T7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5A8T7};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q5A8T7}. Secreted, cell
CC wall {ECO:0000250|UniProtKB:Q5A8T7}. Note=Identified as covalently-
CC linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall
CC layer. {ECO:0000250|UniProtKB:Q5A8T7}.
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:Q5A8T7}.
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:Q5A8T7}.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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DR EMBL; AF025429; AAB88883.1; -; Genomic_DNA.
DR PIR; T30531; T30531.
DR PDB; 6RHA; X-ray; 1.60 A; A/B=156-161.
DR PDB; 6RHB; X-ray; 1.26 A; B=196-201.
DR PDB; 6RHD; X-ray; 1.20 A; B=369-374.
DR PDBsum; 6RHA; -.
DR PDBsum; 6RHB; -.
DR PDBsum; 6RHD; -.
DR AlphaFoldDB; O13368; -.
DR SMR; O13368; -.
DR VEuPathDB; FungiDB:C6_03690W_A; -.
DR VEuPathDB; FungiDB:CAWG_02930; -.
DR VEuPathDB; FungiDB:CAWG_04941; -.
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; 8.
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..1398
FT /note="Agglutinin-like protein 5"
FT /id="PRO_0000020661"
FT PROPEP 1399..1419
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420217"
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 REGION 652..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1398
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1326
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 1419 AA; 149635 MW; 249F33F688A9D5B6 CRC64;
MIQQFTLLFL YLSFATAKAI TGIFNSIDSL TWSNAGNYAF KGPGYPTWNA VLGWSLDGTS
ANPGDTFILN MPCVFKFTAS QKSVDLTADG VKYATCQFYS GEEFTTFSSL KCTVNNNLRS
SIKALGTVTL PIAFNVGGTG SSVDLEDSKC FTAGTNTVTF NDGSKKLSIA VNFEKSTVDQ
SGYLTTSRFM PSLNKIATLY VAPQCENGYT SGTMGFSTSY GDVAIDCSNV HIGISKGVND
WNHPVTSESF SYTKSCSSFG ISITYQNVPA GYRPFIDAYI SPSDNNQYQL SYKNDYTCVD
DYWQHAPFTL KWTGYKNSDA GSNGIVIVAT TRTVTDSTTA VTTLPFNPSV DKTKTIEILQ
PIPTTTITTS YVGVTTSYST KTAPIGETAT VIVDVPYHTT TTVTSEWTGT ITTTTTRTNP
TDSIDTVVVQ VPSPNPTTTT TQFWSESFTS TTTITNSLKG TDSVIVREPH NPTVTTTEFW
SESFATTETI TSKPEGTDSV IVREPHNPTV TTTEFWSESY ATTETITNGP EGTDSVIVRE
PHNPTVTTTK FWSESYATTE TITNKPEGTD SVIVKEPYNP TVTTTEFWSE SYATTETITN
GPEGTDSVIV REPHNPTVTT TEFWSESYAT TETITTGPLG TDSIVIHDPL EESSSTTAIE
SSDSNISSSA QESSSSVEQS SSIVGLSSSS DIPLSSDMPS SSSTGLTSSE SSTVSSYDSD
SSSSIESSTL SSSDRCSSSI SDTTSFWDSS SSDLESTSIT WSSSIDAQSS HLVQSVSNSI
STSQELSSSS SEESSTFATD ALVSSDASSI LSSDTSSYYP SSTISSSDDF PHTIAGESDS
LSISFITSTV EISSDSVSLT SDPASSFDSS SSLNSDSSSS PSSDQSDILT SSSFSTLVVP
SFSLSSSSSL SLTYPHYVNS TTYHASESES SSVASPSMAS ESANDDTYTL SESTDTTSSI
GTDSSTVTFC RRDNGDGCIV TGMPSSSIDS EQTSDVTTTS SFVASSTPTS AEQSITDNPN
IDSSQTSASS STKSSVSVSD TVVNSILLSE TSTLSSDDST SSDTSISSTT NSDTGNINAG
SSHTSTASIK ESSIQKTGVT LSSSYLSTKL SSTSDITIEL ITTELITTEL TTIEDNEPNT
FTSTPSSHSE IFSSDNSVLS KQVDRESTIK TSPTTDVTTV SSLSVHSTEA STATLGENSF
SNVASTPSNI ATSLRSTSSS SNHATESSGT VKSEASAEAI PSPPTSTDNR LSYSTEEAKG
ITYANSGSTN NLITESQVAA PTDSTSVLIE NPVVTSTFDD NSSAAVDQPS KTKSIEESIM
NPDSTNETNN GFIATLSQAQ VPSSSIHSEL ISTTTAKTTD ASMNGDSAAS NSQPTTLIQQ
VATSSYNQPL ITTYAGSSSA TKHPSWLLKF ISVALFFFL
