ALS4_CANAX
ID ALS4_CANAX Reviewed; 875 AA.
AC O74660; O74661; Q9URP8; Q9URP9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Agglutinin-like protein 4;
DE AltName: Full=Adhesin 4;
DE Flags: Precursor; Fragments;
GN Name=ALS4;
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 VARIANTS.
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:A0A1D8PQB9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:A0A1D8PQB9}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:A0A1D8PQB9}. Note=Identified as covalently-
CC linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall
CC layer. Covers the surface of yeast-form cells.
CC {ECO:0000250|UniProtKB:A0A1D8PQB9}.
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:A0A1D8PQB9}.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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DR EMBL; AH006929; AAC64239.1; -; Genomic_DNA.
DR EMBL; AH006929; AAC64240.1; -; Genomic_DNA.
DR EMBL; AH006930; AAC64241.1; -; Genomic_DNA.
DR EMBL; AH006930; AAC64242.1; -; Genomic_DNA.
DR AlphaFoldDB; O74660; -.
DR SMR; O74660; -.
DR VEuPathDB; FungiDB:C6_03700W_A; -.
DR VEuPathDB; FungiDB:C6_04130C_A; -.
DR VEuPathDB; FungiDB:CAWG_04966; -.
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..852
FT /note="Agglutinin-like protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000020694"
FT PROPEP 853..875
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439165"
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..502
FT /note="ALS 4"
FT REGION 546..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 852
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 811
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..298
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 227..256
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT VARIANT 125
FT /note="I -> M (in allele ALS4-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 198
FT /note="N -> S (in allele ALS4-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 265
FT /note="F -> Y (in allele ALS4-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 280
FT /note="I -> V (in allele ALS4-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 697
FT /note="I -> II (in allele ALS4-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT VARIANT 726..729
FT /note="STSL -> GTSS (in allele ALS4-2)"
FT /evidence="ECO:0000269|PubMed:9765564"
FT NON_CONS 469..470
SQ SEQUENCE 875 AA; 90179 MW; 23FAFFA0F47285FC CRC64;
MLLQFLLLSL CVSVATAKVI TGVFNSFNSL TWANAASYPY RGPATPTWTA VIGWSLDGAT
ASAGDTFTLD MPCVFKFITD QTSIDLVADG RTYATCNLNS AEEFTTFSSV SCTVTTTMTA
DTKAIGTVTL PFSFSVGGSG SDVDLANSQC FTAGINTVTF NDGDTSISTT VDFEKSTVAS
SDRILLSRIL PSLSQAVNLF LPQECANGYT SGTMGFSTAG TGATIDCSTV HVGISNGLND
WNYPISSESF SYTKTCTSTS VLVTFQNVPA GYRPFVDAYI SATRVSSYTM QYTNIYACVG
AASVDDSFTH TWRGYSNSQA GSNGITIVVT TRTVTDSTTA VTTLPFNSDT DKTKTIEILQ
PIPTTTITTS YVGVTTSYST KTAPIGETAT VIVDVPYHTT TTVTSEWTGT ITTTTTRTNP
TDSIDTVVVQ VPSPNPTVTT TEYWSQSYAT TTTVTAPPGG TDSVIIREPP NPTVTTTEYW
SQSYATTLTI TAPPGGTNSV IIRVHSSTND ESSESTFSTL SVPSFSGSIS IVSTVSRPHY
VNSTVTHLPS SSSKPVDIPS SDVVTSTNDN SLTSLTGSEN GKTSVAISTT FCDDENGCQT
SIPQGSVVRT TATTTATTTT IIGDNNGSGK SKSGELSSTG SVTTNTATPD VPSTKVPSNP
GAPGTGVPPP LAPSTETQTT NNVPGSPNIP ATGTTDIRES TTVSHTVTGN GNTGVPMNPN
PALTTSTSLT GATNSATNPS HETGVNTGSG GSTNIVTPPS SATATVVIPG TDNGATTKGQ
DTAGGGNSNG STATTNIQGG NNEPGNQPGT NTTGEPVGTT DTQSVESISQ PTTLSQQTTS
SLISTPLAST FDGSGSIVQH SAWLYVLLTA ISIFF
