HYR1_CANAX
ID HYR1_CANAX Reviewed; 937 AA.
AC P46591;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Hyphally-regulated protein;
DE Flags: Precursor;
GN Name=HYR1;
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 10261 / CBS 2718 / NBRC 1061 / FMJ 1011;
RX PubMed=8808922; DOI=10.1128/jb.178.18.5353-5360.1996;
RA Bailey D.A., Feldmann P.J.F., Bovey M., Gow N.A.R., Brown A.J.P.;
RT "The Candida albicans HYR1 gene, which is activated in response to hyphal
RT development, belongs to a gene family encoding yeast cell wall proteins.";
RL J. Bacteriol. 178:5353-5360(1996).
CC -!- FUNCTION: Nonessential component of the hyphal cell wall.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}. Secreted, cell wall.
CC -!- DEVELOPMENTAL STAGE: Abundant in hyphae.
CC -!- INDUCTION: Induced specifically in response to hyphal development.
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DR EMBL; Z50123; CAA90485.1; -; Genomic_DNA.
DR PIR; S58135; S58135.
DR AlphaFoldDB; P46591; -.
DR SMR; P46591; -.
DR VEuPathDB; FungiDB:C1_13450W_A; -.
DR VEuPathDB; FungiDB:CAWG_00106; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:UniProt.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR Pfam; PF11765; Hyphal_reg_CWP; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..913
FT /note="Hyphally-regulated protein"
FT /id="PRO_0000021472"
FT PROPEP 914..937
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021473"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 610..613
FT /note="1"
FT REPEAT 666..669
FT /note="2"
FT REPEAT 680..683
FT /note="3"
FT REPEAT 690..693
FT /note="4"
FT REPEAT 698..701
FT /note="5"
FT REPEAT 738..741
FT /note="6"
FT REPEAT 750..753
FT /note="7"
FT REGION 332..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..753
FT /note="7 X 4 AA repeats of N-E-G-S"
FT COMPBIAS 567..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 913
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
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 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 913
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 937 AA; 93700 MW; 17802F121E5BA926 CRC64;
MKVVSNFIFT ILLTLNLSAA LEVVTSRIDR GGIQGFHGDV KVHSGATWAI LGTTLCSFFG
GLEVEKGASL FIKSDNGPVL ALNVALSTLV RPVINNGVIS LNSKSSTSFS NFDIGGSSFT
NNGEIYLDSS GLVKSTAYLY AREWTNNGLI VAYQNQKAAG NIAFGTAYQT ITNNGQICLR
HQDFVPATKI KGTGCVTADE DTWIKLGNTI LSVEPTHNFY LKDSKSSLIV HAVSSNQTFT
VHGFGNGNKL GLTLPLTGNR DHFRFEYYPD TGILQLRADA LPQYFKIGKG YDSKLFRIVN
SRGLKNAVTY DGPVPNNEIP AVCLIPCTNG PSAPESESDL NTPTTSSIET SSYSSAATES
SVVSESSSAV DSLTSSSLSS KSESSDVVSS TTNIESSSTA IETTMNSESS TDAGSSSISQ
SESSSTAITS SSETSSSESM SASSTTASNT SIETDSGIVS QSESSSNALS STEQSITSSP
GQSTIYVNST VTSTITSCDE NKCTEDVVTI FTTVPCSTDC VPTTGDIPMS TSYTQRTVTS
TITNCDEVSC SQDVVTYTTN VPHTTVDATT TTTTSTGGDN STGGNESGSN HGPGNGSTEG
SGNGSGAGSN EGSQSGPNNG SGSGSEGGSN NGSGSDSGSN NGSGSGSNNG SGSGSTEGSE
GGSGSNEGSQ SGSGSQPGPN EGSEGGSGSN EGSNHGSNEG SGSGSGSGSN NGSGSGSQSG
SGSGSQSGSE SGSNSGSNEG SNPGAGNGSN EGSGQGSGNG SEAGSGQGSG PNNGSGSGHN
DGSGSGSNQG SNPGAGSGSG SESGSKAGSH SGSNEGAKTD SIEGFHTESK PGFNTGAHTD
ATVTGNSVAN PVTTSTESDT TISVTVSITS YMTGFDGKPK PFTTVDVIPV PHSMPSNTTD
SSSSVPTIDT NENGSSIVTG GKSILFGLIV SMVVLFM
