HYR4_CANAL
ID HYR4_CANAL Reviewed; 1225 AA.
AC Q5A849; A0A1D8PRV1;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Hyphally regulated cell wall protein 4;
DE AltName: Full=Adhesin-like protein HYR4;
DE Flags: Precursor;
GN Name=HYR4; Synonyms=HYR8, IFF7; OrderedLocusNames=CAALFM_CR00760CA;
GN ORFNames=CaO19.10789, CaO19.3279;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12734798; DOI=10.1002/yea.988;
RA Lee S.A., Wormsley S., Kamoun S., Lee A.F., Joiner K., Wong B.;
RT "An analysis of the Candida albicans genome database for soluble secreted
RT proteins using computer-based prediction algorithms.";
RL Yeast 20:595-610(2003).
RN [5]
RP INDUCTION.
RX PubMed=16950924; DOI=10.1128/ec.00252-06;
RA Srikantha T., Borneman A.R., Daniels K.J., Pujol C., Wu W.,
RA Seringhaus M.R., Gerstein M., Yi S., Snyder M., Soll D.R.;
RT "TOS9 regulates white-opaque switching in Candida albicans.";
RL Eukaryot. Cell 5:1674-1687(2006).
RN [6]
RP IDENTIFICATION IN THE HYR1/IFF FAMILY.
RX PubMed=17371861; DOI=10.1128/iai.00102-07;
RA Bates S., de la Rosa J.M., MacCallum D.M., Brown A.J., Gow N.A., Odds F.C.;
RT "Candida albicans Iff11, a secreted protein required for cell wall
RT structure and virulence.";
RL Infect. Immun. 75:2922-2928(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21841123; DOI=10.1128/ec.05044-11;
RA Boisrame A., Cornu A., Da Costa G., Richard M.L.;
RT "Unexpected role for a serine/threonine-rich domain in the Candida albicans
RT Iff protein family.";
RL Eukaryot. Cell 10:1317-1330(2011).
CC -!- FUNCTION: GPI-anchored cell wall protein involved in cell wall
CC organization, hyphal growth, as well as in host-fungal interaction and
CC virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:21841123}. Membrane {ECO:0000305}; Lipid-anchor,
CC GPI-anchor {ECO:0000305}.
CC -!- INDUCTION: Constitutive expression independent of white/opaque
CC switching or mating type locus. {ECO:0000269|PubMed:16950924}.
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 -!- SIMILARITY: Belongs to the HYR1/IFF family. {ECO:0000305}.
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DR EMBL; CP017630; AOW30843.1; -; Genomic_DNA.
DR RefSeq; XP_717969.1; XM_712876.1.
DR AlphaFoldDB; Q5A849; -.
DR SMR; Q5A849; -.
DR GeneID; 3640436; -.
DR KEGG; cal:CAALFM_CR00760CA; -.
DR CGD; CAL0000179460; HYR4.
DR VEuPathDB; FungiDB:CR_00760C_A; -.
DR HOGENOM; CLU_268223_0_0_1; -.
DR InParanoid; Q5A849; -.
DR OMA; HIHESAY; -.
DR OrthoDB; 1656680at2759; -.
DR PRO; PR:Q5A849; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR InterPro; IPR031573; Cell_wall_rpt.
DR InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR Pfam; PF11765; Hyphal_reg_CWP; 1.
DR Pfam; PF15789; Hyr1; 2.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1195
FT /note="Hyphally regulated cell wall protein 4"
FT /id="PRO_0000424756"
FT PROPEP 1196..1225
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424757"
FT REGION 832..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1195
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
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 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 634
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1035
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1225 AA; 133951 MW; 95E0039DB2A6D729 CRC64;
MFSYSQAIRF IIFLLPICLT FKITENRIDR GKLNFEIQDI TIKSGAFWSI VDNSICTFFG
SLMVEPQASL YVSSTSPILA LQVAFVSILG VFHNQGNITF DSSASLTSAT YRIITSTFRN
TGRMFFSASG KFPNTMDIVA SDWTNNGLLS FHQDQRTSGV VSLGSALGTI TNNGQIKLSN
QVYQQRTQIS GSGCFVAINN STIYISNSLL PVQITQSFYL ADSTSSIIVD SFSATQTFNV
YGFGNGNMIG LTLPLVGNYW YSSYTYDATT GILIMRNVFL EQKFNIGLGY NPSLFKIVTD
WGAGIPSTIL GSLSYSGCVP SRRLPSICQI DPISSLEIPG TKPTQFTSVF VSTDDSGRNG
QYVGLFEVAT NKNYEWVSAV IIITSIPTVT IELPPTLTLE AQWLPTVSGV LHTSSTITQS
TKIGLLTTVS LVPVAETQLA SRTFSIVGPP IPDTTSLELV VPTKSETRVV TESTVVPVLP
PKVTHFTNSS TSNRRYSSES MVDEEFPSEP FMSDEVSIEV YESYTDESCV ISTDFSVDVD
YSSDLSMNFQ TYDTLDTTEM FNTVENFETY DTFGTIESFD IFETSQTFES YETFNETSDL
SMFSLTSESF SDLPPPLVQT DTPVSFNPVP SRTNMSEKTI MWEVTNSQGS IITESGIILI
SGEYQTTVTT FLRDLDQMEG YTKYTKTWEV TNSNGSVVTE SGIIDESGSY HTTVTTFPQK
DQNWEWAANT VEYTKTWIVT NEDGSIITES GIVGESGLYQ TTVTTFPHEL SSFTIYQSEE
AHSPGVINAG DIESTPLATS SSIYQSVIIE DEFPSSPGNT YTDVFSPTTG HDLDLPDDTT
FTPSQSSSTT VPIESEYISE SIILDAGSSV STMISPTTLT TNFPIFDSSD NQFKHVSLWD
SRVSSRSIVI VSSEFPESDA PLILASPNDG SSNQTSTTAS ITVNDNQNIN NPEFQQGEAV
ISSSIDSSVS HLYYISEETS IASNNGDLSD DLEVDFILLT SLHDTISAKA TSAGYSWKFY
PESDEIQIDQ TGDYNYSLAG AKTHIHESAY TQQDASTQKG ASVQQETSIQ QRVSTKQETY
TQEGTQQVTR TQEKVQQGAS HSTTNSHFEG TFISKTASPT NNDFTLSFEP KDNATDISNS
FFAHLSIVGN STVFETDYTD FSFIANSNTF KSDANGVDST SNQTYSAGVG GSNVSGLISK
SESVVLLIRP VMIFVFLAIC VVIML
