PHR1_CANAL
ID PHR1_CANAL Reviewed; 548 AA.
AC P43076; A0A1D8PM46; Q5A661;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 4.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=pH-responsive protein 1;
DE AltName: Full=pH-regulated protein 1;
DE Flags: Precursor;
GN Name=PHR1; OrderedLocusNames=CAALFM_C404530CA;
GN ORFNames=CaO19.11310, CaO19.3829;
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 [GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=7823929; DOI=10.1128/mcb.15.2.601;
RA Saporito-Irwin S.M., Birse C.E., Sypherd P.S., Fonzi W.A.;
RT "PHR1, a pH-regulated gene of Candida albicans, is required for
RT morphogenesis.";
RL Mol. Cell. Biol. 15:601-613(1995).
RN [2]
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 [3]
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 [4]
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).
CC -!- FUNCTION: Required for apical cell growth and plays an essential role
CC in morphogenesis. May be integral to the pathogenic ability of the
CC organism.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- INDUCTION: Strongly expressed under conditions of alkaline pH but not
CC expressed at any pH below 5.5.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; M90812; AAA68196.1; -; Genomic_DNA.
DR EMBL; CP017626; AOW29201.1; -; Genomic_DNA.
DR RefSeq; XP_717233.2; XM_712140.2.
DR AlphaFoldDB; P43076; -.
DR SMR; P43076; -.
DR BioGRID; 1224182; 2.
DR STRING; 237561.P43076; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR PRIDE; P43076; -.
DR GeneID; 3641108; -.
DR KEGG; cal:CAALFM_C404530CA; -.
DR CGD; CAL0000177455; PHR1.
DR VEuPathDB; FungiDB:C4_04530C_A; -.
DR eggNOG; ENOG502QPST; Eukaryota.
DR HOGENOM; CLU_021855_2_1_1; -.
DR InParanoid; P43076; -.
DR OrthoDB; 728071at2759; -.
DR PHI-base; PHI:33; -.
DR PRO; PR:P43076; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..517
FT /note="pH-responsive protein 1"
FT /id="PRO_0000010483"
FT PROPEP 518..548
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010484"
FT REGION 483..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 517
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..111
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 224..358
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 242..273
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 381..432
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 390..456
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 409..414
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT CONFLICT 79
FT /note="A -> R (in Ref. 1; AAA68196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 59457 MW; 0836AD1428C5769A CRC64;
MYSLIKSLAT FATLFSLTLA KFESSTPPVE VVGNKFYFSN NGSQFLIRGI AYQQDAAGSV
SSGYDADPNR KYNDPLADAD ACKRDVKYFK ESNTNTLRVY AIDPDKDHEE CMKIFSDAGI
YIVADLSEPT VSINRNNPEW NLDLYKRYTK VIDKMQEYSN VLGFFAGNEV TNNRSNTDAS
AFVKAAIRDM KKYIKESDYR QIPVGYSSND DEEIRVAIAD YFSCGSLDDR ADFFGINMYE
WCGKSTFETS GYKDRTEEIK NLTIPAFFSE YGCNANRPRL FQEIGTLYSD KMTDVWSGGI
VYMYFEEANK YGLVSVDGNS VKTLSDYNNY KSEMNKISPS LAHTSTLSSS DASKTLQCPG
TAASTWKAAT NLPPTPDESY CDCISKSLEC VVADDVDKED YGDLFGQVCG YIDCSAISAD
GSKGEYGVAS FCSDKDRLSY VLNQYYLDQD KKSSACDFKG SASINSKASA SGSCKAVSGV
ATGKASSSGG SSKSGSSSAS ASGSSSSSTS SGSSSSSGVK ATQQMSMVKL VSIITIVTAF
VGGMSVVF
