PHR2_CANAL
ID PHR2_CANAL Reviewed; 544 AA.
AC O13318; A0A1D8PC54; Q5AB91;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=pH-responsive protein 2;
DE AltName: Full=pH-regulated protein 2;
DE Flags: Precursor;
GN Name=PHR2; OrderedLocusNames=CAALFM_C100220WA;
GN ORFNames=CaO19.13500, CaO19.6081;
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=9315654; DOI=10.1128/mcb.17.10.5960;
RA Muehlschlegel F.A., Fonzi W.A.;
RT "PHR2 of Candida albicans encodes a functional homolog of the pH-regulated
RT gene PHR1 with an inverted pattern of pH-dependent expression.";
RL Mol. Cell. Biol. 17:5960-5967(1997).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- INDUCTION: Repressed at pH values above 6 and progressively induced at
CC more acidic pH values.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; AF011386; AAB80716.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW25724.1; -; Genomic_DNA.
DR RefSeq; XP_719043.1; XM_713950.1.
DR AlphaFoldDB; O13318; -.
DR SMR; O13318; -.
DR STRING; 237561.O13318; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR PRIDE; O13318; -.
DR GeneID; 3639334; -.
DR KEGG; cal:CAALFM_C100220WA; -.
DR CGD; CAL0000181783; PHR2.
DR VEuPathDB; FungiDB:C1_00220W_A; -.
DR eggNOG; ENOG502QPST; Eukaryota.
DR HOGENOM; CLU_021855_2_1_1; -.
DR InParanoid; O13318; -.
DR OMA; GAYSMCT; -.
DR OrthoDB; 728071at2759; -.
DR PRO; PR:O13318; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:CGD.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; ISA:CGD.
DR GO; GO:0042123; F:glucanosyltransferase activity; IDA:CGD.
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 GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..515
FT /note="pH-responsive protein 2"
FT /id="PRO_0000010485"
FT PROPEP 516..544
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010486"
FT REGION 469..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 515
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..101
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 214..347
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 232..263
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 369..420
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 378..444
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 397..402
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT CONFLICT 84
FT /note="T -> YDS (in Ref. 1; AAB80716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 58716 MW; 0F474FAD270A1EDD CRC64;
MLLKSLFPSI LAATSFVSSV AAEDLPAIEI VGNKFFYSNN GSQFYIKGIA YQQNNLDSNE
SFVDPLANPE HCKRDIPYLE AVDTNVIRVY ALDTSQDHTE CMQMLQDAGI YVIADLSQPD
ESINRDDPSW DLDLFERYTS VVDLFHNYTN ILGFFAGNEV TNKKSNTDAS AFVKAAIRDT
KAYIKSKGYR SIPVGYSAND DSAIRVSLAD YFACGDEDEA ADFFGINMYE WCGDSSYKAS
GYESATNDYK NLGIPIFFSE YGCNEVRPRK FTEVATLFGD QMTPVWSGGI VYMYFEEENN
YGLVSIKDNT VSTLKDYSYY SSEIKDIHPS SAKASAESAS SISRTTCPTN TNNWEASTNL
PPTPDKEVCE CMSASLKCVV DDKVDSDDYS DLFSYICAKI DCDGINANGT TGEYGAYSPC
HSKDKLSFVM NLYYEQNKES KSACDFGGSA SLQSAKTASS CSAYLSSAGS SGLGTVSGTV
RTDTSQSTSD SGSGSSSSSS SSSSSSSSGS SGSKSAASIV SVNLLTKIAT IGISIVVGFG
LITM
