PGA60_CANAL
ID PGA60_CANAL Reviewed; 741 AA.
AC Q5ABW2; A0A1D8PQ20; Q5AC82;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Putative uncharacterized protein;
DE Flags: Precursor;
GN Name=PGA60; OrderedLocusNames=CAALFM_C603060WA;
GN ORFNames=CaO19.13035, CaO19.5588;
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=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [5]
RP INDUCTION.
RX PubMed=23208712; DOI=10.1128/aac.02040-12;
RA Silva L.V., Sanguinetti M., Vandeputte P., Torelli R., Rochat B.,
RA Sanglard D.;
RT "Milbemycins: more than efflux inhibitors for fungal pathogens.";
RL Antimicrob. Agents Chemother. 57:873-886(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- INDUCTION: Up-regulated upon milbemycins A3 oxim derivative (A3Ox)
CC treatment. {ECO:0000269|PubMed:23208712}.
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DR EMBL; CP017628; AOW30237.1; -; Genomic_DNA.
DR RefSeq; XP_719150.2; XM_714057.2.
DR AlphaFoldDB; Q5ABW2; -.
DR STRING; 237561.Q5ABW2; -.
DR GeneID; 3639271; -.
DR KEGG; cal:CAALFM_C603060WA; -.
DR CGD; CAL0000190944; PGA60.
DR VEuPathDB; FungiDB:C6_03060W_A; -.
DR HOGENOM; CLU_370875_0_0_1; -.
DR InParanoid; Q5ABW2; -.
DR OrthoDB; 1733293at2759; -.
DR PRO; PR:Q5ABW2; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..719
FT /note="Putative uncharacterized protein"
FT /id="PRO_0000429960"
FT PROPEP 720..741
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429961"
FT REGION 142..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..167
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 719
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 741 AA; 80686 MW; F8F7B32FB6BEF57A CRC64;
MKTISILAFL VLARLIEAND LFQVKTIIDY QDLYLHINPN NFQVKLSHSS TDVFEFDESS
NKLFCAGTND IITYNKENCP YLMKFADESS SSVLGWSLDR QTLRFDHDLY FCGTKPPYSL
LADPSGSANC RKLNIFRTVL EPKVEKEEEE EEYDGEEDDD DESLTEFESS TDFPTMTDES
TEVEPSTTTE SAISTTETSK DEESSTTVES TTTPKTTTTT SADSVTTTSK SNESLTTTES
NESSTTTESK DSSTTTDEST PESSTTETDK TETTIEEQEE ESTTSSQSEE TEGPSGGNVD
STVAMVISAM FQGDRVYFYS DDKYITLLNG DLATFKIDDG YLQVNNNKWV NVNIERLLEL
VDNQEDATQG WIINDEGIFL VQDGFYSDSV SFSACGHDSG YRVYLGEENG CEPLNQFRIM
NIEEDEIDET ETTESTKTTE TTKTTGPAET TDSAESTDDS NESSAPPPTE DPSDIPSATT
TDEATVDPSD EQSIAPTSEP IDESTESEEP NESVTVTGDT TTDTSEQGLT TFTTETTATV
TDCEDGDDSC TPRTTIRSTV ITTHCPIVTK TEVETIVTDL TITLTTCIDE TICEATTFVV
STTVVTTTLT THSVVTEYVS SAHEGDGSST IANEDKHNDA IVTPQETVAP DTNSPDADQE
QPDSVEPDNE TTDAPINVED DATALISDED TTTSTITTLI YITQSGDQPI KTPVPIFDNA
ANLAGSISLS SGVLLLILML I
