PGA49_CANAL
ID PGA49_CANAL Reviewed; 734 AA.
AC Q59QA5; A0A1D8PMG5; Q59Q85;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Predicted GPI-anchored protein 49;
DE Flags: Precursor;
GN Name=PGA49; OrderedLocusNames=CAALFM_C405920CA;
GN ORFNames=CaO19.11882, CaO19.4404;
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; CP017626; AOW29322.1; -; Genomic_DNA.
DR RefSeq; XP_711852.2; XM_706759.2.
DR AlphaFoldDB; Q59QA5; -.
DR STRING; 237561.Q59QA5; -.
DR PRIDE; Q59QA5; -.
DR GeneID; 3646525; -.
DR KEGG; cal:CAALFM_C405920CA; -.
DR CGD; CAL0000196151; PGA49.
DR VEuPathDB; FungiDB:C4_05920C_A; -.
DR HOGENOM; CLU_377647_0_0_1; -.
DR OrthoDB; 1702990at2759; -.
DR PRO; PR:Q59QA5; -.
DR Proteomes; UP000000559; Chromosome 4.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..707
FT /note="Predicted GPI-anchored protein 49"
FT /id="PRO_0000429952"
FT PROPEP 708..734
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429953"
FT REGION 78..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..128
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..257
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 707
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
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 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 734 AA; 81980 MW; C6189029F30B0ECF CRC64;
MNYITSLLLL SSNTFLHPTT TYLQSMNDSI VLVTSSVSTE LTTLGYDPIS TISGVNGTNN
IDYIKLLNDT NSTFVQLDNS DTDIDDSSSN SEDVSSNDEQ IALMNSSSDF SDESDEGNDS
DDNGDEVENM ENNQANESDT QNENDRVLNY DTSSSENENE NENENENQLE QEHQHYYYKN
RSKFYNHFLR YPEVVINNND DRAELASTKN NLLVRSPKSN NRRLIGSSRK KTLKSKSKSK
SSKLKHKSRK SHKRRPKLLK SKDVETNEIT TVEVITLTIT KVLARHDLAA IVTPIQQHQS
GHLIIGYPLP IATKSRLHGY YKSSGVLKEV DANPTEEYDS GDGKENTQQN PIPEKMRLPT
NDDPYSLKPT HHYDPSATMQ NPHKQFTNRT GNFEIPTNVQ DIDDITFPID LSSSDSTSNL
YSILPMNQTN LPDVNTLSLA PGTGSVPPRY SNHHSEFTVE RPPRPSRTKK RPRIKAKKTM
KVSTQISSAM SKSIHITRIG STSSGIASGI TNIVIPNSSS SIYDNYQDSS SDKQPVSLSM
PTKTITMTTD TTSEPVTITE KLDKPKFPDI FTIIRSKLLS KKPQETKLHS PTSTDTKSSK
LMSSSSSNNN KPEISKTTKE YNQTQESTSY NTTKAVPKTS VVSSTTSTKP NDQGNNILNS
FIQFTETIHS RIRFPTADDN NNNAGNNYHR RFTGVVLPEN RQFVFRSASQ NLSFSVLGLI
ILLLLLPGLL IIIM
