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PGA12_CANAL
ID   PGA12_CANAL             Reviewed;         315 AA.
AC   Q5ACP5; A0A1D8PU65;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Phosphomutase-like protein 3;
DE   AltName: Full=Predicted GPI-anchored protein 12;
DE   Flags: Precursor;
GN   Name=PGA12; Synonyms=PMU3; OrderedLocusNames=CAALFM_CR10210WA;
GN   ORFNames=CaO19.7597;
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).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
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DR   EMBL; CP017630; AOW31672.1; -; Genomic_DNA.
DR   RefSeq; XP_719359.1; XM_714266.1.
DR   AlphaFoldDB; Q5ACP5; -.
DR   SMR; Q5ACP5; -.
DR   STRING; 237561.Q5ACP5; -.
DR   GeneID; 3638920; -.
DR   KEGG; cal:CAALFM_CR10210WA; -.
DR   CGD; CAL0000174441; PGA12.
DR   VEuPathDB; FungiDB:CR_10210W_A; -.
DR   eggNOG; KOG4754; Eukaryota.
DR   HOGENOM; CLU_039184_0_3_1; -.
DR   InParanoid; Q5ACP5; -.
DR   OMA; EIYGSHT; -.
DR   OrthoDB; 1063916at2759; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Isomerase; Lipoprotein; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..286
FT                   /note="Phosphomutase-like protein 3"
FT                   /id="PRO_0000424656"
FT   PROPEP          287..315
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000424657"
FT   ACT_SITE        77
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   ACT_SITE        173
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   SITE            246
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   LIPID           286
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   315 AA;  35799 MW;  8E711809E862DE1A CRC64;
     MQQFLTLGAL WTLFNVATTI SLPKYSSSQT YFAQSDPNIP VSQVDDTNNF GLKSQYSWDD
     VVSNLASNEK LFFLQRHGQG WHNVAPSNFS RVDWNCYWAE QSGRDGVVWE DAELTPKGVQ
     QIQNLHQRIK DTPDFPQPEK FFVSPLRRTL QTWNITWNGL PHKTPLIKEF AREIYGIDSE
     SKRHNKTFIH NYVPSFEFES GFTEQDENWS PDKSESDQHC DYRAAVLLQD IFNDSPDEKV
     ISVVLHSGII YCLLDVVGHR YFPMATGGAI PVVIAIENYN TDYPLNDAWD TFKDWCPNPP
     ASISGTATST ATGSA
 
 
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