CAS1_CRYNJ
ID CAS1_CRYNJ Reviewed; 960 AA.
AC P0CM56; Q55HH1; Q5K709; Q8X227;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Probable O-acetyltransferase CAS1;
DE EC=2.3.1.- {ECO:0000269|PubMed:11703667, ECO:0000269|PubMed:12139628, ECO:0000269|PubMed:12704160, ECO:0000269|PubMed:15004170};
DE AltName: Full=Capsule synthesis protein 1;
GN Name=CAS1; OrderedLocusNames=CNN01530;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11703667; DOI=10.1046/j.1365-2958.2001.02651.x;
RA Janbon G., Himmelreich U., Moyrand F., Improvisi L., Dromer F.;
RT "Cas1p is a membrane protein necessary for the O-acetylation of the
RT Cryptococcus neoformans capsular polysaccharide.";
RL Mol. Microbiol. 42:453-467(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
RN [3]
RP FUNCTION.
RX PubMed=12139628; DOI=10.1046/j.1365-2958.2002.03059.x;
RA Moyrand F., Klaproth B., Himmelreich U., Dromer F., Janbon G.;
RT "Isolation and characterization of capsule structure mutant strains of
RT Cryptococcus neoformans.";
RL Mol. Microbiol. 45:837-849(2002).
RN [4]
RP FUNCTION.
RX PubMed=12704160; DOI=10.1128/iai.71.5.2868-2875.2003;
RA Kozel T.R., Levitz S.M., Dromer F., Gates M.A., Thorkildson P., Janbon G.;
RT "Antigenic and biological characteristics of mutant strains of Cryptococcus
RT neoformans lacking capsular O-acetylation or xylosyl side chains.";
RL Infect. Immun. 71:2868-2875(2003).
RN [5]
RP FUNCTION.
RX PubMed=15004170; DOI=10.4049/jimmunol.172.6.3670;
RA McFadden D.C., Casadevall A.;
RT "Unexpected diversity in the fine specificity of monoclonal antibodies that
RT use the same V region gene to glucuronoxylomannan of Cryptococcus
RT neoformans.";
RL J. Immunol. 172:3670-3677(2004).
CC -!- FUNCTION: Probable O-acetyltransferase required for the O-acetylation
CC of the capsular glucoronoxylmannans (GXM) involved in virulence.
CC {ECO:0000269|PubMed:11703667, ECO:0000269|PubMed:12139628,
CC ECO:0000269|PubMed:12704160, ECO:0000269|PubMed:15004170}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. CASD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF355592; AAL35099.1; -; Genomic_DNA.
DR EMBL; AE017356; AAW47111.1; -; Genomic_DNA.
DR RefSeq; XP_568628.1; XM_568628.1.
DR AlphaFoldDB; P0CM56; -.
DR STRING; 214684.P0CM56; -.
DR PaxDb; P0CM56; -.
DR PRIDE; P0CM56; -.
DR EnsemblFungi; AAW47111; AAW47111; CNN01530.
DR GeneID; 3255512; -.
DR KEGG; cne:CNN01530; -.
DR VEuPathDB; FungiDB:CNN01530; -.
DR eggNOG; KOG1699; Eukaryota.
DR HOGENOM; CLU_008003_0_1_1; -.
DR InParanoid; P0CM56; -.
DR OMA; MIYAACF; -.
DR OrthoDB; 120492at2759; -.
DR PHI-base; PHI:672; -.
DR Proteomes; UP000002149; Chromosome 14.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR InterPro; IPR012419; Cas1_AcylTrans_dom.
DR Pfam; PF07779; Cas1_AcylT; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Oxidoreductase; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..960
FT /note="Probable O-acetyltransferase CAS1"
FT /id="PRO_0000307852"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 115
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT ACT_SITE 350
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT ACT_SITE 353
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 960 AA; 107504 MW; 6AA05D5FCD2650F7 CRC64;
MPNSSKPRSQ ASAAKLNPLW YTYACATLVA AVVLGNILRW AFLELPDSYH CSALLNTGKW
LDPGTWTNWQ PEGCFQLPLS AQSWQKCLAS PTVNTHQALH SSYYDKRTAL FVGDSTVRQL
YFAAARKVGK TSKAWELEGE KHTDRSLLVS DPLGGPSLEL EFWWDPYLNS SKTIGLLSGQ
SSVPSSLLVM GSGLWYLRNP SSGGLASWGA MIYDTFELVK KNQGSPQTAL INPWDNMLLG
PGITLPGLLP NQPPKFVDHS REVEARSLFS RASSISHRPT DFSISDAIVF LPISTPVREK
LSPSRAETIF HTDVEAMNAD LYARLTHPDP PPVVIPSVLN QLLVDDETED GLHFSDKIMN
KQAELLLSWR CNDVMRHEGA TGTCCKRYDW VTPIQGLILA VLILWAPLGT FITPRLPPNS
PILDYLPATS IAPALSTFGL AMGYLFLADR THVFQKEQKD YDAVIFGMIT LAAFVAGLLT
IKNSGKDLGF LNRDITDEWK GWMQIAILIY HFFGASKISG IYNPIRVLVA SYLFMTGYGH
FFFYYKKADF GFQRVVMVLV RLNLLSVVLP YTMNTDYAFY YFAPLVSWWY LIIYATMAIG
SKYNDRPAFL LTKLFTCAGL VTLFMHFPWL MEDVFKVLNT VFNIQWSAKE WSFRVTLDLF
IVWVGMLCAY GFVKFNEHQI SDRPWFPVMR TATLVGSVLG MIWYFWFELH LASKFVYNEY
HAVVCIVPIM SFVFLRNASP VLRSSTSKIF CFIGQCSLET FILQFHGWLA SDTKAILLAV
PSTQWRPVNL VISTICFIWL SYRVSGATGE ITEWLVGKKK ALPLPATSAN SSTSPGRQAT
SPTLTSASAM QAVVVGPQDG AKGGIPESIP MMNQADKDIG GLTPMEDETL ERRDSWPTWM
ASTAASLTGR TVEGYAPLTR RWKDQTVLSV IQNLGDLMKK HNSVKIAVIL LGLWALNWIY
