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MTC6_CANDC
ID   MTC6_CANDC              Reviewed;         615 AA.
AC   B9WE91;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Maintenance of telomere capping protein 6;
DE   Flags: Precursor;
GN   Name=MTC6; ORFNames=CD36_84990;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
CC   -!- FUNCTION: May be involved in telomere capping. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MTC6 family. {ECO:0000305}.
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DR   EMBL; FM992690; CAX43002.1; -; Genomic_DNA.
DR   RefSeq; XP_002419408.1; XM_002419363.1.
DR   AlphaFoldDB; B9WE91; -.
DR   STRING; 42374.XP_002419408.1; -.
DR   EnsemblFungi; CAX43002; CAX43002; CD36_84990.
DR   GeneID; 8047231; -.
DR   KEGG; cdu:CD36_84990; -.
DR   CGD; CAL0000160876; Cd36_84990.
DR   VEuPathDB; FungiDB:CD36_84990; -.
DR   eggNOG; ENOG502QVFP; Eukaryota.
DR   HOGENOM; CLU_033723_0_0_1; -.
DR   OrthoDB; 618092at2759; -.
DR   Proteomes; UP000002605; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..615
FT                   /note="Maintenance of telomere capping protein 6"
FT                   /id="PRO_0000407774"
FT   TOPO_DOM        18..559
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        560..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        581..615
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   615 AA;  70269 MW;  1941DD097502FA7D CRC64;
     MIGLLFVFSV LLSFSVGYIF PFSTSNGPTV NDTLQHAIRS QRDVSKPIPI DRVEFSGVSL
     SSFFESEGYS SDSLSNLYGL LKENIAGVMI DLYWNEFTSK WQLCPAPFPN NITYTSSNRV
     VDVSWNNRTY KCDPNLSTDD IMSILNNFIR DTNTDVEANF MHVMYNLKSI HYKKSNQTIN
     LENAYKEKNS NFNVGMDTLN DTVSLLSSYI FTPLLLEQYQ SSSSKNANSS SSIRYIDSLN
     ETQAIQKFYN QSTILMPSLQ TTLLTQYKRL MVHVISNDMA ESSRSYQISF SDKETIFFNN
     VFPAMIGHTN NASADDFCYE LTHAYNGTDV NIMEFNRVSL NSTLRLIIDN DKTPFTTDSL
     SKYVRCGYCP VFNSTQYSSQ KVTEGNSSII SQEFTSNLFW SWAPGQPSGP DNCTNCTRPV
     TNYTSKYSEA SNGGSDEEEH SNNIAYKCVA LTENGWEVSN CYEKYLFACQ NKLSRNEWKL
     DNYTKRNYFD LDDDDCPEGY FFSLPRSNIE MLSLMTTVKQ ENVSYPIWID LNDITVENCF
     VSGGPYAQCP YQETVTTDKF VRMIAPSFVV AMVVLVLIFL EKVFRKTPIQ TNRKRYWKKA
     IQEYYAKNDY EGVPS
 
 
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