MTC6_VANPO
ID MTC6_VANPO Reviewed; 532 AA.
AC A7TEV4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Maintenance of telomere capping protein 6;
DE Flags: Precursor;
GN Name=MTC6; ORFNames=Kpol_1050p58;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480381; EDO19200.1; -; Genomic_DNA.
DR RefSeq; XP_001647058.1; XM_001647008.1.
DR AlphaFoldDB; A7TEV4; -.
DR STRING; 436907.A7TEV4; -.
DR EnsemblFungi; EDO19200; EDO19200; Kpol_1050p58.
DR GeneID; 5547533; -.
DR KEGG; vpo:Kpol_1050p58; -.
DR eggNOG; ENOG502QVFP; Eukaryota.
DR HOGENOM; CLU_033723_0_0_1; -.
DR InParanoid; A7TEV4; -.
DR OMA; NLNESWY; -.
DR OrthoDB; 618092at2759; -.
DR PhylomeDB; A7TEV4; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..532
FT /note="Maintenance of telomere capping protein 6"
FT /id="PRO_0000407783"
FT TOPO_DOM 24..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
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 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 532 AA; 60421 MW; 67239B57F5FB3561 CRC64;
MIVMQLQQQL LIWVIFWLNY ATALTNFTWS SDSPSMVYAL RAQRDVMSSA TIDQLPLVGV
DVGRVFINGM VIENKDEDEE DEDLLVMLES LLEAGVQALS VDVEYKDEIW VVGNSTIAFD
DFLLTVRDFL DGTNTDLSAN ILMVMLRIQP NSSDYGSPST FNNYTHGYNY SDISDYNKDD
IGDASDIEAL IYSNIGRSYI YSPEDLVDDR NKSYTSDIYG LNSVNGWPTL SHFLYQKRKR
VLFTELTTEM PYNTSSLLFN KTILHLDGGN IAISCPTSNS ELTELSLVAW RFIENEFTDD
SVRSYVDCGY SPIIANKYNQ NNITHLLNLT QSALLWSWEV GQPSTNEKKN SDTLEAYNCV
SFVYTANNYS AYWKVENCYD EKKGLCEAKT DLFSYIVSEN VDSYFNFDSF DGSNCPDGFD
FSIPKTPLEQ LAVINYLRLR NSSDTEIWID LNSISVNNCW VTGGPYATCP YETVMSRRNF
TKMITPASIT SFGLLVLVTC LNLLSLPIHD NRSNWRRMIN KLSRNEFDGV PA