ID   KAR5_CANGA              Reviewed;         469 AA.
AC   Q6FU40;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Nuclear fusion protein KAR5;
DE   AltName: Full=Karyogamy protein 5;
DE   Flags: Precursor;
GN   Name=KAR5; OrderedLocusNames=CAGL0F06589g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Required for nuclear membrane fusion during karyogamy.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}. Nucleus membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KAR5 family. {ECO:0000305}.
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DR   EMBL; CR380952; CAG59178.1; -; Genomic_DNA.
DR   RefSeq; XP_446254.1; XM_446254.1.
DR   AlphaFoldDB; Q6FU40; -.
DR   STRING; 5478.XP_446254.1; -.
DR   EnsemblFungi; CAG59178; CAG59178; CAGL0F06589g.
DR   GeneID; 2887916; -.
DR   KEGG; cgr:CAGL0F06589g; -.
DR   CGD; CAL0131410; CAGL0F06589g.
DR   VEuPathDB; FungiDB:CAGL0F06589g; -.
DR   eggNOG; ENOG502QVCQ; Eukaryota.
DR   HOGENOM; CLU_042075_0_0_1; -.
DR   InParanoid; Q6FU40; -.
DR   Proteomes; UP000002428; Chromosome F.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IEA:InterPro.
DR   GO; GO:0048288; P:nuclear membrane fusion involved in karyogamy; IEA:InterPro.
DR   InterPro; IPR007292; Nuclear_fusion_Kar5.
DR   PANTHER; PTHR28012; PTHR28012; 1.
DR   Pfam; PF04163; Tht1; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Karyogamy; Membrane; Nucleus;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000250"
FT   CHAIN           ?..469
FT                   /note="Nuclear fusion protein KAR5"
FT                   /id="PRO_0000308771"
FT   TOPO_DOM        ?..420
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        442..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        446..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        467..469
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   469 AA;  53659 MW;  A6C98337E8B2B33A CRC64;
     MSMSITQPIK DLLSSQFQSY NISEQVKLYD IFPLLKPSCI KEAITDVVEV CTGYGPESLD
     PSIRAKAAVK LSLCEFEAVG LSIIPQGCYS NSIEEMMDCM LEIEHSSHWW TTYSGNYQRL
     SDVCSTYREY YQEKAIIETF LNITDFMADF HNQFKSSVVS ETQEFQSNMK DKFAGVYNQF
     THFESLLSQM IQKHSGIIND SIVAIKNKLS TEFVDELQML KNDRYILINQ ILESDTEIKK
     TIDSMLVELT EDMKNQISAK SEFLINHMNI TRLNESTALH DIIEENLQER FKDIAIFLDK
     FMVEIQTETN KVLLEVNEKL PTLEQQYLGN FAQALSNIDK QVLSASLQWQ YDYDVVFANL
     YAALDLLNSN LNSSVKKIEQ IEHVIDTIIV DTSFLNDQLA NLILIPSTIL RAFSFIGVKR
     VIIAIIVLYF KSTLLCLVHY GQSFRIAALL MSATAGIFCS KLLMSYIYN