ID   KAR5_DEBHA              Reviewed;         574 AA.
AC   Q6BNJ4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Nuclear fusion protein KAR5;
DE   AltName: Full=Karyogamy protein 5;
DE   Flags: Precursor;
GN   Name=KAR5; OrderedLocusNames=DEHA2E21208g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382137; CAG88499.2; -; Genomic_DNA.
DR   RefSeq; XP_460226.2; XM_460226.1.
DR   AlphaFoldDB; Q6BNJ4; -.
DR   SMR; Q6BNJ4; -.
DR   STRING; 4959.XP_460226.2; -.
DR   EnsemblFungi; CAG88499; CAG88499; DEHA2E21208g.
DR   GeneID; 2902143; -.
DR   KEGG; dha:DEHA2E21208g; -.
DR   VEuPathDB; FungiDB:DEHA2E21208g; -.
DR   eggNOG; ENOG502QVCQ; Eukaryota.
DR   HOGENOM; CLU_474887_0_0_1; -.
DR   InParanoid; Q6BNJ4; -.
DR   OMA; LSICEFQ; -.
DR   OrthoDB; 1476880at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..574
FT                   /note="Nuclear fusion protein KAR5"
FT                   /id="PRO_0000308772"
FT   TOPO_DOM        21..483
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505..540
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        541..561
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        562..574
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   574 AA;  65792 MW;  A2FB400A73A9722B CRC64;
     MDCVNISWFL ITLFAAIATS TMHDGENNNV GKMLQEPTYL QSEMIESIMS RHLESFSLTE
     SDFEDIIFMK PRSKCVKDAL KDIIPECMRL GVDSIEPGLQ KKAAIQLSIC EFENSKVTYP
     SSCYNMINDN DFDSCIFDIE RAPQYWTTFS GYYREITKIC YEESLPFEKE QIISLYSNIT
     KLYSKMFQDL NDSYKDSTHI QQMMKNEFKE LQRMMKVILD QNEKTSEEVK EKYEEFSEQY
     SSMLSTSLEI SKKFSLGTEN LVEDMANNIK YLDFELSRIS IAIEDLDFET KLTDMKNSVL
     DDVRNLSDES ISLLDSILTN LESLDILSQD AQNITNGISQ SLKKNEVLSN NMNNALIETD
     TQLHEHNEVI RFEFEETISY LSQFSDQAID NAIRDTSEEI TKHVATFIDS INLRLEETTT
     KLEEVIYNID DLSDKVGNAS SYLIEGLNLL TSNGIMDALL LTYNNVASGL ESGFGMLTTL
     KSDIFKIVRF ITACILFAIL FIWSMNRLFS QNRTKHTTLS SISPIGILNF RRIFRFLTNL
     ALWLSVMGGT LLAVIVTNFL IQLKVYISKL STND