ID   KAR5_LODEL              Reviewed;         523 AA.
AC   A5E4Z8;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Nuclear fusion protein KAR5;
DE   AltName: Full=Karyogamy protein 5;
DE   Flags: Precursor;
GN   Name=KAR5; ORFNames=LELG_04687;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981530; EDK46506.1; -; Genomic_DNA.
DR   RefSeq; XP_001523874.1; XM_001523824.1.
DR   AlphaFoldDB; A5E4Z8; -.
DR   SMR; A5E4Z8; -.
DR   STRING; 379508.A5E4Z8; -.
DR   EnsemblFungi; EDK46506; EDK46506; LELG_04687.
DR   GeneID; 5231200; -.
DR   KEGG; lel:LELG_04687; -.
DR   VEuPathDB; FungiDB:LELG_04687; -.
DR   eggNOG; ENOG502QVCQ; Eukaryota.
DR   HOGENOM; CLU_039530_0_0_1; -.
DR   InParanoid; A5E4Z8; -.
DR   OMA; LSICEFQ; -.
DR   OrthoDB; 1476880at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..523
FT                   /note="Nuclear fusion protein KAR5"
FT                   /id="PRO_0000308774"
FT   TOPO_DOM        23..469
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        491..500
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        501..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        522..523
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
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        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   523 AA;  58786 MW;  751B6EC0A74189F5 CRC64;
     MVGASAISGV VIIANVVAAI AAAAGDGDGG IASTTDTILT LDGIKILNNA LLQWKDDCNQ
     RALAEVMPQC IHGVENITPS QQKHTAMELS ICEFENNGLD YPLECHASVR NLNTNTCIQA
     LEKSPQYWTT FSGNYRAVKD ICHQISLPYE KDQIIEVYEN MTLLYRSVME DLKSSHHKYT
     VELEMKIQNK FNKLFSVVDD LMRSRAEENN KVNQTFNKFY ENFQVSISNA LVVMQNSYDG
     ANTNFELMQR HVSYFATELQ RILLLVQEQG EKLQVQQEQL VTGNVKLSIQ QERLFDNMQL
     FGNELDKLHN AEVSRVSSVN KQLKLTEFSI RHANSILREN TDELHLQRML IAEYTPIILG
     NITTLLMHFL NQSASEIVEN FEHSLNLSLE KLSLKIDETA NSLAVVNATI ARCSIFASSV
     VETLDSLKNS TIRMMMLFMS MITPSVTFDG LISGAKAIIA FFTLVTRLAA VIAICLLIIL
     IWPIVKSLFF QPLCYLMRRC SYIVVSILVG VAAANFSVWL LQK