ID G8B5L0_CANPC Unreviewed; 491 AA.
AC G8B5L0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Nuclear fusion protein KAR5 {ECO:0000256|ARBA:ARBA00021601, ECO:0000256|RuleBase:RU368082};
DE AltName: Full=Karyogamy protein 5 {ECO:0000256|ARBA:ARBA00031468, ECO:0000256|RuleBase:RU368082};
GN OrderedLocusNames=CPAR2_603210 {ECO:0000313|CGD:CAL0000151095,
GN ECO:0000313|EMBL:CCE39902.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE39902.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., 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., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
CC -!- FUNCTION: Required for nuclear membrane fusion during karyogamy.
CC {ECO:0000256|ARBA:ARBA00003389, ECO:0000256|RuleBase:RU368082}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU368082}. Nucleus membrane
CC {ECO:0000256|RuleBase:RU368082}.
CC -!- SIMILARITY: Belongs to the KAR5 family. {ECO:0000256|ARBA:ARBA00010473,
CC ECO:0000256|RuleBase:RU368082}.
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; HE605202; CCE39902.1; -; Genomic_DNA.
DR AlphaFoldDB; G8B5L0; -.
DR EnsemblFungi; CPAR2_603210-T; CPAR2_603210-T-p1; CPAR2_603210.
DR CGD; CAL0000151095; CPAR2_603210.
DR VEuPathDB; FungiDB:CPAR2_603210; -.
DR eggNOG; ENOG502QVCQ; Eukaryota.
DR Proteomes; UP000005221; Chromosome 6.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IEA:UniProtKB-UniRule.
DR GO; GO:0048288; P:nuclear membrane fusion involved in karyogamy; IEA:UniProtKB-UniRule.
DR InterPro; IPR007292; Nuclear_fusion_Kar5.
DR PANTHER; PTHR28012; NUCLEAR FUSION PROTEIN KAR5; 1.
DR PANTHER; PTHR28012:SF1; NUCLEAR FUSION PROTEIN KAR5; 1.
DR Pfam; PF04163; Tht1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU368082};
KW Karyogamy {ECO:0000256|ARBA:ARBA00022459, ECO:0000256|RuleBase:RU368082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368082};
KW Nucleus {ECO:0000256|RuleBase:RU368082};
KW Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW Signal {ECO:0000256|RuleBase:RU368082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368082}.
FT TRANSMEM 434..458
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368082"
FT TRANSMEM 464..485
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368082"
SQ SEQUENCE 491 AA; 56409 MW; AAA5920B07A72D96 CRC64;
MKTSTSVFLW GQAIAKGLSL SGRFNYLNAL PALEIWKDDC SRQALSSILP QCLDGIETIT
SSQQKEVALE LSICELENAG IEYPLDCNHQ IRHRNIDKCI QFLEKSPQFW TSYSGNYRSV
KEVCHQVSLP LKKEQIVEIY NNVTNLFQSV LNDLLESQAD EKEVQTQLKK RFEAMLNLID
EIMEERKEAA NSVNQTFNVF YENFELSLNN ALIIIRESYH GVNTNLNEIE RHIKYFTKEL
HNINELIREN QIQLKQQQDD LQKGNNILLN QQNLALERMK GINEYAMELR ESTRGQFESM
ERELQFSAFK IQSINALINH NVDDLQVQRR AINQQTETIL NQISEAFVSY LNASGQKVVV
SFESSLNDSL VAIEKRLEQS VVSIELFESR VGNFISKANN ATEYIMNVIP NFAYGVMSYA
SDKYLSMKMV FSRAYAIMMF LVVVVVFLVT KPMIHFIWKL LGKSFTVLFP LILGVVAAIF
TVELIRVLSN V
//
