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KAR5_YEAST
ID   KAR5_YEAST              Reviewed;         504 AA.
AC   Q04746; D6VZN9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Nuclear fusion protein KAR5;
DE   AltName: Full=Factor-induced gene 3 protein;
DE   AltName: Full=Karyogamy protein 5;
DE   Flags: Precursor;
GN   Name=KAR5; Synonyms=FIG3; OrderedLocusNames=YMR065W; ORFNames=YM9916.04;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=8051211; DOI=10.1083/jcb.126.4.911;
RA   Kurihara L.J., Beh C.T., Latterich M., Schekman R., Rose M.D.;
RT   "Nuclear congression and membrane fusion: two distinct events in the yeast
RT   karyogamy pathway.";
RL   J. Cell Biol. 126:911-923(1994).
RN   [4]
RP   FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=9382856; DOI=10.1083/jcb.139.5.1063;
RA   Beh C.T., Brizzio V., Rose M.D.;
RT   "KAR5 encodes a novel pheromone-inducible protein required for homotypic
RT   nuclear fusion.";
RL   J. Cell Biol. 139:1063-1076(1997).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=9456310; DOI=10.1083/jcb.140.3.461;
RA   Erdman S., Lin L., Malczynski M., Snyder M.;
RT   "Pheromone-regulated genes required for yeast mating differentiation.";
RL   J. Cell Biol. 140:461-483(1998).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10069807; DOI=10.1091/mbc.10.3.609;
RA   Brizzio V., Khalfan W., Huddler D., Beh C.T., Andersen S.S.L.,
RA   Latterich M., Rose M.D.;
RT   "Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during
RT   nuclear fusion in Saccharomyces cerevisiae.";
RL   Mol. Biol. Cell 10:609-626(1999).
RN   [7]
RP   INDUCTION.
RX   PubMed=11125145; DOI=10.1126/science.290.5500.2306;
RA   Ren B., Robert F., Wyrick J.J., Aparicio O., Jennings E.G., Simon I.,
RA   Zeitlinger J., Schreiber J., Hannett N., Kanin E., Volkert T.L.,
RA   Wilson C.J., Bell S.P., Young R.A.;
RT   "Genome-wide location and function of DNA binding proteins.";
RL   Science 290:2306-2309(2000).
RN   [8]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH PRM3.
RX   PubMed=19297527; DOI=10.1091/mbc.e08-10-0987;
RA   Shen S., Tobery C.E., Rose M.D.;
RT   "Prm3p is a pheromone-induced peripheral nuclear envelope protein required
RT   for yeast nuclear fusion.";
RL   Mol. Biol. Cell 20:2438-2450(2009).
CC   -!- FUNCTION: Required for nuclear membrane fusion during karyogamy.
CC       {ECO:0000269|PubMed:10069807, ECO:0000269|PubMed:8051211,
CC       ECO:0000269|PubMed:9382856, ECO:0000269|PubMed:9456310}.
CC   -!- SUBUNIT: Interacts with PRM3. {ECO:0000269|PubMed:19297527}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Nucleus membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: By mating pheromone. Expression is directly controlled by
CC       STE12 as cells respond to mating pheromone.
CC       {ECO:0000269|PubMed:11125145, ECO:0000269|PubMed:9382856,
CC       ECO:0000269|PubMed:9456310}.
CC   -!- SIMILARITY: Belongs to the KAR5 family. {ECO:0000305}.
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DR   EMBL; Z48952; CAA88790.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09963.1; -; Genomic_DNA.
DR   PIR; S52825; S52825.
DR   RefSeq; NP_013781.1; NM_001182563.1.
DR   AlphaFoldDB; Q04746; -.
DR   BioGRID; 35240; 52.
DR   DIP; DIP-874N; -.
DR   IntAct; Q04746; 8.
DR   MINT; Q04746; -.
DR   STRING; 4932.YMR065W; -.
DR   PaxDb; Q04746; -.
DR   PRIDE; Q04746; -.
DR   EnsemblFungi; YMR065W_mRNA; YMR065W; YMR065W.
DR   GeneID; 855087; -.
DR   KEGG; sce:YMR065W; -.
DR   SGD; S000004669; KAR5.
DR   VEuPathDB; FungiDB:YMR065W; -.
DR   eggNOG; ENOG502QVCQ; Eukaryota.
DR   HOGENOM; CLU_042075_0_0_1; -.
DR   InParanoid; Q04746; -.
DR   OMA; LSICEFQ; -.
DR   BioCyc; YEAST:G3O-32767-MON; -.
DR   PRO; PR:Q04746; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04746; protein.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0031301; C:integral component of organelle membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:SGD.
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   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Karyogamy; Membrane; Nucleus;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..504
FT                   /note="Nuclear fusion protein KAR5"
FT                   /id="PRO_0000203279"
FT   TOPO_DOM        20..452
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:9382856"
FT   TRANSMEM        453..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        471..481
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:9382856"
FT   TRANSMEM        482..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        503..504
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:9382856"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   504 AA;  58440 MW;  368B9D37FC9C2B0C CRC64;
     MFEMRYVYLF AICIKFVSSS ELGKINNLLQ GRLIYTDNSV ATNVLESKFP FLKSTCVKDA
     LKLFLPQCIA NGLESIDAET RVETAIKLSI CEFQASGLGE IPENCMVDDL GSMMDCMFEL
     ESSSQWWTTY SGNYQRLSSI CYENLLPFEK EQILKLFLNI TELYDSFGDD VDTKLNHLMF
     QMEQDSQNFL DDLARMFRNY DNELRNATES NRIILENDLS FFRNKVNDVL YETSEQLEVQ
     IIEKNSQLMN EVDTVHHIMS DLADELAKND IKSKINDLKD DSLNNLQDLV EMSNDVKEYY
     SRNNKLVNTE LENFSMGLKK QLGGMSKDLS ESQMEAIELL QGFNSILHDS LLPSMTDEIV
     PEMTNFKNTL LQEWTAITST LNGDFALWNE EIFSTFNDIS EKLNGTKKKL DDIEIRVSLV
     HKNVMTMMRV LDFMWKTSKM IIRCGYLAVK NKYYWLLCSV VWIWSKYRTS RVNVKMIPIK
     RYYQWAALLL SIYLGAKTGS LIDF
 
 
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