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KAR5_SCHPO
ID   KAR5_SCHPO              Reviewed;         577 AA.
AC   Q09684;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Nuclear fusion protein tht1;
DE   AltName: Full=Twin horsetail protein 1;
DE   Flags: Precursor;
GN   Name=tht1; Synonyms=kar5; ORFNames=SPAC13C5.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP   TOPOLOGY, INDUCTION, AND GLYCOSYLATION.
RX   PubMed=9442101; DOI=10.1083/jcb.140.2.247;
RA   Tange Y., Horio T., Shimanuki M., Ding D.-Q., Hiraoka Y., Niwa O.;
RT   "A novel fission yeast gene, tht1+, is required for the fusion of nuclear
RT   envelopes during karyogamy.";
RL   J. Cell Biol. 140:247-258(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Required for nuclear membrane fusion during karyogamy.
CC       {ECO:0000269|PubMed:9442101}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:9442101}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:9442101}. Nucleus membrane
CC       {ECO:0000269|PubMed:9442101}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:9442101}.
CC   -!- INDUCTION: During conjugation. {ECO:0000269|PubMed:9442101}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9442101}.
CC   -!- SIMILARITY: Belongs to the KAR5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA90454.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D87337; BAA13334.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA90454.1; ALT_INIT; Genomic_DNA.
DR   PIR; T43207; T43207.
DR   RefSeq; NP_592931.1; NM_001018332.2.
DR   AlphaFoldDB; Q09684; -.
DR   SMR; Q09684; -.
DR   STRING; 4896.SPAC13C5.03.1; -.
DR   iPTMnet; Q09684; -.
DR   SwissPalm; Q09684; -.
DR   PaxDb; Q09684; -.
DR   PRIDE; Q09684; -.
DR   GeneID; 2542365; -.
DR   KEGG; spo:SPAC13C5.03; -.
DR   PomBase; SPAC13C5.03; tht1.
DR   eggNOG; ENOG502QVCQ; Eukaryota.
DR   HOGENOM; CLU_475796_0_0_1; -.
DR   InParanoid; Q09684; -.
DR   PhylomeDB; Q09684; -.
DR   PRO; PR:Q09684; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0031309; C:integral component of nuclear outer membrane; EXP:PomBase.
DR   GO; GO:0031301; C:integral component of organelle membrane; IBA:GO_Central.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:PomBase.
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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..577
FT                   /note="Nuclear fusion protein tht1"
FT                   /id="PRO_0000072529"
FT   TOPO_DOM        30..404
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:9442101"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        426..433
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:9442101"
FT   TRANSMEM        434..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        455..470
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:9442101"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        492..577
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:9442101"
FT   CARBOHYD        163
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   577 AA;  66973 MW;  7F7DDCEC99AE45EF CRC64;
     MKFHPTRPFG LYFEFFIIIS FFFTSESTGD VESFMKYSNV AFSEGLAGFD SLAHVYQALL
     KKSTCYQEVA ATLISKCSLL NTELTIDNRI HSAIQMTLCD FERSQILAPS ECVRGSQSEC
     VSKLESTSTW WLSFTSHFHD VNHLCRLANL EMQKELSIEV NMNVTLVQKQ FLEMVILHLR
     NFESVTDKMN QRIDKFDGKF NSVIENSFKD INFRVNQEIM GLVELQNHQQ EGMVQQKEIL
     STIKQLKSEI FDINSFFANF IEESAGYSNS LIEKLNEKFT SENAIALSAI GKYTSEFSAF
     MEKRIKNLIT TTEDSLQQSV QSNIDFVNSG FQPLYDLTIQ LKEELQSLKR LSSEQQNLQH
     EQILQWKSDF LNVSKDHLKV LQQLRPLIDI VEKFMNVYFK GLSNIISSFA FIGFTLFATL
     SSLFFKVLKI HRRPIIVFGS LSIIFIHIYC FKITSWVNLY GWITCTIART LSFIKLNIRT
     FYLTAFLCAL LNFLRYLKYR NSKKDTELSL FLPAPEECNI YHNEHIQVQE DNYLCPIENS
     LIDLFGSENN KEKLGKQENV RFAFLNSESL EQSPWWD
 
 
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