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};
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; 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