DNI1_SCHPO
ID DNI1_SCHPO Reviewed; 234 AA.
AC O14107;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Cell fusion protein dni1;
DE AltName: Full=Delayed minus-nitrogen induction protein 1;
DE Flags: Precursor;
GN Name=dni1; ORFNames=SPAC31G5.07;
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 [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).
RN [2]
RP INDUCTION, FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19627505; DOI=10.1111/j.1365-2958.2009.06800.x;
RA Clemente-Ramos J.A., Martin-Garcia R., Sharifmoghadam M.R., Konomi M.,
RA Osumi M., Valdivieso M.H.;
RT "The tetraspan protein Dni1p is required for correct membrane organization
RT and cell wall remodelling during mating in Schizosaccharomyces pombe.";
RL Mol. Microbiol. 73:695-709(2009).
CC -!- FUNCTION: Cell membrane protein which plays a relevant role in
CC coordinating membrane organization and cell wall remodeling during
CC mating. {ECO:0000269|PubMed:19627505}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19627505};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19627505}. Cell tip
CC {ECO:0000269|PubMed:19627505}. Note=Localizes to the tip of shmoos
CC which requires fus1, actin and lipid rafts.
CC -!- INDUCTION: Expression is induced during mating.
CC {ECO:0000269|PubMed:19627505}.
CC -!- DISRUPTION PHENOTYPE: Leads to a defect in cell fusion trough defective
CC membrane fusion and organization, as well as cell wall remodeling.
CC {ECO:0000269|PubMed:19627505}.
CC -!- SIMILARITY: Belongs to the SUR7 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11691.2; -; Genomic_DNA.
DR PIR; T38624; T38624.
DR RefSeq; NP_594007.2; NM_001019433.1.
DR AlphaFoldDB; O14107; -.
DR BioGRID; 279597; 3.
DR STRING; 4896.SPAC31G5.07.1; -.
DR PaxDb; O14107; -.
DR EnsemblFungi; SPAC31G5.07.1; SPAC31G5.07.1:pep; SPAC31G5.07.
DR GeneID; 2543166; -.
DR KEGG; spo:SPAC31G5.07; -.
DR PomBase; SPAC31G5.07; dni1.
DR VEuPathDB; FungiDB:SPAC31G5.07; -.
DR HOGENOM; CLU_1185620_0_0_1; -.
DR OMA; FSFCVCG; -.
DR PRO; PR:O14107; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0070867; C:mating projection tip membrane; IDA:PomBase.
DR GO; GO:0000747; P:conjugation with cellular fusion; IBA:GO_Central.
DR GO; GO:0032220; P:plasma membrane fusion involved in cytogamy; IMP:PomBase.
DR GO; GO:0007009; P:plasma membrane organization; IMP:PomBase.
DR InterPro; IPR033481; Dni1/Fig1.
DR PANTHER; PTHR28092; PTHR28092; 1.
DR Pfam; PF12351; Fig1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..234
FT /note="Cell fusion protein dni1"
FT /id="PRO_0000352825"
FT TOPO_DOM 33..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 234 AA; 25388 MW; 408DB5DE49715BB0 CRC64;
MLFLHSVVQG TGTLCTLAAW ILLALVMTGC QSSTTSKFQL FSLATNVAQI NVGYFNMCVL
SANATLICKP QFTGCPGLTS ISLTDVRSKF LINEVHPWMI VFSFCVCGVS FLMGVVSSLP
LIGRLEFLRN IRISLSFFSF FSILVTALFA HVAVSSFVMA VGNGTQNRVT ASLGKKAMIF
LWCSMGLVTL TGITDSIILL VTSRTKKIRK TILEKSKVLT PSSSFSSKSS TTKY
