ISP3_SCHPO
ID ISP3_SCHPO Reviewed; 182 AA.
AC P40899; Q92343; Q96VC0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Spore wall structural constituent isp3 {ECO:0000312|PomBase:SPAC1F8.05};
DE AltName: Full=Meiotic expression up-regulated protein 4;
DE AltName: Full=Sexual differentiation process protein isp3;
GN Name=isp3; Synonyms=meu4; ORFNames=SPAC1F8.05;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=7954893; DOI=10.1007/bf00326301;
RA Sato S., Suzuki H., Widyastuti U., Hotta Y., Tabata S.;
RT "Identification and characterization of genes induced during sexual
RT differentiation in Schizosaccharomyces pombe.";
RL Curr. Genet. 26:31-37(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD16-1;
RX PubMed=11376151; DOI=10.1093/nar/29.11.2327;
RA Watanabe T., Miyashita K., Saito T.T., Yoneki T., Kakihara Y.,
RA Nabeshima K., Kishi Y.A., Shimoda C., Nojima H.;
RT "Comprehensive isolation of meiosis-specific genes identifies novel
RT proteins and unusual non-coding transcripts in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 29:2327-2337(2001).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-7, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=24623719; DOI=10.1091/mbc.e13-12-0731;
RA Fukunishi K., Miyakubi K., Hatanaka M., Otsuru N., Hirata A., Shimoda C.,
RA Nakamura T.;
RT "The fission yeast spore is coated by a proteinaceous surface layer
RT comprising mainly Isp3.";
RL Mol. Biol. Cell 25:1549-1559(2014).
RN [5]
RP DEVELOPMENTAL STAGE, AND PALMITOYLATION.
RX PubMed=23843742; DOI=10.1371/journal.pbio.1001597;
RA Zhang M.M., Wu P.Y., Kelly F.D., Nurse P., Hang H.C.;
RT "Quantitative control of protein S-palmitoylation regulates meiotic entry
RT in fission yeast.";
RL PLoS Biol. 11:e1001597-e1001597(2013).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=33375328; DOI=10.3390/jof7010007;
RA Tahara Y.O., Miyata M., Nakamura T.;
RT "Quick-Freeze, Deep-Etch Electron Microscopy Reveals the Characteristic
RT Architecture of the Fission Yeast Spore.";
RL J. Fungi 7:jof7010007-jof7010007(2020).
CC -!- FUNCTION: Forms fibrillar structures on the spore surface that
CC contribute to spore wall integrity. {ECO:0000269|PubMed:24623719,
CC ECO:0000269|PubMed:33375328}.
CC -!- SUBCELLULAR LOCATION: Spore coat {ECO:0000269|PubMed:24623719,
CC ECO:0000269|PubMed:33375328}. Cytoplasm {ECO:0000269|PubMed:24623719}.
CC -!- DEVELOPMENTAL STAGE: Expressed during sporulation (at protein level)
CC (PubMed:24623719, PubMed:23843742). Expressed during meiosis from the
CC first meiotic nuclear division (PubMed:7954893).
CC {ECO:0000269|PubMed:23843742, ECO:0000269|PubMed:24623719,
CC ECO:0000269|PubMed:7954893}.
CC -!- PTM: Palmitoylated by the erf2-erf4 complex.
CC {ECO:0000269|PubMed:23843742}.
CC -!- DISRUPTION PHENOTYPE: Fibrillar structures absent from spore coat
CC (PubMed:33375328). Increased rate of spore wall collapse during
CC germination (PubMed:33375328). Spores sensitive to thermal stress,
CC ethanol, and cell wall degrading enzymes (PubMed:24623719). Normal rate
CC of spore formation resulting in spores of a normal size
CC (PubMed:24623719). {ECO:0000269|PubMed:24623719,
CC ECO:0000269|PubMed:33375328}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71778.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D14060; BAA03146.1; -; mRNA.
DR EMBL; AB061240; BAB71778.1; ALT_FRAME; mRNA.
DR EMBL; CU329670; CAB03599.1; -; Genomic_DNA.
DR PIR; S45494; S45494.
DR PIR; T38112; T38112.
DR RefSeq; NP_592794.1; NM_001018194.2.
DR AlphaFoldDB; P40899; -.
DR BioGRID; 278369; 3.
DR STRING; 4896.SPAC1F8.05.1; -.
DR SwissPalm; P40899; -.
DR PaxDb; P40899; -.
DR EnsemblFungi; SPAC1F8.05.1; SPAC1F8.05.1:pep; SPAC1F8.05.
DR GeneID; 2541879; -.
DR KEGG; spo:SPAC1F8.05; -.
DR PomBase; SPAC1F8.05; isp3.
DR VEuPathDB; FungiDB:SPAC1F8.05; -.
DR HOGENOM; CLU_1482817_0_0_1; -.
DR PRO; PR:P40899; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990916; C:Isp3 layer of spore wall; IDA:UniProtKB.
DR GO; GO:1990915; F:structural constituent of ascospore wall; IDA:PomBase.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Reference proteome; Sporulation.
FT CHAIN 1..182
FT /note="Spore wall structural constituent isp3"
FT /id="PRO_0000084260"
FT REGION 33..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 3
FT /note="Missing (in Ref. 2; BAB71778)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..76
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 19696 MW; AF3F86BC1EB8C2DA CRC64;
MGLGNLCSYK QDDSLDILQK KVLIDAFNKV TIDGKPNVQH QQPTYWYPPP PPRHHKEHKK
SHHHWEYSSD DDSSDDEESC EKKKPKCCEK KKPKCCESEQ NNGCGRRNQL ARRLAFLGSF
GDGDCDGCNE AFTVTGPITY FRTCPDPLTG ITPAVAAAAA TPAAAATPAT PAAAATPAAP
AA
