MAM3_SCHPO
ID MAM3_SCHPO Reviewed; 1082 AA.
AC Q9HDY9; Q9HDY8;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=M cell-type agglutination protein mam3 {ECO:0000305};
DE AltName: Full=Adhesin mam3 {ECO:0000303|PubMed:17870620};
DE Flags: Precursor;
GN Name=mam3 {ECO:0000303|PubMed:17032641};
GN ORFNames=SPAP11E10.02c {ECO:0000312|PomBase:SPAP11E10.02c}, SPAPB1A10.01c;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION.
RX PubMed=17032641; DOI=10.1073/pnas.0603403103;
RA Mata J., Baehler J.;
RT "Global roles of Ste11p, cell type, and pheromone in the control of gene
RT expression during early sexual differentiation in fission yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15517-15522(2006).
RN [4]
RP REPEATS.
RX PubMed=17870620; DOI=10.1016/j.fgb.2007.08.002;
RA Linder T., Gustafsson C.M.;
RT "Molecular phylogenetics of ascomycotal adhesins--a novel family of
RT putative cell-surface adhesive proteins in fission yeasts.";
RL Fungal Genet. Biol. 45:485-497(2008).
CC -!- FUNCTION: M cell-type specific protein involved in agglutination during
CC conjugation. {ECO:0000269|PubMed:17032641}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the mam3/map4 family. {ECO:0000305}.
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DR EMBL; CU329670; CAC19750.1; -; Genomic_DNA.
DR RefSeq; XP_001713059.1; XM_001713007.2.
DR AlphaFoldDB; Q9HDY9; -.
DR BioGRID; 280593; 11.
DR STRING; 4896.SPAP11E10.02c.1; -.
DR PaxDb; Q9HDY9; -.
DR EnsemblFungi; SPAP11E10.02c.1; SPAP11E10.02c.1:pep; SPAP11E10.02c.
DR PomBase; SPAP11E10.02c; mam3.
DR VEuPathDB; FungiDB:SPAP11E10.02c; -.
DR HOGENOM; CLU_285927_0_0_1; -.
DR InParanoid; Q9HDY9; -.
DR OMA; PNTGAEW; -.
DR PRO; PR:Q9HDY9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0070263; C:external side of fungal-type cell wall; IMP:PomBase.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
PE 3: Inferred from homology;
KW Conjugation; Glycoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1082
FT /note="M cell-type agglutination protein mam3"
FT /id="PRO_0000014210"
FT REPEAT 646..681
FT /note="1"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 682..717
FT /note="2"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 718..753
FT /note="3"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 754..789
FT /note="4"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 790..825
FT /note="5"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 826..861
FT /note="6"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 862..897
FT /note="7"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 898..933
FT /note="8"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 934..969
FT /note="9"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 970..1005
FT /note="10"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REPEAT 1006..1041
FT /note="11"
FT /evidence="ECO:0000305|PubMed:17870620"
FT REGION 353..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..1043
FT /note="11 X 36 AA approximate tandem repeats"
FT /evidence="ECO:0000305|PubMed:17870620"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1082 AA; 109143 MW; 76CD8274B04C2F82 CRC64;
MSIALAFFIL VLLGFSWASP SALDDTFNVS RSVGLISSSN LESCQSSPLE VGNIYNSTSA
SEILSTLDAK YITIIGVIGS SNSSIQDLID SVGNSNNAAS SNPTSTVTEY VDRVQTVTEY
VTLSCGQAFT STVDISSSTS SSVINSPTGT AVSSQISTLS MSPSSTPVFS PSASVSSKVA
SSVSYVSSEP SDSSSSTNTV ILTTSVNSPA VSSSETLTSV SITSTESAYT SSSVDIAAST
TASSTLPVST SEATVSFSTD IPATPSTLSS PASSSSSYLV ETSSTLTDSV FTTVTATSDS
SVITYTLINS VTSSSETTNL PSSSSSLVTI GESSFPSSLL SLLTQSFSTV RSTSSSSTDQ
LTSASPISSS VISPSVSSPT SSILTNSGSI KSGDHQIVTT SFVQTTTHGS QVETLTYVTT
LTETILTTTY DSHTFLTTIT PSPSNSISYT NNTFIPSSSI KSSIVYSVTP TSAENYTSSE
AFSTSSSLVV IPPVNSSLVT SSTSFTKFSS LSSSQLSTEN FTSASSSLSL TNAKSSLSTP
STTIPTSNSS VSLQTSSSLI ISSPIISSSL TATSTSTPAL THSITPSNTS YTSSLIPSSS
TDYSSSLITV CSNVTSEISS TSLASLISTL TSQQISSNKS SEFVGQTTTE YTTSGSVGFT
TTLATQSGSV PGTVLVDVPT PSWITETVTS GSVGFTTTIA TPIGTTAGTV LVDIPTPSWV
TETVTSGSIG FTTTIATPIG STAGTVLVDV PTPSWVTETV TSGSVGFTTT IATPIGSTAG
TVLVDIPTPS WVTETVTSGS VGFTTTIATP VGTTAGTVLV DIPTPSWVTE TVTSGSVGFT
TTIATPVGTT AGTVVVDVPT PSWVTETVTS GSVGFTTTIA TPIGSTAGTV LVDIPTPSWV
TETVTSGSVG FTTTIATPVG TTAGTVLVDI PTPSWVTETV TSGSVGFTTT IATPIGTTAG
TVLVDIPTPS WVTETVTSGS VGFTTTIATP VGTTAGTVLV DIPTPSWVTE TVTSGSVGFT
TTIATPIGTT AGTVLVDIPQ QHATTTTTTT FDGFSGYTSS YTGSITETIV IGTPHHSVVD
VS
