MAP4_SCHPO
ID MAP4_SCHPO Reviewed; 948 AA.
AC O74346;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=P cell-type agglutination protein map4 {ECO:0000305};
DE AltName: Full=Adhesin map4 {ECO:0000303|PubMed:16857197};
DE Flags: Precursor;
GN Name=map4 {ECO:0000303|PubMed:16857197};
GN ORFNames=SPBC21D10.06c {ECO:0000312|PomBase:SPBC21D10.06c};
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16857197; DOI=10.1016/j.febslet.2006.07.016;
RA Sharifmoghadam M.R., Bustos-Sanmamed P., Valdivieso M.-H.;
RT "The fission yeast Map4 protein is a novel adhesin required for mating.";
RL FEBS Lett. 580:4457-4462(2006).
RN [3]
RP DOMAIN, AND 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: P cell-type specific protein which involved in agglutination
CC during conjugation. {ECO:0000269|PubMed:16857197}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16857197}.
CC Note=Localizes at the mating projection tip.
CC {ECO:0000269|PubMed:16857197}.
CC -!- MISCELLANEOUS: According to PubMed:16857197 the number of the
CC intragenic tandem repeats for map4 is 9 rather than the 5 annotated in
CC the reference sequence, producing a protein of 1092 amino acids.
CC {ECO:0000305|PubMed:16857197}.
CC -!- SIMILARITY: Belongs to the mam3/map4 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01169}.
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DR EMBL; CU329671; CAA20762.1; -; Genomic_DNA.
DR PIR; T11678; T11678.
DR RefSeq; NP_596007.1; NM_001021915.2.
DR AlphaFoldDB; O74346; -.
DR STRING; 4896.SPBC21D10.06c.1; -.
DR PaxDb; O74346; -.
DR EnsemblFungi; SPBC21D10.06c.1; SPBC21D10.06c.1:pep; SPBC21D10.06c.
DR GeneID; 2540608; -.
DR KEGG; spo:SPBC21D10.06c; -.
DR PomBase; SPBC21D10.06c; map4.
DR VEuPathDB; FungiDB:SPBC21D10.06c; -.
DR HOGENOM; CLU_310385_0_0_1; -.
DR InParanoid; O74346; -.
DR OMA; SIQGDPN; -.
DR PRO; PR:O74346; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0070263; C:external side of fungal-type cell wall; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
DR InterPro; IPR021746; DIPSY.
DR Pfam; PF11763; DIPSY; 1.
DR PROSITE; PS51825; DIPSY; 1.
PE 3: Inferred from homology;
KW Conjugation; Glycoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..948
FT /note="P cell-type agglutination protein map4"
FT /id="PRO_0000353808"
FT REPEAT 617..652
FT /note="1"
FT /evidence="ECO:0000305|PubMed:16857197"
FT REPEAT 653..688
FT /note="2"
FT /evidence="ECO:0000305|PubMed:16857197"
FT REPEAT 689..724
FT /note="3"
FT /evidence="ECO:0000305|PubMed:16857197"
FT REPEAT 725..760
FT /note="4"
FT /evidence="ECO:0000305|PubMed:16857197"
FT REPEAT 761..796
FT /note="5"
FT /evidence="ECO:0000305|PubMed:16857197"
FT DOMAIN 796..948
FT /note="DIPSY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01169"
FT REGION 136..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..796
FT /note="5 X 36 AA approximate tandem repeats"
FT /evidence="ECO:0000305|PubMed:16857197"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 684
FT /note="D -> DVPTPSWVTETVTSGSVEFTTTIATPVGTTAGTVVVDIPTPSWVTET
FT VTSGSVGFTTTIATPIGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTITTPVGSTAGTV
FT LVDIPTPSWVTETVTSGSVEFTTTIATPVGSTAGTVLVD (in Ref. 2; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 948 AA; 98664 MW; 173705578FEB5C22 CRC64;
MNSYAILLSL FFSFERLLTL ANANSLYSPF NNSSFVDSDT SFSDLSRNGL LSLLDSNTTS
ASVQTIAISQ TDNAASCIPS ASLLSSSVVL YSAKETVTVS SYWSLVSTSV TGTVYVPYTS
SVACFPYATS DAPNPIPRGD SATSTSIAPT YSASDSSATT ITSSSPSTSI IGTGSTDTSV
SSTLTYHTPI ASPTTSSNSD NEYTVDVITS SSLSSFVITN VDSTTTSVIN YIGASTLESS
SLTNTVSPTE STFYETKSST SSVPTQTIDS SSFTSSTPVS LTSSSTSSSG SSQDSTTIDS
TPSTIATSTL QPTTSSPITT SAPSLSSALP TTYPSSLSTE VEVEYFTKTI TDTSSIVTYS
TGVETLYETE TITSSEISSI IYNFSTPISG SSFPDGFKPI NPTSFPSLTS STKKIPSTTL
PTSSKMITTT TPSVSNNTQS SFLIISTFTS SYEHSEPFKV SSVPLTSNNF SSISHSSASS
LPITPSSYLS NTTLHSSVQS SQSSQFTVSV PSSTQSYSTS SNFTTPITIS TSLSSFPTTI
VSSSFQYSSL SSNVTTTNAQ SSSLSSSNSS ALTHISSSIV SSGSSSALSS STIVSSINSS
SSVFISSVSS SLQYSSSYVT ETTTSGSVGF TTTIATPVGS TAGTVVVDIP TPSWVTETVT
SGSVGFTTTI ATPVGSTAGT VLVDIPTPSW VTETVTSGSV EFTTTIATPV GTTAGTVVVD
IPTPSWVTET VTSGSVGFTT TIATPIGTTA GTVLVDIPTP SWVTETVTSG SVGFTTTIAT
PVGTTAGTVL IDVPTPTASS SPFPSCNTQC TNENSFRIQV INDDIYPSYV HLDSNNYAIA
AARGDSDGEN VFIYDSDIKR IVSCCGVKPI YRLDQDDTEG YSFEIYKDND GQLQFKYPLN
DALYPMELLT LTDGRIGITT NLTLYKPYYL NNVENERAAN VVLRALEY
