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PFL9_SCHPO
ID   PFL9_SCHPO              Reviewed;         326 AA.
AC   Q9P7Q2;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Putative cell agglutination protein pfl9 {ECO:0000305};
DE   AltName: Full=Adhesin pfl9 {ECO:0000303|PubMed:17870620};
DE   AltName: Full=Pombe flocculin 9 {ECO:0000303|PubMed:23236291};
DE   Flags: Precursor;
GN   Name=pfl9 {ECO:0000303|PubMed:23236291};
GN   ORFNames=SPAC186.01 {ECO:0000312|PomBase:SPAC186.01};
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.
RX   PubMed=12738880; DOI=10.1073/pnas.1030497100;
RA   Samuelsen C.O., Baraznenok V., Khorosjutina O., Spaehr H., Kieselbach T.,
RA   Holmberg S., Gustafsson C.M.;
RT   "TRAP230/ARC240 and TRAP240/ARC250 Mediator subunits are functionally
RT   conserved through evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:6422-6427(2003).
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).
RN   [4]
RP   FUNCTION.
RX   PubMed=23236291; DOI=10.1371/journal.pgen.1003104;
RA   Kwon E.J., Laderoute A., Chatfield-Reed K., Vachon L., Karagiannis J.,
RA   Chua G.;
RT   "Deciphering the transcriptional-regulatory network of flocculation in
RT   Schizosaccharomyces pombe.";
RL   PLoS Genet. 8:E1003104-E1003104(2012).
CC   -!- FUNCTION: May be involved in agglutination during conjugation or other
CC       aspects of colony formation (By similarity). Induces flocculation when
CC       overexpressed (PubMed:23236291). {ECO:0000250|UniProtKB:O74346,
CC       ECO:0000269|PubMed:23236291}.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000305}.
CC   -!- INDUCTION: Repressed by the srb8 and srb9 transcription factors.
CC       {ECO:0000269|PubMed:12738880}.
CC   -!- SIMILARITY: Belongs to the mam3/map4 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01169}.
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DR   EMBL; CU329670; CAB75865.1; -; Genomic_DNA.
DR   PIR; T50128; T50128.
DR   RefSeq; NP_595019.1; NM_001020450.2.
DR   AlphaFoldDB; Q9P7Q2; -.
DR   BioGRID; 278914; 27.
DR   STRING; 4896.SPAC186.01.1; -.
DR   PaxDb; Q9P7Q2; -.
DR   EnsemblFungi; SPAC186.01.1; SPAC186.01.1:pep; SPAC186.01.
DR   GeneID; 2542453; -.
DR   KEGG; spo:SPAC186.01; -.
DR   PomBase; SPAC186.01; pfl9.
DR   VEuPathDB; FungiDB:SPAC186.01; -.
DR   HOGENOM; CLU_774238_0_0_1; -.
DR   PRO; PR:Q9P7Q2; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0010339; C:external side of cell wall; TAS:PomBase.
DR   GO; GO:0000128; P:flocculation; IMP:PomBase.
DR   InterPro; IPR021746; DIPSY.
DR   Pfam; PF11763; DIPSY; 1.
DR   PROSITE; PS51825; DIPSY; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..326
FT                   /note="Putative cell agglutination protein pfl9"
FT                   /id="PRO_0000353815"
FT   REPEAT          103..137
FT                   /note="1"
FT                   /evidence="ECO:0000305|PubMed:17870620"
FT   REPEAT          138..175
FT                   /note="2"
FT                   /evidence="ECO:0000305|PubMed:17870620"
FT   DOMAIN          164..326
FT                   /note="DIPSY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01169"
FT   REGION          103..175
FT                   /note="2 X 36 AA approximate tandem repeats"
FT                   /evidence="ECO:0000305|PubMed:17870620"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   326 AA;  35266 MW;  BE7B7751D652346C CRC64;
     MNVVKYIIFS FALAPLLLVN ANTYNFTQIQ KRSVNQAVLE SSQDTNSVGG EASSTACPLF
     TTIYTNGITP GTTTIYPTSI STSGVSSNNI DETSVSSESI ITSTITTTIT SGSQLYTTTI
     TGQNTPVDTV EVVIPTAGTF TTTLTSGSSY PVATTTVRTA SGTQSGEVEV ITPSCGCSPE
     NSFHLKIDND KISPSYVYMD PNAPVRTNGA GREGNMFAST NGDNEGLNLF YYDSTIQRVL
     TCDCQRPSYT VYIEDPIIGN GFSSAWNLIK NSDGIFTPVE SRNNEPLHFH VDNNGRVWMT
     SQEYDTEVSS TDERNFRAND VTLQLY
 
 
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