PFL8_SCHPO
ID PFL8_SCHPO Reviewed; 385 AA.
AC Q92344;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Putative cell agglutination protein pfl8 {ECO:0000305};
DE AltName: Full=Adhesin pfl8 {ECO:0000303|PubMed:17870620};
DE AltName: Full=Pombe flocculin 8 {ECO:0000303|PubMed:23236291};
DE AltName: Full=Sim4-mal2-associated protein 5 {ECO:0000303|PubMed:16079914};
DE Flags: Precursor;
GN Name=pfl8 {ECO:0000303|PubMed:23236291};
GN Synonyms=fta5 {ECO:0000303|PubMed:16079914}, sma5;
GN ORFNames=SPAC1F8.06 {ECO:0000312|PomBase:SPAC1F8.06};
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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16079914; DOI=10.1038/sj.emboj.7600762;
RA Liu X., McLeod I., Anderson S., Yates J.R. III, He X.;
RT "Molecular analysis of kinetochore architecture in fission yeast.";
RL EMBO J. 24:2919-2930(2005).
RN [3]
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 [4]
RP DOMAIN.
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 [5]
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: Secreted {ECO:0000269|PubMed:16823372}. Cell
CC surface {ECO:0000305|PubMed:17870620}.
CC -!- CAUTION: Was originally thought to be a kinetochore protein, but co-
CC localization has not been confirmed (PubMed:16079914). A more recent
CC study identified it as a secreted protein (PubMed:16823372).
CC {ECO:0000305|PubMed:16079914, ECO:0000305|PubMed:16823372}.
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DR EMBL; CU329670; CAB03600.1; -; Genomic_DNA.
DR PIR; T38113; T38113.
DR RefSeq; NP_592795.1; NM_001018195.2.
DR AlphaFoldDB; Q92344; -.
DR BioGRID; 278345; 7.
DR STRING; 4896.SPAC1F8.06.1; -.
DR MaxQB; Q92344; -.
DR PaxDb; Q92344; -.
DR EnsemblFungi; SPAC1F8.06.1; SPAC1F8.06.1:pep; SPAC1F8.06.
DR GeneID; 2541854; -.
DR KEGG; spo:SPAC1F8.06; -.
DR PomBase; SPAC1F8.06; pfl8.
DR VEuPathDB; FungiDB:SPAC1F8.06; -.
DR eggNOG; ENOG502SWCY; Eukaryota.
DR HOGENOM; CLU_717978_0_0_1; -.
DR InParanoid; Q92344; -.
DR PhylomeDB; Q92344; -.
DR PRO; PR:Q92344; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0010339; C:external side of cell wall; TAS:PomBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000128; P:flocculation; IMP:PomBase.
DR InterPro; IPR018871; GLEYA_adhesin_domain.
DR InterPro; IPR037524; PA14/GLEYA.
DR Pfam; PF10528; GLEYA; 1.
DR PROSITE; PS51820; PA14; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..385
FT /note="Putative cell agglutination protein pfl8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000116633"
FT DOMAIN 196..360
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT REGION 41..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 385 AA; 41001 MW; 88A58F377701F5C4 CRC64;
MNSYISLIFT LLFFTSAARS SSVSVETGSC VRYTTIYSSG SSEFTSTITP ETPSSSSSTF
VPISTHTSSA TNTTSGQLSI SSSSSTSSEY SSSSIPITTV SSSDSFIPSS SQTISASSST
TDNVIVSSSI SSTVSSTPVS TIYSGTSGTT FVSSSTTYQV IPTQICDGVR GLEYAVYNYD
LPSESTFCHP SNGYTEVSTF NKPAYFGSKD LKQSAPLFTG IFSSLDDIPT YSASDYLPAY
PPNPEGMSST SSSCKTIVYQ FFFRVPATDN WSLFVKNVDD AFFGWFGDKA ISGWSNVNYD
AYAHWRIGAY GMGTFDLGYL EQDSFVPVRF VLANGAYIGG FDFAFNSSST GPVRTTSYSY
TSTCDKSFLP FGKGNGGLDE GTANV
