PFL2_SCHPO
ID PFL2_SCHPO Reviewed; 1036 AA.
AC Q8TFG9; P78869; Q8TFG2;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 3.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Putative GPI-anchored protein pfl2 {ECO:0000305};
DE AltName: Full=Pombe flocculin 2 {ECO:0000303|PubMed:23236291};
DE Flags: Precursor;
GN Name=pfl2 {ECO:0000303|PubMed:23236291};
GN ORFNames=SPAPB15E9.01c {ECO:0000312|PomBase:SPAPB15E9.01c}, SPAPB18E9.06c;
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 [LARGE SCALE MRNA] OF 718-1036.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
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 membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
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DR EMBL; CU329670; CAD27472.2; -; Genomic_DNA.
DR EMBL; D89219; BAA13880.1; -; mRNA.
DR PIR; T43040; T43040.
DR RefSeq; XP_001713096.1; XM_001713044.2.
DR AlphaFoldDB; Q8TFG9; -.
DR BioGRID; 858075; 1.
DR STRING; 4896.SPAPB15E9.01c.1; -.
DR PaxDb; Q8TFG9; -.
DR EnsemblFungi; SPAPB15E9.01c.1; SPAPB15E9.01c.1:pep; SPAPB15E9.01c.
DR PomBase; SPAPB15E9.01c; pfl2.
DR VEuPathDB; FungiDB:SPAPB15E9.01c; -.
DR HOGENOM; CLU_293405_0_0_1; -.
DR OMA; ATEWTTK; -.
DR PRO; PR:Q8TFG9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS:PomBase.
DR GO; GO:0098631; F:cell adhesion mediator activity; ISS:PomBase.
DR GO; GO:0000128; P:flocculation; IMP:PomBase.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1011
FT /note="Putative GPI-anchored protein pfl2"
FT /id="PRO_0000014212"
FT PROPEP 1012..1036
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000415888"
FT REGION 88..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1011
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 918
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 924
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 930
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 947
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 858..859
FT /note="TA -> SV (in Ref. 2; BAA13880)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="N -> Y (in Ref. 2; BAA13880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1036 AA; 99496 MW; C2C2A81D4AB71CE5 CRC64;
MKFFTASTLF LLAAQSLNSG VSASLSDPAN TPTILADDIV HGYTPATYLS SVPTLLKRAT
TSYNYNTSSA SSSSLTSSSA ASSSLTSSSS LASSSTNSTT SASPTSSSLT SSSATSSSLA
SSSTTSSSLA SSSITSSSLA SSSITSSSLA SSSTTSSSLA SSSTNSTTSA TPTSSATSSS
LSSTAASNSA TSSSLASSSL NSTTSATATS SSLSSTAASN SATSSSLASS SLNSTTSATA
TSSSISSTVS SSTPLTSSNS TTAATSASAT SSSAQYNTSS LLPSSTPSST PLSSANSTTA
TSASSTPLTS VNSTTTTSAS STPLSSVSSA NSTTATSTSS TPLSSVNSTT ATSASSTPLT
SVNSTTATSA SSTPLTSVNS TSATSASSTP LTSANSTTST SVSSTAPSYN TSSVLPTSSV
SSTPLSSANS TTATSASSTP LSSVNSTTAT SASSTPLSSV NSTTATSASS TPLTSVNSTT
ATSASSTPLT SVNSTSATSA SSTPLTSANS TTSTSVSSTA PSYNTSSVLP TSSVSSTPLS
SANSTTATSA SSTPLTSVNS TTATSASSTP FGNSTITSSA SGSTGEFTNT NSGNGDVSGS
VTTPTSTPLS NSTVAPTSTF TSSGFNTTSG LPTSSASTPL SNSTVAPTST FTSSGFNTTS
GLPTSSASTP SSNSSIVPTS TFTSSGFNTT SGLPTSSAST PLSNSTVAPT STFTSSGFNT
TSGLPTSSVS TPLSNSSAYP SSGSSTFSRL SSTLTSSIIP TETFGSTSGS ATGTRPTGSS
SQGSVVPTTS TGSSVTSTGT GTTTGVTEVT ETSTFETTEI ITSTIEPTTA SGTGGGNPTA
APTNEPTVTT GTETTEGTAT YTEPTTFTST FSFTTTIIGG TTTIIPVNPG NPSSSVSAPP
TTSFTPGPGG SGYPSYSNTT QGMNTTSIWN SSNSTIVSNV TATITGNVTI TTGDLTTIDP
TTFTSTYLSS GFQTVSNTTA TSGSDDDVKT ASTSSSTSYT SSSSSSSSTT SAASSKASVS
MGLNGLMIAA VILLVA
