ECM33_SCHPO
ID ECM33_SCHPO Reviewed; 421 AA.
AC O13960; O13887; Q9P7A7;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Cell wall protein ecm33;
DE Flags: Precursor;
GN Name=ecm33; ORFNames=SPAC1705.03c, SPAC1F2.01, SPAC23H4.19;
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, AND SUBCELLULAR LOCATION.
RX PubMed=17230583; DOI=10.1002/yea.1443;
RA de Groot P.W.J., Yin Q.Y., Weig M., Sosinska G.J., Klis F.M.,
RA de Koster C.G.;
RT "Mass spectrometric identification of covalently bound cell wall proteins
RT from the fission yeast Schizosaccharomyces pombe.";
RL Yeast 24:267-278(2007).
RN [3]
RP INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20032302; DOI=10.1091/mbc.e09-09-0810;
RA Takada H., Nishida A., Domae M., Kita A., Yamano Y., Uchida A.,
RA Ishiwata S., Fang Y., Zhou X., Masuko T., Kinoshita M., Kakehi K.,
RA Sugiura R.;
RT "The cell surface protein gene ecm33+ is a target of the two transcription
RT factors Atf1 and Mbx1 and negatively regulates Pmk1 MAPK cell integrity
RT signaling in fission yeast.";
RL Mol. Biol. Cell 21:674-685(2010).
CC -!- FUNCTION: Involved in the negative feedback regulation of pmk1 cell
CC integrity signaling and is linked to cellular calcium signaling.
CC {ECO:0000269|PubMed:20032302}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Secreted, cell wall {ECO:0000269|PubMed:17230583,
CC ECO:0000269|PubMed:20032302}.
CC -!- INDUCTION: Expression is under the control of atf1 and mbx1 via the
CC putative cAMP-responsive element (CRE) sequence TTACAGTAA and the RLM1-
CC binding sequence GTATATATAG in the promoter region.
CC {ECO:0000269|PubMed:20032302}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Extensively N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPS2 family. {ECO:0000305}.
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DR EMBL; Z98976; CAB11655.3; -; Genomic_DNA.
DR EMBL; CU329670; CAB86946.1; -; Genomic_DNA.
DR PIR; T38309; T38309.
DR RefSeq; XP_001713055.1; XM_001713003.2.
DR AlphaFoldDB; O13960; -.
DR SMR; O13960; -.
DR BioGRID; 280614; 11.
DR IntAct; O13960; 1.
DR MINT; O13960; -.
DR STRING; 4896.SPAC1705.03c.1; -.
DR MaxQB; O13960; -.
DR PaxDb; O13960; -.
DR EnsemblFungi; SPAC1705.03c.1; SPAC1705.03c.1:pep; SPAC1705.03c.
DR PomBase; SPAC1705.03c; ecm33.
DR VEuPathDB; FungiDB:SPAC1705.03c; -.
DR eggNOG; ENOG502QUZC; Eukaryota.
DR HOGENOM; CLU_035846_0_1_1; -.
DR InParanoid; O13960; -.
DR OMA; DELNSCT; -.
DR PhylomeDB; O13960; -.
DR PRO; PR:O13960; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; NAS:PomBase.
DR GO; GO:0009986; C:cell surface; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IGI:PomBase.
DR Gene3D; 3.80.20.20; -; 1.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..398
FT /note="Cell wall protein ecm33"
FT /id="PRO_0000014204"
FT PROPEP 399..421
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000417675"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 365..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 398
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 421 AA; 43346 MW; A349C6D8501D8A29 CRC64;
MLFKSFALTL LFAAARVQAA SNCSSGPYNI SAQGTLDELN SCTVLNGDLY ISDAGNSGIT
TLTVNGIESV QGDVVVSDGQ YLTSLSFPSL KNVSGAFNVN NMIRMNNLAT PELTSVGSLN
LAVLPNLQEL QFNAGLSDSD SVVIDDTQLQ AIDGISLDSV TTFQVTNNRY IQEITMEGLE
SAQNIQISAN SKGVSVNFSK LSNVTTATFD GISNVFIGNL KSAAGNLYFS NTTLDNISVP
YLTEIGQSFA VLYSPELTSL NFPNLTTVGG GFVINDTGLT SIDGFPVISE IGGGLVLLGN
FSSIDMPDLS DVKGALTVET KATNFTCPWS NDDSVIKGDD FTCQGSVATI SATSSYDLSS
TVSATSGSAT SATGSATTTS YSSDSSASSS SSSSHESSAA SNGFTAGALV LGSLLVAALA
M
