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Protein

Cell wall protein ecm33

Gene

ecm33

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the negative feedback regulation of pmk1 cell integrity signaling and is linked to cellular calcium signaling.1 Publication

GO - Biological processi

  • fungal-type cell wall organization Source: GO_Central
  • intracellular signal transduction Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Cell wall biogenesis/degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Cell wall protein ecm33
Gene namesi
Name:ecm33
ORF Names:SPAC1705.03c, SPAC1F2.01, SPAC23H4.19
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1705.03c.
PomBaseiSPAC1705.03c. ecm33.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei401 – 42121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • cell surface Source: PomBase
  • cytosol Source: PomBase
  • extracellular region Source: UniProtKB-KW
  • fungal-type cell wall Source: PomBase
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell wall, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 398379Cell wall protein ecm33PRO_0000014204Add
BLAST
Propeptidei399 – 42123Removed in mature formSequence analysisPRO_0000417675Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi22 – 221N-linked (GlcNAc...)Sequence analysis
Glycosylationi29 – 291N-linked (GlcNAc...)Sequence analysis
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence analysis
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence analysis
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence analysis
Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence analysis
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence analysis
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence analysis
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence analysis
Lipidationi398 – 3981GPI-anchor amidated serineSequence analysis

Post-translational modificationi

The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).By similarity
Extensively N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiO13960.

Expressioni

Inductioni

Expression is under the control of atf1 and mbx1 via the putative cAMP-responsive element (CRE) sequence TTACAGTAA and the RLM1-binding sequence GTATATATAG in the promoter region.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi280614. 10 interactions.
IntActiO13960. 1 interaction.
MINTiMINT-4669337.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi380 – 39415Poly-SerAdd
BLAST

Sequence similaritiesi

Belongs to the SPS2 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiO13960.
OMAiHENELDS.
OrthoDBiEOG79KPR9.
PhylomeDBiO13960.

Family and domain databases

Gene3Di3.80.20.20. 1 hit.
InterProiIPR032675. L_dom-like.
IPR000494. Rcpt_L-dom.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O13960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFKSFALTL LFAAARVQAA SNCSSGPYNI SAQGTLDELN SCTVLNGDLY
60 70 80 90 100
ISDAGNSGIT TLTVNGIESV QGDVVVSDGQ YLTSLSFPSL KNVSGAFNVN
110 120 130 140 150
NMIRMNNLAT PELTSVGSLN LAVLPNLQEL QFNAGLSDSD SVVIDDTQLQ
160 170 180 190 200
AIDGISLDSV TTFQVTNNRY IQEITMEGLE SAQNIQISAN SKGVSVNFSK
210 220 230 240 250
LSNVTTATFD GISNVFIGNL KSAAGNLYFS NTTLDNISVP YLTEIGQSFA
260 270 280 290 300
VLYSPELTSL NFPNLTTVGG GFVINDTGLT SIDGFPVISE IGGGLVLLGN
310 320 330 340 350
FSSIDMPDLS DVKGALTVET KATNFTCPWS NDDSVIKGDD FTCQGSVATI
360 370 380 390 400
SATSSYDLSS TVSATSGSAT SATGSATTTS YSSDSSASSS SSSSHESSAA
410 420
SNGFTAGALV LGSLLVAALA M
Length:421
Mass (Da):43,346
Last modified:June 1, 1998 - v2
Checksum:iA349C6D8501D8A29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98976 Genomic DNA. Translation: CAB11655.3.
CU329670 Genomic DNA. Translation: CAB86946.1.
PIRiT38309.
RefSeqiXP_001713055.1. XM_001713003.2.

Genome annotation databases

EnsemblFungiiSPAC1705.03c.1; SPAC1705.03c.1:pep; SPAC1705.03c.
GeneIDi3361538.
KEGGispo:SPAC1705.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98976 Genomic DNA. Translation: CAB11655.3.
CU329670 Genomic DNA. Translation: CAB86946.1.
PIRiT38309.
RefSeqiXP_001713055.1. XM_001713003.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280614. 10 interactions.
IntActiO13960. 1 interaction.
MINTiMINT-4669337.

Proteomic databases

MaxQBiO13960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1705.03c.1; SPAC1705.03c.1:pep; SPAC1705.03c.
GeneIDi3361538.
KEGGispo:SPAC1705.03c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1705.03c.
PomBaseiSPAC1705.03c. ecm33.

Phylogenomic databases

InParanoidiO13960.
OMAiHENELDS.
OrthoDBiEOG79KPR9.
PhylomeDBiO13960.

Miscellaneous databases

PROiO13960.

Family and domain databases

Gene3Di3.80.20.20. 1 hit.
InterProiIPR032675. L_dom-like.
IPR000494. Rcpt_L-dom.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Mass spectrometric identification of covalently bound cell wall proteins from the fission yeast Schizosaccharomyces pombe."
    de Groot P.W.J., Yin Q.Y., Weig M., Sosinska G.J., Klis F.M., de Koster C.G.
    Yeast 24:267-278(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  3. "The cell surface protein gene ecm33+ is a target of the two transcription factors Atf1 and Mbx1 and negatively regulates Pmk1 MAPK cell integrity signaling in fission yeast."
    Takada H., Nishida A., Domae M., Kita A., Yamano Y., Uchida A., Ishiwata S., Fang Y., Zhou X., Masuko T., Kinoshita M., Kakehi K., Sugiura R.
    Mol. Biol. Cell 21:674-685(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, SUBCELLULAR LOCATION, FUNCTION.

Entry informationi

Entry nameiECM33_SCHPO
AccessioniPrimary (citable) accession number: O13960
Secondary accession number(s): O13887, Q9P7A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.