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UniProtKB/Swiss-Prot entry P31178


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GLE_CHLRE
Primary accession number P31178
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 58)
Name and origin of the protein
Protein name Autolysin [Precursor]
Synonyms EC 3.4.24.38
Gametolysin
Gamete lytic enzyme
GLE
Gene name None
From
Chlamydomonas reinhardtii [TaxID: 3055] 
Taxonomy Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 184-203.
PubMed=1584806 [NCBI, ExPASy, EBI, Israel, Japan]
Kinoshita T., Fukuzawa H., Shimada T., Saito T., Matsuda Y.;
"Primary structure and expression of a gamete lytic enzyme in Chlamydomonas reinhardtii: similarity of functional domains to matrix metalloproteases.";
Proc. Natl. Acad. Sci. U.S.A. 89:4693-4697(1992).
Comments
  • FUNCTION: Mediates digestion of the cell walls of the 2 mating type gametes during mating as a necessary prelude to cell fusion. This enzyme acts specifically on the framework proteins (inner wall) of the cell wall, cleaving several model peptides at specific sites.
  • CATALYTIC ACTIVITY: Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-|-Arg-Phe-Ala.
  • COFACTOR: Binds 1 zinc ion per subunit (By similarity).
  • SUBCELLULAR LOCATION: Periplasm. Secreted, cell wall. Note=Stored in the periplasm of gametes until its release. Secreted concurrently with release of the cell walls.
  • INDUCTION: By the signal of flagellar agglutination between gametes of the opposite mating type.
  • DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
  • PTM: Present in 2 forms: an inactive V-form in vegetative cells and an active and soluble G-form. The V-form enzyme may be converted to the G-form enzyme during gametic differentiation under nitrogen-starved conditions.
  • SIMILARITY: Belongs to the peptidase M11 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M94265; AAA33094.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D10542; BAA01400.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45287; A45287.
3D structure databases
ModBase P31178.
Protein family/group databases
MEROPS M11.001; -.
Ontologies
GO
GO:0005618; Cellular component: cell wall (inferred from electronic annotation from UniProtKB-KW).
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0005578; Cellular component: proteinaceous extracellular matrix (inferred from electronic annotation from InterPro).
GO:0004222; Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007047; Biological process: cell wall organization (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001818; Pept_M10A_M12B.
IPR006025; Pept_M_Zn_BS.
IPR008752; Peptidase_M11.
IPR016517; Peptidase_M11_autolysin.
Graphical view of domain structure.
Pfam PF05548; Peptidase_M11; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF007635; Autolysin; 1.
PROSITE PS00546; CYSTEINE_SWITCH; 1.
PS00142; ZINC_PROTEASE; FALSE_NEG.
BLOCKS P31178.
ProtoNet P31178.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Periplasm; Protease; Secreted; Signal; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    28  28     Potential. 
PROPEP   29   183  155     Activation peptide. PRO_0000028870
CHAIN   184   638  455     Autolysin. PRO_0000028871
MOTIF   95   102  8     Cysteine switch (By similarity). 
COMPBIAS   49    62  14     Pro-rich. 
COMPBIAS   271   283  13     Pro-rich. 
ACT_SITE   397   397        By similarity. 
METAL   97    97        Zinc; in inhibited form (By similarity). 
METAL   396   396        Zinc; catalytic (By similarity). 
METAL   400   400        Zinc; catalytic (By similarity). 
METAL   406   406        Zinc; catalytic (By similarity). 
CARBOHYD   30    30        N-linked (GlcNAc...) (Potential). 
CARBOHYD   126   126        N-linked (GlcNAc...) (Potential). 
CARBOHYD   296   296        N-linked (GlcNAc...) (Potential). 
CARBOHYD   458   458        N-linked (GlcNAc...) (Potential). 
CARBOHYD   465   465        N-linked (GlcNAc...) (Potential). 
CARBOHYD   470   470        N-linked (GlcNAc...) (Potential). 
CARBOHYD   523   523        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 638 AA [This is the length of the unprocessed precursor] Molecular weight: 69833 Da [This is the MW of the unprocessed precursor] CRC64: D3E3467701177251 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLATRRFGA AAALLVAACV LCTAPAWAQN ETTGTGMVKT KSAFRWIRPP PARPPPFRRP 

        70         80         90        100        110        120 
PPAQTPYVHK VEYTELQILC PQTIDSVTGY PMDDPRCNVP RATVAAGEEA LTIRNEFELL 

       130        140        150        160        170        180 
NGDVLNVTLE EVDTPENPSR RRLLSIIREE QRTGRVLLAT SAELPTPTFR LKSLKSILKG 

       190        200        210        220        230        240 
SQKEIYAGKP IDLRTIVYIM DFSSCKLSGW SAPATLTPEK VTSDMLRGAS APTNNLANYY 

       250        260        270        280        290        300 
GACSYEKTLF NPDNFLVLGP VPVPCIGGVT PPPRPPRPPR PPPRAGSTIS SLSRRNDTYD 

       310        320        330        340        350        360 
DWWDLSKYCT ASEQQAWERA AEAYAQAIVA QDPNSATGKK LQGILQWRER RRNIYILPPG 

       370        380        390        400        410        420 
VKCSWSGYAD VTCTSATCSA YVRGYSDTNA MQVIMHEAMH NYGLEHAGRG TLEYGDATDV 

       430        440        450        460        470        480 
MGDFNKAGKG LLCPNAPNMY RIGWAKPINE PGVAPFQNAT GAWGNLTAAN FTTDPWIRGL 

       490        500        510        520        530        540 
VIPAQGTRDD NMIVVNVGAQ STRDGAMKAT GAQAYYFSYR IKNTTAGGYD SGLTLDFHKK 

       550        560        570        580        590        600 
VLVHAYNGIQ SERVFGFKSN LLDWGPNFQS RSNTWTSPFL AYNNGLGGGV RLVVQSTSDT 

       610        620        630 
QAVVDICRIS ENGKELSCDD GIDNDCDGLQ DNEDPDCQ 

P31178 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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