位置:首页 > 蛋白库 > GLE_CHLRE
GLE_CHLRE
ID   GLE_CHLRE               Reviewed;         638 AA.
AC   P31178;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Autolysin;
DE            EC=3.4.24.38;
DE   AltName: Full=Gamete lytic enzyme;
DE            Short=GLE;
DE   AltName: Full=Gametolysin;
DE   Flags: Precursor;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 184-203.
RX   PubMed=1584806; DOI=10.1073/pnas.89.10.4693;
RA   Kinoshita T., Fukuzawa H., Shimada T., Saito T., Matsuda Y.;
RT   "Primary structure and expression of a gamete lytic enzyme in Chlamydomonas
RT   reinhardtii: similarity of functional domains to matrix metalloproteases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:4693-4697(1992).
CC   -!- FUNCTION: Mediates digestion of the cell walls of the 2 mating type
CC       gametes during mating as a necessary prelude to cell fusion. This
CC       enzyme acts specifically on the framework proteins (inner wall) of the
CC       cell wall, cleaving several model peptides at specific sites.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of the proline- and hydroxyproline-rich proteins of
CC         the Chlamydomonas cell wall. Also cleaves azocasein, gelatin and Leu-
CC         Trp-Met-|-Arg-Phe-Ala.; EC=3.4.24.38;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Periplasm. Secreted, cell wall. Note=Stored in
CC       the periplasm of gametes until its release. Secreted concurrently with
CC       release of the cell walls.
CC   -!- INDUCTION: By the signal of flagellar agglutination between gametes of
CC       the opposite mating type.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC       binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC       dissociation of the cysteine from the zinc ion upon the activation-
CC       peptide release activates the enzyme.
CC   -!- PTM: Present in 2 forms: an inactive V-form in vegetative cells and an
CC       active and soluble G-form. The V-form enzyme may be converted to the G-
CC       form enzyme during gametic differentiation under nitrogen-starved
CC       conditions.
CC   -!- SIMILARITY: Belongs to the peptidase M11 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M94265; AAA33094.1; -; mRNA.
DR   EMBL; D10542; BAA01400.1; -; mRNA.
DR   PIR; A45287; A45287.
DR   AlphaFoldDB; P31178; -.
DR   STRING; 3055.EDO96296; -.
DR   MEROPS; M11.001; -.
DR   EnsemblPlants; PNW70408; PNW70408; CHLRE_17g718500v5.
DR   Gramene; PNW70408; PNW70408; CHLRE_17g718500v5.
DR   BRENDA; 3.4.24.38; 1318.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR021158; Pept_M10A_Zn_BS.
DR   InterPro; IPR008752; Peptidase_M11.
DR   InterPro; IPR016517; Peptidase_M11_autolysin.
DR   Pfam; PF05548; Peptidase_M11; 1.
DR   PIRSF; PIRSF007635; Autolysin; 1.
DR   PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Periplasm;
KW   Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..183
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:1584806"
FT                   /id="PRO_0000028870"
FT   CHAIN           184..638
FT                   /note="Autolysin"
FT                   /id="PRO_0000028871"
FT   REGION          269..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           95..102
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        269..285
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        397
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         400
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         406
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   638 AA;  69833 MW;  D3E3467701177251 CRC64;
     MSLATRRFGA AAALLVAACV LCTAPAWAQN ETTGTGMVKT KSAFRWIRPP PARPPPFRRP
     PPAQTPYVHK VEYTELQILC PQTIDSVTGY PMDDPRCNVP RATVAAGEEA LTIRNEFELL
     NGDVLNVTLE EVDTPENPSR RRLLSIIREE QRTGRVLLAT SAELPTPTFR LKSLKSILKG
     SQKEIYAGKP IDLRTIVYIM DFSSCKLSGW SAPATLTPEK VTSDMLRGAS APTNNLANYY
     GACSYEKTLF NPDNFLVLGP VPVPCIGGVT PPPRPPRPPR PPPRAGSTIS SLSRRNDTYD
     DWWDLSKYCT ASEQQAWERA AEAYAQAIVA QDPNSATGKK LQGILQWRER RRNIYILPPG
     VKCSWSGYAD VTCTSATCSA YVRGYSDTNA MQVIMHEAMH NYGLEHAGRG TLEYGDATDV
     MGDFNKAGKG LLCPNAPNMY RIGWAKPINE PGVAPFQNAT GAWGNLTAAN FTTDPWIRGL
     VIPAQGTRDD NMIVVNVGAQ STRDGAMKAT GAQAYYFSYR IKNTTAGGYD SGLTLDFHKK
     VLVHAYNGIQ SERVFGFKSN LLDWGPNFQS RSNTWTSPFL AYNNGLGGGV RLVVQSTSDT
     QAVVDICRIS ENGKELSCDD GIDNDCDGLQ DNEDPDCQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024