Reviewed, UniProtKB/Swiss-Prot P31178 (GLE_CHLRE)

Names and origin

Protein names	Recommended name:     Autolysin     EC=3.4.24.38 Alternative name(s):     Gametolysin     Gamete lytic enzyme       Short name=GLE
Organism	Chlamydomonas reinhardtii
Taxonomic identifier	3055 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Post-translational modification	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.
Sequence similarities	Belongs to the peptidase M11 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Periplasm Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell proteinaceous extracellular matrix Inferred from electronic annotation. Source: InterPro
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Propeptide	29 – 183	155	Activation peptide Ref.1		PRO_0000028870
	Chain	184 – 638	455	Autolysin		PRO_0000028871
Regions
	Motif	95 – 102	8	Cysteine switch By similarity
	Compositional bias	49 – 62	14	Pro-rich
	Compositional bias	271 – 283	13	Pro-rich
Sites
	Active site	397	1	By similarity
	Metal binding	97	1	Zinc; in inhibited form By similarity
	Metal binding	396	1	Zinc; catalytic By similarity
	Metal binding	400	1	Zinc; catalytic By similarity
	Metal binding	406	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	30	1	N-linked (GlcNAc...) Potential
	Glycosylation	126	1	N-linked (GlcNAc...) Potential
	Glycosylation	296	1	N-linked (GlcNAc...) Potential
	Glycosylation	458	1	N-linked (GlcNAc...) Potential
	Glycosylation	465	1	N-linked (GlcNAc...) Potential
	Glycosylation	470	1	N-linked (GlcNAc...) Potential
	Glycosylation	523	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P31178-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: D3E3467701177251	FASTA	638	69,833
	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

References

[1]

"Primary structure and expression of a gamete lytic enzyme in Chlamydomonas reinhardtii: similarity of functional domains to matrix metalloproteases." Kinoshita T., Fukuzawa H., Shimada T., Saito T., Matsuda Y. Proc. Natl. Acad. Sci. U.S.A. 89:4693-4697(1992) [PubMed: 1584806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 184-203.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M94265 mRNA. Translation: AAA33094.1. D10542 mRNA. Translation: BAA01400.1.
PIR	A45287.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M11.001.
Proteomic databases
PRIDE	P31178.
Enzyme and pathway databases
BRENDA	3.4.24.38. 144.
Family and domain databases
InterPro	IPR001818. Pept_M10A_M12B. IPR006025. Pept_M_Zn_BS. IPR008752. Peptidase_M11. IPR016517. Peptidase_M11_autolysin. [Graphical view]
Pfam	PF05548. Peptidase_M11. 1 hit. [Graphical view]
PIRSF	PIRSF007635. Autolysin. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00142. ZINC_PROTEASE. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
PMAP-CutDB	P31178.

Entry information

Entry name

GLE_CHLRE

Accession

Primary (citable) accession number: P31178

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)