[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 167-191 AND 325-333. PubMed=2167841 [NCBI, ExPASy, EBI, Israel, Japan] Lepage T., Gache C.; "Early expression of a collagenase-like hatching enzyme gene in the sea urchin embryo."; EMBO J. 9:3003-3012(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8112336 [NCBI, ExPASy, EBI, Israel, Japan] Ghiglione C., Lhomond G., Lepage T., Gache C.; "Structure of the sea urchin hatching enzyme gene."; Eur. J. Biochem. 219:845-854(1994).

Comments

FUNCTION: Allows the sea urchin to digest the protective envelope derived from the egg extracellular matrix; thus allowing the sea urchin to swim freely.
CATALYTIC ACTIVITY: Hydrolysis of proteins of the fertilization envelope and dimethylcasein.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
DEVELOPMENTAL STAGE: Embryo, blastula stage.
DOMAIN: There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity.
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.
SIMILARITY: Belongs to the peptidase M10A family [view classification].
SIMILARITY: Contains 4 hemopexin-like domains.

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

X53598; CAA37667.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X65722; CAA46638.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S12805; S12805.
S41409; S41409.

3D structure databases

HSSP

P08254; 1HY7. [HSSP ENTRY / PDB]

ModBase

P22757.

Protein family/group databases

MEROPS

M10.010; -.

Ontologies

GO:0005578;	Cellular component: proteinaceous extracellular matrix (inferred from electronic annotation from InterPro).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000585; Hemopexin.
IPR001818; Pept_M10A_M12B.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR002477; Peptidoglycan-bd-like.
Graphical view of domain structure.

Gene3D

G3DSA:2.110.10.10; Hemopexin; 1.

Pfam

PF00045; Hemopexin; 4.
PF00413; Peptidase_M10; 1.
PF01471; PG_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00138; MATRIXIN.

SMART

SM00120; HX; 4.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.

PROSITE

PS00546; CYSTEINE_SWITCH; 1.
PS00024; HEMOPEXIN; FALSE_NEG.
PS00142; ZINC_PROTEASE; 1.

ProtoNet

P22757.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Autocatalytic cleavage; Calcium; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease; Repeat; Signal; Zinc; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Probable.`
`PROPEP`	`19 166`	`148`	`Activation peptide.`	`PRO_0000028864`
`CHAIN`	`167 587`	`421`	`Hatching enzyme.`	`PRO_0000028865`
`CHAIN`	`167 324`	`158`	`Hatching enzyme 18 kDa form.`	`PRO_0000028866`
`DOMAIN`	`384 426`	`43`	`Hemopexin-like 1.`
`DOMAIN`	`428 470`	`43`	`Hemopexin-like 2.`
`DOMAIN`	`472 515`	`44`	`Hemopexin-like 3.`
`DOMAIN`	`521 565`	`45`	`Hemopexin-like 4.`
`MOTIF`	`157 164`	`8`	`Cysteine switch (By similarity).`
`COMPBIAS`	`334 376`	`43`	`Arg/Thr-rich (hinge region).`
`ACT_SITE`	`284 284`		`By similarity.`
`METAL`	`159 159`		`Zinc; in inhibited form (By similarity).`
`METAL`	`283 283`		`Zinc; catalytic (By similarity).`
`METAL`	`287 287`		`Zinc; catalytic (By similarity).`
`METAL`	`293 293`		`Zinc; catalytic (By similarity).`
`SITE`	`324 325`	`2`	`Cleavage; by autolysis.`
`CARBOHYD`	`64 64`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`126 126`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`141 141`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`584 584`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`380 582`		`By similarity.`
`CONFLICT`	`158 158`		`R -> L (in Ref. 2; CAA46638).`
`CONFLICT`	`196 196`		`V -> A (in Ref. 2; CAA46638).`
`CONFLICT`	`269 269`		`E -> I (in Ref. 2; CAA46638).`
`CONFLICT`	`316 316`		`N -> S (in Ref. 2; CAA46638).`
`CONFLICT`	`558 558`		`P -> A (in Ref. 2; CAA46638).`

Sequence information

Length: 587 AA [This is the length of the unprocessed precursor]

Molecular weight: 65207 Da [This is the MW of the unprocessed precursor]

CRC64: 0A1733EC547279AA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MANSGLILLV MFMIHVTTVH NVPLPSTAPS IITQLSDITT SIIEEDAFGL TTPTTGLLTP 

        70         80         90        100        110        120 
VSENDSDDDG DDITTIQTTT SSSQTVISGV VVEEGVHESN VEILKAHLEK FGYTPPGSTF 

       130        140        150        160        170        180 
GEANLNYTSA ILDFQEHGGI NQTGILDADT AELLSTPRCG VPDVLPFVTS SITWSRNQPV 

       190        200        210        220        230        240 
TYSFGALTSD LNQNDVKDEI RRAFRVWDDV SGLSFREVPD TTSVDIRIKF GSYDHGDGIS 

       250        260        270        280        290        300 
FDGRGGVLAH AFLPRNGDAH FDDSETWTEG TRSGTNLFQV AAHEFGHSLG LYHSTVRSAL 

       310        320        330        340        350        360 
MYPYYQGYVP NFRLDNDDIA GIRSLYGSNS GSGTTTTTRR PTTTRATTTR RTTTTRATTT 

       370        380        390        400        410        420 
RATTTTTTSP SRPSPPRRAC SGSFDAVVRD SSNRIYALTG PYFWQLDQPS PSWGLVSNRF 

       430        440        450        460        470        480 
GFGLPQNIDA SFQRGVVTYF FSECYYYYQT STQRNFPRIP VNRKWVGLPC NIDAVYRSSR 

       490        500        510        520        530        540 
GPTYFFKDSF VYKFNSNNRL QRRTRISSLF NDVPSALHDG VEAVVRADRN YIHFYRDGRY 

       550        560        570        580 
YRMTDYGRQF VNFPNGLPYS DVIESVIPQC RGRSLSYESE GCSNSSE

P22757 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools