HE_PARLI
ID HE_PARLI Reviewed; 587 AA.
AC P22757;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Hatching enzyme;
DE Short=HE;
DE Short=HEZ;
DE EC=3.4.24.12;
DE AltName: Full=Envelysin;
DE AltName: Full=Sea-urchin-hatching proteinase;
DE Contains:
DE RecName: Full=Hatching enzyme 18 kDa form;
DE Flags: Precursor;
OS Paracentrotus lividus (Common sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinidae; Paracentrotus.
OX NCBI_TaxID=7656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 167-191 AND 325-333.
RX PubMed=2167841; DOI=10.1002/j.1460-2075.1990.tb07493.x;
RA Lepage T., Gache C.;
RT "Early expression of a collagenase-like hatching enzyme gene in the sea
RT urchin embryo.";
RL EMBO J. 9:3003-3012(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8112336; DOI=10.1111/j.1432-1033.1994.tb18566.x;
RA Ghiglione C., Lhomond G., Lepage T., Gache C.;
RT "Structure of the sea urchin hatching enzyme gene.";
RL Eur. J. Biochem. 219:845-854(1994).
CC -!- FUNCTION: Allows the sea urchin to digest the protective envelope
CC derived from the egg extracellular matrix; thus allowing the sea urchin
CC to swim freely.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins of the fertilization envelope and
CC dimethylcasein.; EC=3.4.24.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- DEVELOPMENTAL STAGE: Embryo, blastula stage.
CC -!- DOMAIN: There are two distinct domains in this protein; the catalytic
CC N-terminal, and the C-terminal which is involved in substrate
CC specificity.
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 -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; X53598; CAA37667.1; -; mRNA.
DR EMBL; X65722; CAA46638.1; -; Genomic_DNA.
DR PIR; S12805; S12805.
DR PIR; S41409; S41409.
DR AlphaFoldDB; P22757; -.
DR SMR; P22757; -.
DR MEROPS; M10.010; -.
DR KEGG; ag:CAA37667; -.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.110.10.10; -; 2.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR021158; Pept_M10A_Zn_BS.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR Pfam; PF00045; Hemopexin; 2.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease; Repeat;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..166
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2167841"
FT /id="PRO_0000028864"
FT CHAIN 167..587
FT /note="Hatching enzyme"
FT /id="PRO_0000028865"
FT CHAIN 167..324
FT /note="Hatching enzyme 18 kDa form"
FT /id="PRO_0000028866"
FT REPEAT 381..422
FT /note="Hemopexin 1"
FT REPEAT 425..468
FT /note="Hemopexin 2"
FT REPEAT 469..513
FT /note="Hemopexin 3"
FT REPEAT 518..570
FT /note="Hemopexin 4"
FT REGION 325..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 157..164
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 325..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 159
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 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 324..325
FT /note="Cleavage; by autolysis"
FT CARBOHYD 64
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 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 380..582
FT /evidence="ECO:0000250"
FT CONFLICT 158
FT /note="R -> L (in Ref. 2; CAA46638)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="V -> A (in Ref. 2; CAA46638)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="E -> I (in Ref. 2; CAA46638)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="N -> S (in Ref. 2; CAA46638)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="P -> A (in Ref. 2; CAA46638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 65207 MW; 0A1733EC547279AA CRC64;
MANSGLILLV MFMIHVTTVH NVPLPSTAPS IITQLSDITT SIIEEDAFGL TTPTTGLLTP
VSENDSDDDG DDITTIQTTT SSSQTVISGV VVEEGVHESN VEILKAHLEK FGYTPPGSTF
GEANLNYTSA ILDFQEHGGI NQTGILDADT AELLSTPRCG VPDVLPFVTS SITWSRNQPV
TYSFGALTSD LNQNDVKDEI RRAFRVWDDV SGLSFREVPD TTSVDIRIKF GSYDHGDGIS
FDGRGGVLAH AFLPRNGDAH FDDSETWTEG TRSGTNLFQV AAHEFGHSLG LYHSTVRSAL
MYPYYQGYVP NFRLDNDDIA GIRSLYGSNS GSGTTTTTRR PTTTRATTTR RTTTTRATTT
RATTTTTTSP SRPSPPRRAC SGSFDAVVRD SSNRIYALTG PYFWQLDQPS PSWGLVSNRF
GFGLPQNIDA SFQRGVVTYF FSECYYYYQT STQRNFPRIP VNRKWVGLPC NIDAVYRSSR
GPTYFFKDSF VYKFNSNNRL QRRTRISSLF NDVPSALHDG VEAVVRADRN YIHFYRDGRY
YRMTDYGRQF VNFPNGLPYS DVIESVIPQC RGRSLSYESE GCSNSSE
