HE_HEMPU
ID HE_HEMPU Reviewed; 591 AA.
AC P91953;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=50 kDa 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=38 kDa hatching enzyme;
DE Contains:
DE RecName: Full=32 kDa hatching enzyme non-specific;
DE Contains:
DE RecName: Full=15 kDa peptide;
DE Flags: Precursor;
OS Hemicentrotus pulcherrimus (Sea urchin) (Strongylocentrotus pulcherrimus).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Hemicentrotus.
OX NCBI_TaxID=7650;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 170-220 AND 504-528.
RC TISSUE=Blastula;
RX PubMed=9188724; DOI=10.1021/bi9629790;
RA Nomura K., Shimizu T., Kinoh H., Sendai Y., Inomata M., Suzuki N.;
RT "Sea urchin hatching enzyme (envelysin): cDNA cloning and deprivation of
RT protein substrate specificity by autolytic degradation.";
RL Biochemistry 36:7225-7238(1997).
RN [2]
RP CLEAVAGE SPECIFICITY.
RX PubMed=1711895; DOI=10.1021/bi00239a005;
RA Nomura K., Tanaka H., Kikkawa Y., Yamaguchi M., Suzuki N.;
RT "The specificity of sea urchin hatching enzyme (envelysin) places it in the
RT mammalian matrix metalloproteinase family.";
RL Biochemistry 30:6115-6123(1991).
RN [3]
RP STEREOSPECIFICITY.
RX PubMed=8467915; DOI=10.1016/0014-5793(93)80626-6;
RA Nomura K., Suzuki N.;
RT "Stereo-specific inhibition of sea urchin envelysin (hatching enzyme) by a
RT synthetic autoinhibitor peptide with a cysteine-switch consensus
RT sequence.";
RL FEBS Lett. 321:84-88(1993).
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 -!- SUBUNIT: During hatching, the 50 kDa mature enzyme is autocatalytically
CC cleaved to produce a major 38 kDa and a minor 15 kDa form which may be
CC disulfide linked. Subsequent cleavage of the 38 kDa species yields a 32
CC kDa non-specific protease.
CC -!- DEVELOPMENTAL STAGE: Embryo, blastula stage. Highest activity at 12.5
CC hours embryo 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; AB000719; BAA19171.1; -; mRNA.
DR AlphaFoldDB; P91953; -.
DR SMR; P91953; -.
DR MEROPS; M10.010; -.
DR BRENDA; 3.4.24.12; 2635.
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; -; 1.
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; IPR018486; Hemopexin_CS.
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; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 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; PS00024; HEMOPEXIN; 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..169
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028859"
FT CHAIN 170..591
FT /note="50 kDa hatching enzyme"
FT /id="PRO_0000028860"
FT CHAIN 170..503
FT /note="38 kDa hatching enzyme"
FT /id="PRO_0000028861"
FT CHAIN 170..450
FT /note="32 kDa hatching enzyme non-specific"
FT /id="PRO_0000028862"
FT CHAIN 504..591
FT /note="15 kDa peptide"
FT /id="PRO_0000028863"
FT REPEAT 384..419
FT /note="Hemopexin 1"
FT REPEAT 428..471
FT /note="Hemopexin 2"
FT REPEAT 472..517
FT /note="Hemopexin 3"
FT REPEAT 522..574
FT /note="Hemopexin 4"
FT REGION 333..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 160..167
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 333..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 162
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 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 450..451
FT /note="Cleavage; by autolysis"
FT SITE 503..504
FT /note="Cleavage; by autolysis"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 383..586
FT /evidence="ECO:0000250"
FT CONFLICT 195
FT /note="S -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="T -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="L -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..216
FT /note="SL -> GN (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="E -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="P -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 511..512
FT /note="SS -> RR (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="P -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="R -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 66126 MW; 5DCB448C6758C70D CRC64;
MANFCLIFAA VFLTRLTTVL NTPISVTFGP TQLTDITKLV SETGDDFGLT TPRSAILTTV
SEDDSDDDDG GESVEDTTIL QTTTSSEIVI SGIVVDEDID ESKVVKLKAN LEQFGYVPLG
STFGEANINY TSAILEYQQN GGINQTGILD AETAALLDTP RCGVPDILPY VTGGIAWPRN
VAVTYSFGTL SNDLSQTAIK NELRRAFQVW DDVSSLTFRE VVDSSSVDIR IKFGSYEHGD
GISFDGQGGV LAHAFLPRNG DAHFDDSERW TIGTNSGTNL FQVAAHEFGH SLGLYHSDVQ
SALMYPYYRG YNPNFNLDRD DIAGITSLYG RNTGSTTTTT RRPTITRTTT RRTTTRRTTT
QLATTQTTTI RPPTYPTPPR QACTGSFDAV IKDNSDRIYA LAGRYYWRLD QASPSWGVVR
NRFGFDLPEN VDASFQNGIF SYFFSGCYYY YQTSTRRRFP RTPFNRRWVG LPCDIDAVYK
SGDSGTTYFF KGRFVYKFSS SNQLQRRSPI SSYFRNTPYA LRDGVEAVVR VDDVYLHFYR
DGRYYRMIES TKQFVNFPNG LSYRDVIDTL IPQCRSLNLS VEIESCSNSS E
