HE12_DANRE
ID HE12_DANRE Reviewed; 263 AA.
AC Q1LW01; Q75NR9;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Hatching enzyme 1.2 {ECO:0000305};
DE EC=3.4.24.67 {ECO:0000269|PubMed:19021768, ECO:0000269|PubMed:20727360};
DE AltName: Full=Choriolysin H homolog 1 {ECO:0000303|PubMed:9108332};
DE AltName: Full=High choriolytic enzyme 1 homolog {ECO:0000303|PubMed:9108332};
DE Short=zHCE-1 {ECO:0000303|PubMed:9108332};
DE Flags: Precursor;
GN Name=he1.2 {ECO:0000312|ZFIN:ZDB-GENE-030131-2100};
GN Synonyms=he1 {ECO:0000312|ZFIN:ZDB-GENE-030131-2100},
GN he1a {ECO:0000312|ZFIN:ZDB-GENE-030131-2100},
GN he1b {ECO:0000312|ZFIN:ZDB-GENE-030131-2100};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:BAD15105.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9108332; DOI=10.1046/j.1440-169x.1997.t01-1-00007.x;
RA Inohaya K., Yasumasu S., Araki K., Naruse K., Yamazaki K., Yasumasu I.,
RA Iuchi I., Yamagami K.;
RT "Species-dependent migration of fish hatching gland cells that express
RT astacin-like proteases in common.";
RL Dev. Growth Differ. 39:191-197(1997).
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000312|EMBL:AAI33962.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Singapore {ECO:0000312|EMBL:AAI33962.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAI33962.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 65-70, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19021768; DOI=10.1111/j.1742-4658.2008.06722.x;
RA Sano K., Inohaya K., Kawaguchi M., Yoshizaki N., Iuchi I., Yasumasu S.;
RT "Purification and characterization of zebrafish hatching enzyme - an
RT evolutionary aspect of the mechanism of egg envelope digestion.";
RL FEBS J. 275:5934-5946(2008).
RN [5] {ECO:0000305}
RP CRYSTALLIZATION.
RX PubMed=19851011; DOI=10.1107/s1744309109033016;
RA Okada A., Nagata K., Sano K., Yasumasu S., Kubota K., Ohtsuka J., Iuchi I.,
RA Tanokura M.;
RT "Crystallization and preliminary X-ray analysis of ZHE1, a hatching enzyme
RT from the zebrafish Danio rerio.";
RL Acta Crystallogr. F 65:1018-1020(2009).
RN [6] {ECO:0007744|PDB:3LQB}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 65-263 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND DISULFIDE BONDS.
RX PubMed=20727360; DOI=10.1016/j.jmb.2010.08.023;
RA Okada A., Sano K., Nagata K., Yasumasu S., Ohtsuka J., Yamamura A.,
RA Kubota K., Iuchi I., Tanokura M.;
RT "Crystal structure of zebrafish hatching enzyme 1 from the zebrafish Danio
RT rerio.";
RL J. Mol. Biol. 402:865-878(2010).
CC -!- FUNCTION: Metalloendopeptidase which participates in the breakdown of
CC the egg envelope at the time of hatching. Cleaves the N-terminal
CC regions of the zona pellucia glycoproteins ZP2 and ZP3, where it
CC specifically recognizes the peptide sequences TVQQS-|-DYLIK (major
CC site) and KLMLK-|-APEPF (minor site). {ECO:0000269|PubMed:19021768,
CC ECO:0000269|PubMed:20727360}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the inner layer of fish egg envelope. Also
CC hydrolysis of casein and small molecule substrates such as succinyl-
CC Leu-Leu-Val-Tyr-|-7-(4-methyl)coumarylamide.; EC=3.4.24.67;
CC Evidence={ECO:0000269|PubMed:19021768, ECO:0000269|PubMed:20727360};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211,
CC ECO:0000255|RuleBase:RU361183, ECO:0000305|PubMed:20727360};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211, ECO:0000255|RuleBase:RU361183,
CC ECO:0000305|PubMed:20727360};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19021768}.
CC -!- TISSUE SPECIFICITY: Expressed in cells of the hatching gland.
CC {ECO:0000269|PubMed:19021768, ECO:0000269|PubMed:9108332}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos just before the bud stage, in
CC an oval patch in the polster (anterior prechordal plate)
CC (PubMed:9108332). At the 3-somite stage, found in a horseshoe-shaped
CC cluster of cells surrounding the head primordium (PubMed:9108332). From
CC 24 hours post-fertilization (hpf) onwards, expressed in a belt-like
CC shape on the anterior surface of the yolk sac (PubMed:9108332,
CC PubMed:19021768). Little or no expression detected after hatching
CC (PubMed:9108332, PubMed:19021768). {ECO:0000269|PubMed:19021768,
CC ECO:0000269|PubMed:9108332}.
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DR EMBL; AB175621; BAD15105.1; -; mRNA.
DR EMBL; BX649296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC133961; AAI33962.1; -; mRNA.
DR RefSeq; NP_998800.2; NM_213635.2.
DR PDB; 3LQB; X-ray; 1.10 A; A=65-263.
DR PDBsum; 3LQB; -.
DR AlphaFoldDB; Q1LW01; -.
DR SMR; Q1LW01; -.
DR STRING; 7955.ENSDARP00000009264; -.
DR MEROPS; M12.007; -.
DR PaxDb; Q1LW01; -.
DR Ensembl; ENSDART00000018432; ENSDARP00000009264; ENSDARG00000019122.
DR GeneID; 407971; -.
DR KEGG; dre:407971; -.
DR CTD; 407971; -.
DR ZFIN; ZDB-GENE-030131-2100; he1.2.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000163716; -.
DR InParanoid; Q1LW01; -.
DR OrthoDB; 681837at2759; -.
DR PhylomeDB; Q1LW01; -.
DR TreeFam; TF315280; -.
DR EvolutionaryTrace; Q1LW01; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000019122; Expressed in internal ear and 5 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:ZFIN.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0035188; P:hatching; IDA:ZFIN.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd04283; ZnMc_hatching_enzyme; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR034039; ZnMP_hatching_enz.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..64
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000452500"
FT CHAIN 65..263
FT /note="Hatching enzyme 1.2"
FT /evidence="ECO:0000269|PubMed:19021768"
FT /id="PRO_5015019995"
FT DOMAIN 65..263
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20727360,
FT ECO:0007744|PDB:3LQB"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20727360,
FT ECO:0007744|PDB:3LQB"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20727360,
FT ECO:0007744|PDB:3LQB"
FT DISULFID 69..74
FT /evidence="ECO:0000269|PubMed:20727360,
FT ECO:0007744|PDB:3LQB"
FT DISULFID 114..263
FT /evidence="ECO:0000269|PubMed:20727360,
FT ECO:0007744|PDB:3LQB"
FT DISULFID 135..155
FT /evidence="ECO:0000269|PubMed:20727360,
FT ECO:0007744|PDB:3LQB"
FT CONFLICT 28
FT /note="I -> V (in Ref. 1; BAD15105)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="R -> G (in Ref. 1; BAD15105)"
FT /evidence="ECO:0000305"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3LQB"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:3LQB"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:3LQB"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:3LQB"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:3LQB"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:3LQB"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:3LQB"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:3LQB"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3LQB"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3LQB"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3LQB"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3LQB"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:3LQB"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:3LQB"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3LQB"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:3LQB"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:3LQB"
SQ SEQUENCE 263 AA; 29448 MW; BBB0DFD117B80A9E CRC64;
MDIRASLSIL LLLFGLSQAS PLREFEAIFV SEPETVDITT QILETNKGSS EVLFEGDVVL
PKNRNALICE DKSCFWKKNA NNIVEVPYVV SGEFSINDKS VIANAISIFH AQTCIRFVPR
SIQADYLSIE NKDGCYSAIG RTGGKQVVSL NRKGCVYSGI AQHELNHALG FYHEQSRSDR
DQYVRINWNN ISPGMAYNFL KQKTNNQNTP YDYGSLMHYG KTAFAIQPGL ETITPIPDEN
VQIGQRQGLS KIDILRINKL YGC
