ASTL_COTJA
ID ASTL_COTJA Reviewed; 409 AA.
AC P42662; Q587K6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Astacin-like metalloendopeptidase;
DE EC=3.4.24.-;
DE AltName: Full=Chorioallantoic membrane-1 {ECO:0000303|PubMed:8286408};
DE Short=CAM-1 {ECO:0000303|PubMed:8286408};
DE AltName: Full=Quail hatching enzyme {ECO:0000303|PubMed:16003522};
DE Short=QHE {ECO:0000303|PubMed:16003522};
DE Flags: Precursor;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION BY
RP 1,25-DIHYDROXYVITAMIN D-3.
RC TISSUE=Chorioallantoic membrane;
RX PubMed=8286408; DOI=10.1016/0167-4781(94)90116-3;
RA Elaroussi M.A., Deluca H.F.;
RT "A new member to the astacin family of metalloendopeptidases: a novel 1,25-
RT dihydroxyvitamin D-3-stimulated mRNA from chorioallantoic membrane of
RT quail.";
RL Biochim. Biophys. Acta 1217:1-8(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, FUNCTION,
RP PROTEOLYTIC CLEAVAGE, AND ALTERNATIVE SPLICING.
RC TISSUE=Embryo;
RX PubMed=16003522; DOI=10.1007/s00427-005-0007-x;
RA Yasumasu S., Mao K.M., Sultana F., Sakaguchi H., Yoshizaki N.;
RT "Cloning of a quail homologue of hatching enzyme: its conserved function
RT and additional function in egg envelope digestion.";
RL Dev. Genes Evol. 215:489-498(2005).
CC -!- FUNCTION: Probable oocyte-specific oolemmal receptor involved in sperm
CC and egg adhesion and fertilization (By similarity). Protease which may
CC play a role in the breaking down of the vitelline membrane (days 0-5)
CC and possibly, in the digestion of the egg white (days 9-12)
CC (PubMed:16003522). {ECO:0000250|UniProtKB:Q6HA09,
CC ECO:0000269|PubMed:16003522}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6HA09}. Cell
CC membrane {ECO:0000250|UniProtKB:Q6HA09}. Cytoplasmic vesicle, secretory
CC vesicle, Cortical granule {ECO:0000250|UniProtKB:Q6HA09}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42662-1; Sequence=Displayed;
CC Name=2; Synonyms=CAM-1;
CC IsoId=P42662-2; Sequence=VSP_059666;
CC -!- DEVELOPMENTAL STAGE: Expressed in ectodermal cells of the yolk sac
CC during epiboly on days 0 - 5 (PubMed:16003522). Expressed in ectodermal
CC cells of the albumen sac on days 8 - 13 (PubMed:16003522).
CC {ECO:0000269|PubMed:16003522}.
CC -!- INDUCTION: By 1,25-dihydroxyvitamin D-3. {ECO:0000269|PubMed:8286408}.
CC -!- MISCELLANEOUS: [Isoform 2]: Minor transcript.
CC {ECO:0000269|PubMed:16003522}.
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DR EMBL; U12642; AAA20842.1; -; mRNA.
DR EMBL; AB210833; BAD95472.1; -; mRNA.
DR PIR; S41055; S41055.
DR AlphaFoldDB; P42662; -.
DR SMR; P42662; -.
DR MEROPS; M12.324; -.
DR BRENDA; 3.4.24.21; 1673.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070001; F:aspartic-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0070002; F:glutamic-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:2000360; P:negative regulation of binding of sperm to zona pellucida; ISS:UniProtKB.
DR GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0060468; P:prevention of polyspermy; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd04283; ZnMc_hatching_enzyme; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR017370; Hatching_enzyme_Uvs2-like.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR034039; ZnMP_hatching_enz.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR PIRSF; PIRSF038057; Hatching_enzyme_Uvs2; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Disulfide bond; Fertilization; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..86
FT /evidence="ECO:0000305|PubMed:16003522"
FT /id="PRO_0000444990"
FT CHAIN 87..409
FT /note="Astacin-like metalloendopeptidase"
FT /id="PRO_0000078183"
FT DOMAIN 87..285
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 287..399
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 30..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 91..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 134..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 155..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 287..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 339..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059666"
FT CONFLICT 101..199
FT /note="Missing (in Ref. 1; AAA20842)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="C -> D (in Ref. 2; BAD95472)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="R -> A (in Ref. 2; BAD95472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 46446 MW; B3C0D3964F9504C5 CRC64;
MDLKMLLIFT AFLLPAVLGF PIQDNYENST ATSESTQVTT EESIYDSPSP TETDSEDDVI
FNRILEVNKD SSRYLQEGDI VPRRSRSAFN CRNCYWPQSM DGIVRIPYVL DPTYEENHVR
GILEAMAEFE TLTCINFVKR KTERDYLIIR SADGCWSNYG KVGGGQTVSV MKGGCMWKGI
IQHELDHALG FLHEHSRSDR DKYVKIMWEY ISPACRPDFR KFENSNNLGL PYDYSSVMHY
GPHTFTNTTG KATIVPVPDG SVHIGQRLGL SNLDVAKINK LYNCSRCSTI IDAAFGSLKS
ANYPRNYSDN TNCVWLIRTR SRKISLHFRD FDLRRTRGCQ GDYVKVYDGS SKYSPVLMNK
TCGSQIPTDV VSSSSLMLIE FVTDGRDTAS GFQATFTSAR MQRRFNTRN
