ID K9J884_XENTR Unreviewed; 557 AA.
AC K9J884; A0A5G3JCD0;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=astl2c {ECO:0000313|Ensembl:ENSXETP00000034111};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000034111};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000034111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000034111};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000034111}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (DEC-2012) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR AlphaFoldDB; K9J884; -.
DR Ensembl; ENSXETT00000034111; ENSXETP00000034111; ENSXETG00000024385.
DR Xenbase; XB-GENE-6449741; astl2c.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_321757_0_0_1; -.
DR TreeFam; TF316506; -.
DR Bgee; ENSXETG00000024385; Expressed in head and 10 other cell types or tissues.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd04283; ZnMc_hatching_enzyme; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
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 PANTHER; PTHR10127:SF872; ASTACIN-LIKE METALLOENDOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 2.
DR PIRSF; PIRSF038057; Hatching_enzyme_Uvs2; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT DOMAIN 115..314
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 313..425
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 427..536
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 119..122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 557 AA; 62177 MW; 565135F0E79AE640 CRC64;
MKCIFFNMTL FSWVFIPNNW IKFVIFNDTK KMGPFYKQVF HKCHFIILQC NICKQNVSPA
EKDALATEGT VRGMEMPVLG KKSGSVDVFT QISKVNRGIR VPTYQGDILR PKGRSAMNCT
ECLWPKSTDG TVIVPYNFSS NYSADQLALF KSTMQEYESL TCVRFVPRAN ETDFLSIVSD
NGCASFLGKV GGDQTVQLDS YGCIYRGIIQ HELNHALGFY HEQSRSDRDD YVTIHTENII
PGYEGNFNKA DSNNLGLEYD YSSVMHYPGD AFSKNGNLTI VPKPDPTVPI GQRDGLSILD
VSKINRLYQC DVCSNLLSNT NGTMISANYP SAYPNNANCV WLIRIPSEQV TLQFQAFDIQ
SSPGCVSDYI KIYDGPSKTS PVLVDRACGT GLIPIQIAST NQMLVEFVSD GAVNGTGFKA
TYGSVQCGGA FYAPNKTFTS PGYPANYDNN LDCTWTITAP VGYKISLNIS DFELEDNRYC
MYDYVIIYNT TRSPVQNCGS IKFSSEFVST SNSVMITFHS DISIVKRGFS ATYRFGEYSD
IDPSWICKHT HVHFKIP
//