GenomeNet

Database: UniProt
Entry: K9J884_XENTR
LinkDB: K9J884_XENTR
Original site: K9J884_XENTR 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system