ID F6ZRI3_XENTR Unreviewed; 505 AA.
AC F6ZRI3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=astl2g {ECO:0000313|Ensembl:ENSXETP00000001993,
GN ECO:0000313|RefSeq:XP_002934115.1,
GN ECO:0000313|Xenbase:XB-GENE-22069768};
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:ENSXETP00000001993};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000001993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000001993};
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:ENSXETP00000001993}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_002934115.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002934115.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002934115.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_002934115.1; XM_002934069.5.
DR PaxDb; 8364-ENSXETP00000016028; -.
DR Ensembl; ENSXETT00000001993; ENSXETP00000001993; ENSXETG00000000918.
DR GeneID; 100491886; -.
DR KEGG; xtr:100491886; -.
DR CTD; 100491886; -.
DR Xenbase; XB-GENE-22069768; astl2g.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_005140_1_0_1; -.
DR OMA; QFDLGQR; -.
DR TreeFam; TF315280; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Bgee; ENSXETG00000000918; Expressed in neurula embryo and 1 other cell type or tissue.
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:SF780; 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};
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 Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 20..505
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5041474044"
FT DOMAIN 73..271
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 273..385
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 387..498
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 505 AA; 55177 MW; 0735CAA2CB70EC17 CRC64;
MDIVTSCLIV ASLMQCILGA PLEIYFEEAN KIAVSQEEAK PEPKDVFTII SETNKGVKKL
LHESDIVVSV DRNAMKCDGD TCRWKTSDGI VRVPYTISAN FSATEVSVIV DAMQDFATLT
CVNFVPRTVE PDYLQIIPDS GCWSYVGKTG GAQEVSLNQG GCVGKGTVQH ELNHALGFYH
EQSRSDRDNY VNILTGNIIP ASIGNFDKYN TNNLGQEYDY SSVMHYGRNA FAKQPGLDTI
VPKPNPNVPI GQRYGLSNLD ISKINQLYQC GACSTVLSDS TGSLMSSNYP GSYPHNTKCS
WLIRAPSDQI FLQFSAFDVQ SSAGCASDYL KIYDGGSRSD PVLLDRACGT GQLPSVVSTG
NLLLLDFVSD QSIGGNGFKA SYNTVQCGSS FFNPSGQFST PNYPSPYPPN TNCTWIISAP
DGYQVSLNMA DFYLEYQRSC SYDNLQVFDG PRPTSPLIGR YCVSTPSTIV STGNSLLLQF
HSDSEVENKG FMAKYSFVPK KLKKN
//
