ID F6R0P6_XENTR Unreviewed; 512 AA.
AC F6R0P6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=accs {ECO:0000313|Ensembl:ENSXETP00000002002};
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:ENSXETP00000002002};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000002002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000002002};
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:ENSXETP00000002002}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) 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; F6R0P6; -.
DR Ensembl; ENSXETT00000002002; ENSXETP00000002002; ENSXETG00000022231.
DR AGR; Xenbase:XB-GENE-989873; -.
DR Xenbase; XB-GENE-989873; accs.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_321757_0_0_1; -.
DR InParanoid; F6R0P6; -.
DR OrthoDB; 2876645at2759; -.
DR TreeFam; TF315280; -.
DR Bgee; ENSXETG00000022231; Expressed in neurula embryo and 2 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 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 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, 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 82..279
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 281..395
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 397..509
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 86..89
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 512 AA; 56871 MW; 486A004B0F957834 CRC64;
MAASGSVNSN GQGSIQMVSV VLPGDLCVSC SDKSFAVDQL PSGNYEDEEA YHEDVFSQIL
KSNNGTVKKL WQGDIAIETG RSATKCTSCL WPKSADGTVR VPYRLSADYS DNEKSSIRDA
LLEFNTLTCV HFVERSTEED FLDIVSDSGC WSSIGRTGGA QTLSLMSSGC LAKGIIQHEV
DHALGFYHEQ SRSDRDTYID VLWQYICESD WGSFEMVDTD NLDLPYDYSS VMHYGWYAFS
NTSGQPSLRP KPDPTANIGQ RYGLSPLDVS KVKELYGCKL CTYLLTGVNG SLDSHNYMSE
YPTETSCLWL IRVNKNKVLL QFDTFRMSPS GGCTDNYIMV YDGPSRSSRV LVERACGSLE
LPLLVASSGV LLVEFVHQKG LRASETEFRA SYSSVDCGGT YRNDNGTVTS PGYPNPYTNL
VHCMTTIWAP PGYQIILNFT LFELEYSFSC SYDYLLIHDG SQPSSPEVGR FCSDMEIPTI
VSTGNVLLLQ FYSDHWMNNL GYRADYHFVP AL
//
