UVS2_XENLA
ID UVS2_XENLA Reviewed; 514 AA.
AC P42664;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Embryonic protein UVS.2;
DE EC=3.4.24.-;
DE Flags: Precursor;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9074934;
RA Katagiri C., Maeda R., Yamashika C., Mita K., Sargent T.D., Yasumasu S.;
RT "Molecular cloning of Xenopus hatching enzyme and its specific expression
RT in hatching gland cells.";
RL Int. J. Dev. Biol. 41:19-25(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 196-514.
RX PubMed=1688538; DOI=10.1016/0012-1606(90)90014-a;
RA Sato S.M., Sargent T.D.;
RT "Molecular approach to dorsoanterior development in Xenopus laevis.";
RL Dev. Biol. 137:135-141(1990).
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 -!- DEVELOPMENTAL STAGE: Exclusively in the anterior neural fold of neurula
CC stage embryos. By the tailbud stage, the protein is localized in
CC specialized cephalic ectoderm, in a region probably corresponding to
CC the hatching gland.
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DR EMBL; D89632; BAA14003.1; -; mRNA.
DR EMBL; M27162; AAA49980.1; -; mRNA.
DR PIR; I51569; I51569.
DR RefSeq; NP_001081221.1; NM_001087752.1.
DR AlphaFoldDB; P42664; -.
DR SMR; P42664; -.
DR MEROPS; M12.014; -.
DR GeneID; 397718; -.
DR KEGG; xla:397718; -.
DR CTD; 397718; -.
DR Xenbase; XB-GENE-6252624; astl3a.1.L.
DR OrthoDB; 681837at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 397718; Expressed in neurula embryo and 1 other tissue.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd04283; ZnMc_hatching_enzyme; 1.
DR Gene3D; 2.60.120.290; -; 2.
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; 2.
DR PIRSF; PIRSF038057; Hatching_enzyme_Uvs2; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..514
FT /note="Embryonic protein UVS.2"
FT /id="PRO_0000028905"
FT DOMAIN 90..286
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 288..400
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 402..513
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 137..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 158..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 288..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 340..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 402..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 455..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 514 AA; 56845 MW; DE1FCB599014D986 CRC64;
MDVKISAILL ACIIQYAVSS PIQVFYSGAK ILAEEDAMAK EDILKAIEKA DPGSVKTQDS
MDILSQILEA NKGIKLQTQE GDIIQKQGRS AINDARFLWP KSADGIVPVP YNLSYSYNAD
QLALFKKAIQ EFEALTCVRF VPWTTEVNFL NIMSNGGCGS LIGKNGGAQR LELDANGCMN
MGIIQHELNH ALGFYHEQNR SDRDDYVIIH TENIIPDFLK MFEKYNTNNL GIEYDYASVM
HYSRYHYSIN GDITIEPKPD PNVPIGQRDG LSILDISKIN KLYECNVCSN LLPYSNGMMI
SANYPSAYPN NANCVWLIRT PSGQVTLQFQ AFDIQSSSGC VSDYIKIYDG PTKAFPVLVN
RACGTGLIPL QIASTNQMLV EFVSDRAVTG TGFKATYGSI QCGGAFYSSP KTFTSPNYPG
NYTTNTNCTW TITAPAGFKV SLRITDFELE IGASCRYDYL NIYNSTLGAV MGPYCGPIDF
HSAIVSKSNS MMITMNSDFS KQYKGFSATY TFVR
