BP10_PARLI
ID BP10_PARLI Reviewed; 597 AA.
AC P42674;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Blastula protease 10;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=BP10;
OS Paracentrotus lividus (Common sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinidae; Paracentrotus.
OX NCBI_TaxID=7656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1339338; DOI=10.1242/dev.114.1.147;
RA Lepage T., Ghiglione C., Gache C.;
RT "Spatial and temporal expression pattern during sea urchin embryogenesis of
RT a gene coding for a protease homologous to the human protein BMP-1 and to
RT the product of the Drosophila dorsal-ventral patterning gene tolloid.";
RL Development 114:147-163(1992).
CC -!- FUNCTION: Could be involved in the differentiation of ectodermal
CC lineages and subsequent patterning of the embryo.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasm, cell
CC cortex. Secreted, extracellular space. Note=First detected in a
CC perinuclear region, then in an apical and submembranous position just
CC before its secretion into the perivitelline space.
CC -!- DEVELOPMENTAL STAGE: Embryonic. The protein is first detected in early
CC blastula stages, its level peaks in late cleavage, declines abruptly
CC before ingression of primary mesenchyme cells and remains constant in
CC late development.
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DR EMBL; X56224; CAA39673.1; -; mRNA.
DR AlphaFoldDB; P42674; -.
DR SMR; P42674; -.
DR MEROPS; M12.012; -.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR017369; SPAN/blastula_protease_10.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 2.
DR PIRSF; PIRSF038056; BP10_SPAN; 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; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Cytoplasm; Disulfide bond;
KW EGF-like domain; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..93
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028897"
FT CHAIN 94..597
FT /note="Blastula protease 10"
FT /id="PRO_0000028898"
FT DOMAIN 93..294
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 295..329
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 339..449
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 484..595
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 24..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
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 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 134..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 162..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 299..315
FT /evidence="ECO:0000250"
FT DISULFID 305..317
FT /evidence="ECO:0000250"
FT DISULFID 319..328
FT /evidence="ECO:0000250"
FT DISULFID 339..365
FT /evidence="ECO:0000250"
FT DISULFID 392..412
FT /evidence="ECO:0000250"
FT DISULFID 484..510
FT /evidence="ECO:0000250"
FT DISULFID 537..557
FT /evidence="ECO:0000250"
SQ SEQUENCE 597 AA; 66176 MW; 965703A7165FE6A4 CRC64;
MKLILFLSGL VSLVLCTLAA PTGDQKEIHT ETPPPKKPSE TTTPGALKTP QPEPKDEEPT
PGAFQGDMML TEDQQRESKE AIDDEMTGRK KRKATIYESQ RWPYKVIPYV ISPSSSGQSS
LIRNAMDHWE QNTCLRFEPR TSSHSRQLGH NAYLSFFRGS GCWSYVGKAF NGEQQISIGN
GCAYFGTIVH EIGHAIGFHH EQSRPDRDDY INVLYQNIQS GRQHNFAKYT WGRVTSRNVE
YDVGSIMHYG GYGFSSNGRP TITTRDPRLN SRLGQRIALS PADIELANLI YECDDIEDCA
GANECLNGGY HDTECNCVCP SGYNGDLCED AVTTTRPDCS ERFTEMTGVI TSPNWPGRYE
DNMACVYQIE GPPGSTIELT FTEMNIENHA ACRYDAVEVR KDDINSDGEK FCGNTLPAVQ
ISSGNQMLIS FTSDPSITGR GFRATYRIVI LTTTQIPDTT TISTTTPVPT TTQATTDETV
VGSCGGSFGG TQGRVATPNY PNNYDNDLEC VYVIEVEIGR RVELDFIDFV LEDETNCRWD
SLSINLGDGI KIDMKMCGRE YPAASLVSIG NNMELTLISD RSVTDRGFMA DYRAIDL
