ID OVCH2_BUFJA Reviewed; 974 AA.
AC Q90WD8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Ovochymase-2 {ECO:0000305};
DE EC=3.4.21.120 {ECO:0000269|PubMed:11846486};
DE AltName: Full=Oviductal protease;
DE AltName: Full=Oviductin {ECO:0000303|PubMed:11846486};
DE Flags: Precursor;
GN Name=OVCH2; Synonyms=OVTN;
OS Bufo japonicus (Japanese toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Bufo.
OX NCBI_TaxID=8387;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 50-62, FUNCTION, TISSUE
RP SPECIFICITY, INDUCTION, PTM, AND CATALYTIC ACTIVITY.
RC TISSUE=Oviduct;
RX PubMed=11846486; DOI=10.1006/dbio.2001.0558;
RA Hiyoshi M., Takamune K., Mita K., Kubo H., Sugimoto Y., Katagiri C.;
RT "Oviductin, the oviductal protease that mediates gamete interaction by
RT affecting the vitelline coat in Bufo japonicus: its molecular cloning and
RT analyses of expression and posttranslational activation.";
RL Dev. Biol. 243:176-184(2002).
CC -!- FUNCTION: Mediates gamete interaction by affecting the vitelline coat.
CC {ECO:0000269|PubMed:11846486}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage at 371-Gly-Ser-Arg-|-Trp-374 of
CC glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield
CC gp41.; EC=3.4.21.120; Evidence={ECO:0000269|PubMed:11846486};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P79953}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the cells lining the
CC bottom of epithelial folds in the oviductal pars recta.
CC {ECO:0000269|PubMed:11846486}.
CC -!- INDUCTION: By human chorionic gonadotropin (HCG).
CC {ECO:0000269|PubMed:11846486}.
CC -!- PTM: The catalytically inactive 107 kDa form is processed both N- and
CC C-terminally to give rise to the 66 kDa catalytically active form and
CC inactive forms of 82 kDa and 59 kDa. {ECO:0000269|PubMed:11846486}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AB070367; BAB63372.1; -; mRNA.
DR AlphaFoldDB; Q90WD8; -.
DR SMR; Q90WD8; -.
DR MEROPS; S01.240; -.
DR GlyCosmos; Q90WD8; 3 sites, No reported glycans.
DR KEGG; ag:BAB63372; -.
DR BRENDA; 3.4.21.120; 1020.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 3.
DR CDD; cd00190; Tryp_SPc; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Protease; Repeat; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..49
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:11846486"
FT /id="PRO_0000261188"
FT CHAIN 50..589
FT /note="Ovochymase-2"
FT /id="PRO_0000261189"
FT PROPEP 590..974
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000261190"
FT DOMAIN 50..299
FT /note="Peptidase S1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 312..425
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 435..547
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 590..819
FT /note="Peptidase S1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 830..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..91
FT /evidence="ECO:0000250"
FT DISULFID 174..244
FT /evidence="ECO:0000250"
FT DISULFID 205..223
FT /evidence="ECO:0000250"
FT DISULFID 234..263
FT /evidence="ECO:0000250"
FT DISULFID 312..342
FT /evidence="ECO:0000250"
FT DISULFID 369..388
FT /evidence="ECO:0000250"
FT DISULFID 435..462
FT /evidence="ECO:0000250"
FT DISULFID 489..510
FT /evidence="ECO:0000250"
FT DISULFID 615..631
FT /evidence="ECO:0000250"
FT DISULFID 713..776
FT /evidence="ECO:0000250"
FT DISULFID 741..754
FT /evidence="ECO:0000250"
FT DISULFID 766..795
FT /evidence="ECO:0000250"
SQ SEQUENCE 974 AA; 107648 MW; F19705A470465553 CRC64;
MAETSIFPIM MLTVMIGVGR GVTDSPGRVS RCGERPAANT SVSYGLLSRI VGGTSAVKGE
SPWMVSLKRD GKHFCGGTII SDKYVLTAAH CVLEKNFEFQ VSVSIGDHDF AVYERSEQRF
AIKSVFKHPN FKPSRPFNYD LAILELVESI TFDKDIQPAC LPSPDDVFPT GTLCMALGWG
RLQENGRLPS SLQKVVLPLI EYRRCLSIME TVDRRLAFET VVCAGFPEGG KDACQGDSGG
PFLCQRSQGR WVLVGVTSWG LGCARKWADN ILDPVESKGS PGVFTDIQRL LNWLSENLNQ
DKPDFPTYQV QCSTNDGIEK GTTGEILLPT GYKKYYSNNE KCIWTIIVPR GKHILLTFKS
FNVECDYSCD LDYLVIYSAL GRLIGKFCGD VSPRPLLIAD ASITLKFISD FHEYKTGFSL
FYEAVEPDTY PDSDCGSVAV IFEEGEIQTM NHPHLYSSHA NCQWVVHSPA NYIIKITFLV
FEVEPSEGCI FDRLVVYHDL QGTVVAGFFC GFALPDPVLS VSNVMQITFT SDYSANYLGF
RAVISFVLPS SPVKPEKGNN QPRKNQDAMQ HFDEGCGVSP LPPRFLYHNL IKAEEAMPNS
WPWHVSINFG NKHVCNGAIL SKTFVVTSAN CVADREEFPS IGLIVAGLHD LESSINTQKR
PVEYVIVHPD YNRLSKDYDV ALIHVQRPFQ YNSYVQPICL PDGHSRLEPS KLCVVSGWDL
NVELSTKLQQ LEVPVLMDDV CKKYYDGITD RMFCAGVIAE EDNASCLAQS GAPLVCQSAP
GTYAIFGIVS RGVGCNETPK AGVYSSVFLF IPWIMETILS VAGIIDTDSE PHHPLFPPDK
PSQQKALLPD SPPSSSSQDI YVTCKDVLSL QSPGEIKLVA SGQDGPEGGR CQLIFQAPEG
HFILLTFKQL SHEHYSLIIY EGASSNKTFK AQLMEEKIPT IMKSAGAVIT LEASSTAQDS
ALHLWLSYSF HNQN
//
