OVCH2_RHIAE
ID OVCH2_RHIAE Reviewed; 980 AA.
AC Q66TN7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Ovochymase-2 {ECO:0000305};
DE EC=3.4.21.120 {ECO:0000250|UniProtKB:Q90WD8};
DE AltName: Full=Oviductal protease;
DE AltName: Full=Oviductin {ECO:0000303|PubMed:20810007};
DE Flags: Precursor;
GN Name=OVCH2; Synonyms=OVTN;
OS Rhinella arenarum (Argentine common toad) (Bufo arenarum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX NCBI_TaxID=38577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=20810007; DOI=10.1017/s0967199410000468;
RA Barrera D., Valdecantos P.A., Garcia E.V., Miceli D.C.;
RT "Cloning and sequence analysis of Bufo arenarum oviductin cDNA and
RT detection of its orthologous gene expression in the mouse female
RT reproductive tract.";
RL Zygote 20:17-26(2012).
CC -!- FUNCTION: Mediates gamete interaction by affecting the vitelline coat.
CC {ECO:0000250|UniProtKB:Q90WD8}.
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:0000250|UniProtKB:Q90WD8};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P79953}.
CC -!- TISSUE SPECIFICITY: Differentially expressed in the oviductal pars
CC recta (PR) region. {ECO:0000269|PubMed:20810007}.
CC -!- PTM: The catalytically inactive 108 kDa form is processed both N- and
CC C-terminally to give rise to catalytically active and inactive forms.
CC {ECO:0000305|PubMed:20810007}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AY704215; AAU11501.2; -; mRNA.
DR AlphaFoldDB; Q66TN7; -.
DR SMR; Q66TN7; -.
DR MEROPS; S01.240; -.
DR BRENDA; 3.4.21.120; 1018.
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; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 3.
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 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; SSF49854; 3.
DR SUPFAM; SSF50494; SSF50494; 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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..49
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000261185"
FT CHAIN 50..592
FT /note="Ovochymase-2"
FT /id="PRO_0000261186"
FT PROPEP 593..980
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000261187"
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 593..822
FT /note="Peptidase S1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 835..863
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 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 932
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 618..634
FT /evidence="ECO:0000250"
FT DISULFID 716..779
FT /evidence="ECO:0000250"
FT DISULFID 744..757
FT /evidence="ECO:0000250"
FT DISULFID 769..798
FT /evidence="ECO:0000250"
SQ SEQUENCE 980 AA; 108566 MW; 4B8164AE26E5CDC5 CRC64;
MAETSVFSIM MLTVMTAVGR GATDRPGRVS RCGERPSANA SVTYNLLSRI VGGTSAVKGE
SPWMVSLKRD GKHFCGGTII SDKHVLTAAH CVLDKNIEYH VRVSIGDHDF TVYERSEQIF
AIKAVFKHPN FNPIRPFNYD LAIVELGESI AFDKDIQPAC LPSPDDVFPT GTLCIALGWG
RLQENGRLPS SLQQVVLPLI EYRKCLSIME TVDRRLAFET VVCAGFPEGG KDACQGDSGG
PFLCQRSQGR WVLVGVTSWG LGCARKWVDN ILDPPERRGS PGVFTDIQRL LNWLSANLNQ
DKPDFPTYEV QCSTNDGIEK GTAGEILLPT DYRKYYSNNE KCIWTIIVPK GKHILLTFNS
FNVEWDYSCD LDYLVIYSAL GRLIGKFCGD VRPRPLLIAD ASVTLKFISD FQEYKTGFSL
FYQAVEPNTY PDSDCGSVAV IFEEGEIQTM NHPHVYSSHA NCQWVVHSPA NHIIKITFLV
FEVEPSEGCI FDRLVVYHDL QGTMVAGIFC GFSLPDPVLS VSNVMQITFT SDYSVNYLGF
QAVISFVLPS SPVKSETQWK GNNQPRKNQD AMQHYEEGCG VSPLPPRFIH HNIIKAEEAM
PNSWPWHVSI NFGNKHLCNG AILSKTFVVT SANCVADREE FPSVGLIVAG LHDLESSTDA
QKRTVEYVIV HPDYNRLSKD YDVALIHVQM PFQYNSHVQP ICLPDGHSKL EPSKLCVVSG
WDLNVELSTK LQQLEVPVLM DDVCKKYYDG ITDRMFCAGV IAEEDNVSCL AQSGAPLVCQ
SDPGTYVIFG IVSWGVGCNE PPKAGVYSSV PLFIPWIMET ILSVAGIANT DTEPHHPLIP
PDKLSQEKAL LPDSPPSNDS SSSQDIYVTC KDVMSLQSPG EIKLVASAQD GPEGGRCQLI
FQAPEDHFIL LHFKQLSHEH YSLIIYEGAS SNKTFKAQLT EEKIPTIMKS VGPVITIEAS
STAQDSALHL WLSYSFHNQN
