OVCH2_XENLA
ID OVCH2_XENLA Reviewed; 1004 AA.
AC P79953;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ovochymase-2 {ECO:0000305};
DE EC=3.4.21.120 {ECO:0000269|PubMed:10084976};
DE AltName: Full=Oviductal protease;
DE AltName: Full=Oviductin {ECO:0000303|PubMed:10084976};
DE Flags: Precursor;
GN Name=ovch2; Synonyms=ovtn;
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], PROTEIN SEQUENCE OF 46-73, FUNCTION, PTM,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=10084976; DOI=10.1095/biolreprod60.4.989;
RA Lindsay L.L., Wieduwilt M.J., Hedrick J.L.;
RT "Oviductin, the Xenopus laevis oviductal protease that processes egg
RT envelope glycoprotein gp43, increases sperm binding to envelopes, and is
RT translated as part of an unusual mosaic protein composed of two protease
RT and several CUB domains.";
RL Biol. Reprod. 60:989-995(1999).
CC -!- FUNCTION: Converts the glycoprotein envelope surrounding the egg from
CC an unfertilizable to a fertilizable form during its transit through the
CC pars recta portion of the oviduct by selectively hydrolyzing the
CC envelope glycoprotein gp43. The egg envelope is converted to a sperm-
CC penetrable form, via an increase in sperm binding.
CC {ECO:0000269|PubMed:10084976}.
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:10084976};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10084976}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the pars recta oviduct.
CC {ECO:0000269|PubMed:10084976}.
CC -!- PTM: The catalytically inactive 110 kDa form is processed both N- and
CC C-terminally to give rise to the 66 kDa catalytically active form.
CC {ECO:0000269|PubMed:10084976}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; U81291; AAB53972.1; -; mRNA.
DR PIR; T30338; T30338.
DR RefSeq; NP_001081896.1; NM_001088427.1.
DR AlphaFoldDB; P79953; -.
DR SMR; P79953; -.
DR MEROPS; S01.240; -.
DR GeneID; 398108; -.
DR KEGG; xla:398108; -.
DR CTD; 398108; -.
DR Xenbase; XB-GENE-955936; ovch2.S.
DR OrthoDB; 1314811at2759; -.
DR BRENDA; 3.4.21.120; 6725.
DR Proteomes; UP000186698; Chromosome 4S.
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; 3.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 3.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..45
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:10084976"
FT /id="PRO_0000261191"
FT CHAIN 46..583
FT /note="Ovochymase-2"
FT /id="PRO_0000261192"
FT PROPEP 584..1004
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000261193"
FT DOMAIN 46..295
FT /note="Peptidase S1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 309..419
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 429..541
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 580..820
FT /note="Peptidase S1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 136
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
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 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..87
FT /evidence="ECO:0000250"
FT DISULFID 170..240
FT /evidence="ECO:0000250"
FT DISULFID 201..219
FT /evidence="ECO:0000250"
FT DISULFID 230..259
FT /evidence="ECO:0000250"
FT DISULFID 363..382
FT /evidence="ECO:0000250"
FT DISULFID 429..456
FT /evidence="ECO:0000250"
FT DISULFID 483..504
FT /evidence="ECO:0000250"
FT DISULFID 609..625
FT /evidence="ECO:0000250"
FT DISULFID 706..776
FT /evidence="ECO:0000250"
FT DISULFID 737..754
FT /evidence="ECO:0000250"
FT DISULFID 766..796
FT /evidence="ECO:0000250"
SQ SEQUENCE 1004 AA; 110612 MW; 5ECACE265E6433CE CRC64;
MPTRNLLLGS ILLSLAVKGD PGPHRGARCG VSPLGSATEL NYLSRIVGGR ESKKGQHPWT
VSLKRNGKHF CGGTLVSHCH VLTAAHCLLD RNVKLYMRVY IGEYDQILKE ETEQMFRVIE
IFKHPNFNQS QPMNYDVAVL LLDGSVTFDE NIQPACLPNP DDVFEPGDLC VTLGWGHLTE
NGILPVVLQE VYLPIVDLSS CLHVMSALKG TVVSSYIVCA GFPEGGKDAC QGDSGGPLLC
QRRHGSWVLH GLTSWGMGCG RSWKNNVFLP HNRKGSPGIF TDIQKLLGWV SSQLNTAVPN
KNQESCSMQD GVLSGKSGEL IFLKNPMSVT RTMSGAPGFS LSLKTCTSCL NFTHLDIESD
FACNLDYLAI YTDSHRLIGK FCGDIPPRSL LISFSSIKLN FFSDFHENRT GFVLYYSAVE
PNTYPDSGCG SFAVLFEEGE IQSMNYPENY LSNSRCHWII HGPSGSYIKL QFEDFALEPS
DDCRSDYLAV YQDLAAEDKI ETFCGFSLPA PVYSTTAVMH IKFSTDERDN DKGFRATFTF
VSPNSLVEDS RQGNMPSTNK KETTAQDSIC GVSQVPPIFI YNSIAKVEEA VPHSWPWHTS
LQYAGEHVCD GAIIAENWIL TTASCVLNRK FNDVWLVDPG IHDLLRPGHN QKGLVKQIIP
HPSFSSQTND FDIALVELDE SLQFNSDIFP ICLPGKTSEL APASLCVVSG WSLRGKEAEK
STKLQQREVP ILTDDACSAH YIQNPGGITD RMLCAGIGTG QDNDSCSEQS GSPLVCLLEK
KGIYTIFGIA SWGVNCKENS KPGIYTKVSP FIDWIRQIMS DTGQIHSNLG DPKPHPMGNI
EPEETAGRDI IQGGFPTNDA SSNQNLYIAS SCEDVVLLQS PGEIKMETKS QMYPNGFSCQ
WRIIAPKFQI IKLVMKQVHM SAENGKCCNS LIIYEGISKN KTLKVRFPTD EMVPGTVWSE
GSSVTIESPP HPVDPEFGFC LVYSFHSRTQ SQDHVVPDSD SSEP
