OVCH2_HUMAN
ID OVCH2_HUMAN Reviewed; 564 AA.
AC Q7RTZ1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ovochymase-2 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000269|PubMed:32499443};
DE AltName: Full=Oviductin {ECO:0000250|UniProtKB:P79953};
DE Flags: Precursor;
GN Name=OVCH2 {ECO:0000312|HGNC:HGNC:29970}; Synonyms=OVTN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP IDENTIFICATION.
RX PubMed=12838346; DOI=10.1038/nrg1111;
RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT "Human and mouse proteases: a comparative genomic approach.";
RL Nat. Rev. Genet. 4:544-558(2003).
RN [3]
RP FUNCTION.
RX PubMed=32499443; DOI=10.1126/science.aay5134;
RA Kiyozumi D., Noda T., Yamaguchi R., Tobita T., Matsumura T., Shimada K.,
RA Kodani M., Kohda T., Fujihara Y., Ozawa M., Yu Z., Miklossy G.,
RA Bohren K.M., Horie M., Okabe M., Matzuk M.M., Ikawa M.;
RT "NELL2-mediated lumicrine signaling through OVCH2 is required for male
RT fertility.";
RL Science 368:1132-1135(2020).
CC -!- FUNCTION: May be required for sperm ADAM3 processing and consequential
CC sperm fertilizing ability (By similarity). In vitro, has an
CC endopeptidase activity (PubMed:32499443).
CC {ECO:0000250|UniProtKB:Q7M761, ECO:0000269|PubMed:32499443}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P79953}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AC104237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000120; CAD66452.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7RTZ1; -.
DR SMR; Q7RTZ1; -.
DR STRING; 9606.ENSP00000484497; -.
DR MEROPS; S01.320; -.
DR GlyGen; Q7RTZ1; 4 sites.
DR iPTMnet; Q7RTZ1; -.
DR PhosphoSitePlus; Q7RTZ1; -.
DR BioMuta; OVCH2; -.
DR DMDM; 118573095; -.
DR MassIVE; Q7RTZ1; -.
DR PeptideAtlas; Q7RTZ1; -.
DR PRIDE; Q7RTZ1; -.
DR ProteomicsDB; 68941; -.
DR GeneCards; OVCH2; -.
DR HGNC; HGNC:29970; OVCH2.
DR MIM; 618962; gene.
DR neXtProt; NX_Q7RTZ1; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q7RTZ1; -.
DR PhylomeDB; Q7RTZ1; -.
DR PathwayCommons; Q7RTZ1; -.
DR SignaLink; Q7RTZ1; -.
DR ChiTaRS; OVCH2; human.
DR Pharos; Q7RTZ1; Tdark.
DR PRO; PR:Q7RTZ1; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q7RTZ1; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.290; -; 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 Pfam; PF00431; CUB; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Calcium; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..51
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000261181"
FT CHAIN 52..564
FT /note="Ovochymase-2"
FT /id="PRO_0000261182"
FT DOMAIN 52..299
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 311..421
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 431..543
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 92
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..93
FT /evidence="ECO:0000250"
FT DISULFID 176..246
FT /evidence="ECO:0000250"
FT DISULFID 207..225
FT /evidence="ECO:0000250"
FT DISULFID 236..265
FT /evidence="ECO:0000250"
FT DISULFID 311..341
FT /evidence="ECO:0000250"
FT DISULFID 365..384
FT /evidence="ECO:0000250"
FT DISULFID 431..458
FT /evidence="ECO:0000250"
FT DISULFID 485..506
FT /evidence="ECO:0000250"
FT VARIANT 19
FT /note="R -> Q (in dbSNP:rs7927138)"
FT /id="VAR_029097"
FT VARIANT 24
FT /note="T -> A (in dbSNP:rs12289558)"
FT /id="VAR_059786"
FT VARIANT 292
FT /note="P -> S (in dbSNP:rs10839849)"
FT /id="VAR_029098"
FT VARIANT 381
FT /note="G -> E (in dbSNP:rs3925028)"
FT /id="VAR_029099"
FT VARIANT 410
FT /note="N -> T (in dbSNP:rs4528317)"
FT /id="VAR_029100"
FT VARIANT 410
FT /note="N -> Y (in dbSNP:rs4528317)"
FT /id="VAR_057160"
FT VARIANT 413
FT /note="R -> G (in dbSNP:rs3925027)"
FT /id="VAR_029101"
FT VARIANT 526
FT /note="H -> Q (in dbSNP:rs4519083)"
FT /id="VAR_029102"
FT VARIANT 539
FT /note="T -> I (in dbSNP:rs4633461)"
FT /id="VAR_029103"
SQ SEQUENCE 564 AA; 62642 MW; 3AFC00C5C97F01F9 CRC64;
MLISRNKLIL LLGIVFFERG KSATLSLPKA PSCGQSLVKV QPWNYFNIFS RILGGSQVEK
GSYPWQVSLK QRQKHICGGS IVSPQWVITA AHCIANRNIV STLNVTAGEY DLSQTDPGEQ
TLTIETVIIH PHFSTKKPMD YDIALLKMAG AFQFGHFVGP ICLPELREQF EAGFICTTAG
WGRLTEGGVL SQVLQEVNLP ILTWEECVAA LLTLKRPISG KTFLCTGFPD GGRDACQGDS
GGSLMCRNKK GAWTLAGVTS WGLGCGRGWR NNVRKSDQGS PGIFTDISKV LPWIHEHIQT
GNRRKSSRAW CSEQDVIVSG AEGKLHFPES LHLYYESKQR CVWTLLVPEE MHVLLSFSHL
DVESCHHSYL SMYSLEDRPI GKFCGESLPS SILIGSNSLR LKFVSDATDN AARFNLTYKA
LKPNYIPDSG CSYLTVLFEE GLIQSLNYPE NYSDKANCDW IFQASKHHLI KLSFQSLEIE
ESGDCTSDYV TVHSDVERKK EIARLCGYDV PTPVLSPSSI MLISFHSDEN GTCRGFQATV
SFIPKAGKKI ELPTLWFPVL ILVM
