OVCH2_MOUSE
ID OVCH2_MOUSE Reviewed; 609 AA.
AC Q7M761; Q8BZQ8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ovochymase-2 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q7RTZ1};
DE AltName: Full=Oviductin {ECO:0000250|UniProtKB:P79953};
DE Flags: Precursor;
GN Name=Ovch2 {ECO:0000312|MGI:MGI:3045251}; Synonyms=Ovtn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Epididymis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION OF ISOFORM 1.
RC STRAIN=C57BL/6J;
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 [5]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND 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 (PubMed:32499443). In vitro, has an
CC endopeptidase activity (By similarity). {ECO:0000250|UniProtKB:Q7RTZ1,
CC ECO:0000269|PubMed:32499443}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P79953}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7M761-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7M761-2; Sequence=VSP_021668;
CC -!- TISSUE SPECIFICITY: Only expressed in uterus tissue (PubMed:20810007).
CC Expressed in the initial segment (IS) of the caput epididymis, the
CC region most proximal to the testis (PubMed:32499443).
CC {ECO:0000269|PubMed:20810007, ECO:0000269|PubMed:32499443}.
CC -!- DISRUPTION PHENOTYPE: Knockout male mice lacking OVCH2 are sterile.
CC {ECO:0000269|PubMed:32499443}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AK033776; BAC28471.1; -; mRNA.
DR EMBL; BC125284; AAI25285.1; -; mRNA.
DR EMBL; BC125288; AAI25289.1; -; mRNA.
DR EMBL; BN000123; CAD67553.1; -; mRNA.
DR CCDS; CCDS21692.1; -. [Q7M761-1]
DR RefSeq; NP_766496.2; NM_172908.3. [Q7M761-1]
DR AlphaFoldDB; Q7M761; -.
DR SMR; Q7M761; -.
DR STRING; 10090.ENSMUSP00000102366; -.
DR MEROPS; S01.320; -.
DR GlyGen; Q7M761; 5 sites.
DR PhosphoSitePlus; Q7M761; -.
DR PaxDb; Q7M761; -.
DR PRIDE; Q7M761; -.
DR ProteomicsDB; 294409; -. [Q7M761-1]
DR ProteomicsDB; 294410; -. [Q7M761-2]
DR Antibodypedia; 73573; 15 antibodies from 5 providers.
DR DNASU; 244199; -.
DR Ensembl; ENSMUST00000106755; ENSMUSP00000102366; ENSMUSG00000048236. [Q7M761-1]
DR GeneID; 244199; -.
DR KEGG; mmu:244199; -.
DR UCSC; uc009jbk.1; mouse. [Q7M761-1]
DR CTD; 341277; -.
DR MGI; MGI:3045251; Ovch2.
DR VEuPathDB; HostDB:ENSMUSG00000048236; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157791; -.
DR HOGENOM; CLU_034620_0_0_1; -.
DR InParanoid; Q7M761; -.
DR OMA; GAFQFDH; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q7M761; -.
DR TreeFam; TF326419; -.
DR BRENDA; 3.4.21.120; 3474.
DR BioGRID-ORCS; 244199; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q7M761; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7M761; protein.
DR Bgee; ENSMUSG00000048236; Expressed in anatomical structure and 1 other tissue.
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; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; IMP: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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Repeat; Secreted;
KW 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_0000261183"
FT CHAIN 52..609
FT /note="Ovochymase-2"
FT /id="PRO_0000261184"
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 REGION 580..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 356
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 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
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 VAR_SEQ 1..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021668"
SQ SEQUENCE 609 AA; 67611 MW; 4653B1DAC4A2E5FB CRC64;
MPISKDKLIL ILGMVCLEQG HSETLSSIRN PDCGQSLVKP QPQNYFSLFS RIVGGSQVEK
GSYPWQVSLK QKQKHICGGT IISSQWVITA AHCMANRNIA LTLNVTAGEH DLSQAEPGEQ
TLAIETIIIH PQFSTRKPMI YDIALLKMAG TFQFGQFVRP VCLPEPGEHF NAGFICTTAG
WGRLSEGGRL PQVLQQVNLP ILTQEECEAV LLTLKNPITG KTFLCTGSPD GGRDACQGDS
GGSLMCQNRK GAWTLAGVTS WGLGCGRSWR NNARKKEQGS PGIFTDLRRV LPWILKHIQT
GHRRKSTKAL CSEPDGLISG SEGELHFPES LHLYYESKQL CVWTFLVPED MHMLLNLSHL
DIESCHHNYL AMYSLEDRLV GKFCGENLPS SILIGSSSIR LRFISDATDY ATGFNLTYKA
LKPRYHPDSG CRSLTILFEE GTIQSLHYPE DYSNMASCTW IFQAPNYCLI KLSFQSLEIE
ENGDCSSDYV TVHSDVEKEK EIARFCDYVI PSPVLSSSSV MLISFQSDEN GTARGFQADI
SFISRADLNI SISEDESVPL ETWDLPPGAM EIFDAERDTH TKPPYEEDIG EMPAIDSGLL
KQGERRGKH
