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Protein

Ovochymase-2

Gene

ovch2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts the glycoprotein envelope surrounding the egg from an unfertlizable to a fertlizable form during its transit through the pars recta portion of the oviduct by selectively hydrolyzing the envelope glycoprotein gp43. The egg envelope is converted to a sperm-penetrable form, via an increase in sperm binding.1 Publication

Catalytic activityi

Preferential cleavage at 371-Gly-Ser-Arg-|-Trp-374 of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei86Charge relay systemBy similarity1
Metal bindingi113CalciumBy similarity1
Active sitei136Charge relay systemBy similarity1
Active sitei234Charge relay systemBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.120. 6725.

Protein family/group databases

MEROPSiS01.240.

Names & Taxonomyi

Protein namesi
Recommended name:
Ovochymase-2 (EC:3.4.21.120)
Alternative name(s):
Oviductal protease
Oviductin
Gene namesi
Name:ovch2
Synonyms:ovtn
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-955936. ovch2.

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000026119120 – 45Activation peptide1 PublicationAdd BLAST26
ChainiPRO_000026119246 – 583Ovochymase-2Add BLAST538
PropeptideiPRO_0000261193584 – 1004Activation peptideSequence analysisAdd BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi71 ↔ 87By similarity
Glycosylationi128N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi170 ↔ 240By similarity
Disulfide bondi201 ↔ 219By similarity
Disulfide bondi230 ↔ 259By similarity
Glycosylationi351N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi363 ↔ 382By similarity
Glycosylationi408N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi429 ↔ 456By similarity
Disulfide bondi483 ↔ 504By similarity
Disulfide bondi609 ↔ 625By similarity
Disulfide bondi706 ↔ 776By similarity
Disulfide bondi737 ↔ 754By similarity
Glycosylationi763N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi766 ↔ 796By similarity
Glycosylationi940N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

The catalytically inactive 110 kDa form is processed both N- and C-terminally to give rise to the 66 kDa catalytically active form.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Tissue specificityi

Specifically expressed in the pars recta oviduct.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP79953.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 295Peptidase S1 1PROSITE-ProRule annotationAdd BLAST250
Domaini309 – 419CUB 1PROSITE-ProRule annotationAdd BLAST111
Domaini429 – 541CUB 2PROSITE-ProRule annotationAdd BLAST113
Domaini580 – 820Peptidase S1 2PROSITE-ProRule annotationAdd BLAST241

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 CUB domains.PROSITE-ProRule annotation
Contains 2 peptidase S1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOVERGENiHBG082093.
KOiK20111.

Family and domain databases

CDDicd00041. CUB. 3 hits.
cd00190. Tryp_SPc. 2 hits.
Gene3Di2.60.120.290. 3 hits.
InterProiIPR000859. CUB_dom.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 3 hits.
PF00089. Trypsin. 2 hits.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00042. CUB. 3 hits.
SM00020. Tryp_SPc. 2 hits.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 3 hits.
SSF50494. SSF50494. 2 hits.
PROSITEiPS01180. CUB. 2 hits.
PS50240. TRYPSIN_DOM. 2 hits.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P79953-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTRNLLLGS ILLSLAVKGD PGPHRGARCG VSPLGSATEL NYLSRIVGGR
60 70 80 90 100
ESKKGQHPWT VSLKRNGKHF CGGTLVSHCH VLTAAHCLLD RNVKLYMRVY
110 120 130 140 150
IGEYDQILKE ETEQMFRVIE IFKHPNFNQS QPMNYDVAVL LLDGSVTFDE
160 170 180 190 200
NIQPACLPNP DDVFEPGDLC VTLGWGHLTE NGILPVVLQE VYLPIVDLSS
210 220 230 240 250
CLHVMSALKG TVVSSYIVCA GFPEGGKDAC QGDSGGPLLC QRRHGSWVLH
260 270 280 290 300
GLTSWGMGCG RSWKNNVFLP HNRKGSPGIF TDIQKLLGWV SSQLNTAVPN
310 320 330 340 350
KNQESCSMQD GVLSGKSGEL IFLKNPMSVT RTMSGAPGFS LSLKTCTSCL
360 370 380 390 400
NFTHLDIESD FACNLDYLAI YTDSHRLIGK FCGDIPPRSL LISFSSIKLN
410 420 430 440 450
FFSDFHENRT GFVLYYSAVE PNTYPDSGCG SFAVLFEEGE IQSMNYPENY
460 470 480 490 500
LSNSRCHWII HGPSGSYIKL QFEDFALEPS DDCRSDYLAV YQDLAAEDKI
510 520 530 540 550
ETFCGFSLPA PVYSTTAVMH IKFSTDERDN DKGFRATFTF VSPNSLVEDS
560 570 580 590 600
RQGNMPSTNK KETTAQDSIC GVSQVPPIFI YNSIAKVEEA VPHSWPWHTS
610 620 630 640 650
LQYAGEHVCD GAIIAENWIL TTASCVLNRK FNDVWLVDPG IHDLLRPGHN
660 670 680 690 700
QKGLVKQIIP HPSFSSQTND FDIALVELDE SLQFNSDIFP ICLPGKTSEL
710 720 730 740 750
APASLCVVSG WSLRGKEAEK STKLQQREVP ILTDDACSAH YIQNPGGITD
760 770 780 790 800
RMLCAGIGTG QDNDSCSEQS GSPLVCLLEK KGIYTIFGIA SWGVNCKENS
810 820 830 840 850
KPGIYTKVSP FIDWIRQIMS DTGQIHSNLG DPKPHPMGNI EPEETAGRDI
860 870 880 890 900
IQGGFPTNDA SSNQNLYIAS SCEDVVLLQS PGEIKMETKS QMYPNGFSCQ
910 920 930 940 950
WRIIAPKFQI IKLVMKQVHM SAENGKCCNS LIIYEGISKN KTLKVRFPTD
960 970 980 990 1000
EMVPGTVWSE GSSVTIESPP HPVDPEFGFC LVYSFHSRTQ SQDHVVPDSD

SSEP
Length:1,004
Mass (Da):110,612
Last modified:May 1, 1997 - v1
Checksum:i5ECACE265E6433CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81291 mRNA. Translation: AAB53972.1.
PIRiT30338.
RefSeqiNP_001081896.1. NM_001088427.1.
UniGeneiXl.484.

Genome annotation databases

GeneIDi398108.
KEGGixla:398108.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81291 mRNA. Translation: AAB53972.1.
PIRiT30338.
RefSeqiNP_001081896.1. NM_001088427.1.
UniGeneiXl.484.

3D structure databases

ProteinModelPortaliP79953.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398108.
KEGGixla:398108.

Organism-specific databases

CTDi341277.
XenbaseiXB-GENE-955936. ovch2.

Phylogenomic databases

HOVERGENiHBG082093.
KOiK20111.

Enzyme and pathway databases

BRENDAi3.4.21.120. 6725.

Family and domain databases

CDDicd00041. CUB. 3 hits.
cd00190. Tryp_SPc. 2 hits.
Gene3Di2.60.120.290. 3 hits.
InterProiIPR000859. CUB_dom.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00431. CUB. 3 hits.
PF00089. Trypsin. 2 hits.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00042. CUB. 3 hits.
SM00020. Tryp_SPc. 2 hits.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 3 hits.
SSF50494. SSF50494. 2 hits.
PROSITEiPS01180. CUB. 2 hits.
PS50240. TRYPSIN_DOM. 2 hits.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOVCH2_XENLA
AccessioniPrimary (citable) accession number: P79953
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 1, 1997
Last modified: November 30, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.