OVCH_HALRO
ID OVCH_HALRO Reviewed; 1575 AA.
AC A0A182C2Z2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Ovochymase {ECO:0000303|PubMed:26896838};
DE Short=HrOVCH {ECO:0000303|PubMed:26896838};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274};
DE Flags: Precursor;
GN Name=OVCH {ECO:0000303|PubMed:26896838};
OS Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Pyuridae; Halocynthia.
OX NCBI_TaxID=7729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND FUNCTION.
RX PubMed=26896838; DOI=10.1002/mrd.22627;
RA Mino M., Sawada H.;
RT "Follicle cell trypsin-like protease HrOvochymase: Its cDNA cloning,
RT localization, and involvement in the late stage of oogenesis in the
RT ascidian Halocynthia roretzi.";
RL Mol. Reprod. Dev. 83:347-358(2016).
CC -!- FUNCTION: May be responsible for elevation of the vitelline coat at the
CC late developmental stage of oogenesis and during fertilization in
CC ovarian eggs. {ECO:0000269|PubMed:26896838}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P79953}.
CC -!- TISSUE SPECIFICITY: Expressed in the testis and ovary. Expressed in the
CC gonads and gametes. Expressed in the follicle cells covering the
CC vitelline coat of ovarian egg. {ECO:0000269|PubMed:26896838}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LC102208; BAV13855.1; -; mRNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0009566; P:fertilization; IDA:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 4.
DR CDD; cd00190; Tryp_SPc; 3.
DR Gene3D; 2.40.10.10; -; 4.
DR Gene3D; 2.60.120.290; -; 5.
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; 5.
DR Pfam; PF00089; Trypsin; 3.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 6.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF49854; SSF49854; 6.
DR SUPFAM; SSF50494; SSF50494; 3.
DR PROSITE; PS01180; CUB; 6.
DR PROSITE; PS50240; TRYPSIN_DOM; 3.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Repeat; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1575
FT /note="Ovochymase"
FT /evidence="ECO:0000255"
FT /id="PRO_5008116124"
FT DOMAIN 36..280
FT /note="Peptidase S1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 300..423
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 432..545
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 575..810
FT /note="Peptidase S1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 830..949
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 956..1070
FT /note="CUB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1080..1197
FT /note="CUB 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1221..1341
FT /note="CUB 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 1314..1575
FT /note="Peptidase S1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 76
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 227
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 617
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 665
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 760
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 968
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1027
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1087
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 61..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 166..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 199..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 223..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 300..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 358..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 432..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 486..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 602..618
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 700..766
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 730..745
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 756..786
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 830..859
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 889..913
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 956..984
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 1012..1034
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 1080..1108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 1135..1158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 1221..1246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 1376..1392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 1493..1507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 1575 AA; 174957 MW; 6CB7C22C89F06500 CRC64;
MIVTFVALAL SCCTPQVTAD CGLRPRLQSA IITGRIVGGE MAKLGEFPWQ AAFLYKHVQV
CGGTIIDTTW ILSAAHCFDP HMYKLQSIKK EDALIRVADL DKTDDTDEGE MTFEVKDIII
HEQYNRQTFD NDIMLIEILG SITYGPTVQP ACIPGANDAV ADGTKCLISG WGDTQDHVHN
RWPDKLQKAQ VEVFARAQCL AAYPESTENM ICAGLRTGGI DSCQGDSGGP LACPFTENTA
QPTFFLQGIV SWGRGCALDG FPGVYTEVRK YSSWIANYTQ HLLQDRNADV ATFTITGDPC
SSNGSIISGS EGDFSSPGFY SGSYTDNLDC KWIIQIPDIG SRIQLSFTEF GVEYHTFCWY
DDVKVYSGAV GNIASADAAD LLGSHCGMNI PSDLLSDGSS MTVIFHSDYM THTLGFRAVF
HAVSADVSQS GCGGIRELLT DHGEFSSKHY PNYYDADSIC ECFITAPTGK TIELNFLSFR
LAGSDCADNV AIYDGLNSSY PRIIRLCINQ GFNVTVPSSS NTMFVSFKTD GQVQDVGFEA
YYYFSSNGNS TDDTDYSQCG FSSTPINADQ TAARIVNGDI AIAGSWPWQI SIRLCDTCNH
YCGGSIISPS WIVTAAHCIE SSAHITYIRA GDFDRFTIEI SETIVPVAQI FIHPDYQKDL
PNNADIALLK LANPLSYSST IRPVCFPSQI STIPEENAEC YVTGWGLTEE NVMAQKLREA
KLPLMPYDQC LNVYTSYVLN ENMLCAGNIS SGIDTCLGDS GGPFVCRKSR NDPWILYGVS
AFGRECGSSR YPGVYTKVTR YIDWIIATAN VSTVTSVVEE HDPTEFEQGC IQLLVLSNHE
GDLSSPEYPE LYGEGMLDCQ WKIVLMDRTK SLNINFRFSH SQQDTAAACS LANIRISESY
SDGTVGRQYG PYCGSSESIL ISSLHDLVVS LHNSQSQVKI GLKLEYRLEE LEQSGCGQLK
HLIENKGNFS SINYPNIYSA NSHCEWYLHA SIATHYLQIS LSQFSLENAY QCRYDFLTVI
DVTENGNISH GPYCGNSIPH VITGHGLFHI KFRSDASLNY KGFFASFVEL NERPQEESGC
GGVKFLNGTN GTFQTAGFPL AYEANLDCTW VIEVEDGYKV RLNFQQFSLE SSSSCKYDWA
MLYNGEFAFE AQRIDTLCGY DVKLEDIFES TSNVMRIDFH SDFSFNKQGF LAMYTAVSPG
SSRSSVHQRE NHLQEKRSGG CQDSIFTDEE GVIEYKQGDH TGNTRCLFRI LTNHLHVIRL
WLRKLSSLNL HENDSIKIYD KIDVDDIYSG VVKPVFQFTG IIGYLDSLPA YLDYNGGEIS
MLFSSDGQHG DTSFELIYKL MQDKSSTTNP KQLWNDHHGK WPWMVSLFGS SKYYFCSGVI
ISSRWIATAA TCNLRSSEIH IIFPEGTNPK KIWEVEKIVV HPEFKMIYNV PQNDLALIQL
VDPIEHIPPV CLPVASNIYS DCHVLKIPRL AGSAAFPDIV RISSVDTLAH DICMREWHLR
ITDDMLCGRI NGTNSCQRDV GGPLVCQSPS DDAWYFVGIS SWGPKICNDN TAHHRLPDVY
VSVAYFLKWI TKIIQ
