ID   NECA_HYDVU              Reviewed;         793 AA.
AC   P29146;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=PC3-like endoprotease variant A;
DE            EC=3.4.21.-;
DE   AltName: Full=SPC3;
DE   Flags: Precursor;
OS   Hydra vulgaris (Hydra) (Hydra attenuata).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1495957; DOI=10.1073/pnas.89.15.6678;
RA   Chan S.J., Oliva A.A. Jr., Lamendola J., Grens A., Bode H., Steiner D.F.;
RT   "Conservation of the prohormone convertase gene family in metazoa: analysis
RT   of cDNAs encoding a PC3-like protein from hydra.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6678-6682(1992).
CC   -!- FUNCTION: Probably involved in the processing of hormone and other
CC       protein precursors at sites comprised of pairs of basic amino acid
CC       residues.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Variant A;
CC         IsoId=P29146-1; Sequence=Displayed;
CC       Name=Variant B;
CC         IsoId=P29145-1; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Predominantly in the body column.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M95931; AAA29214.1; -; mRNA.
DR   PIR; A46184; A46184.
DR   AlphaFoldDB; P29146; -.
DR   SMR; P29146; -.
DR   Proteomes; UP000694840; Unplaced.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 3.30.70.850; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..152
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000027073"
FT   CHAIN           153..793
FT                   /note="PC3-like endoprotease variant A"
FT                   /id="PRO_0000027074"
FT   DOMAIN          164..486
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          495..638
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        242
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        419
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        259..411
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..381
FT                   /evidence="ECO:0000250"
FT   DISULFID        501..527
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   793 AA;  88841 MW;  85E281C78B559D7D CRC64;
     MNYRGIYRRR YVFVLLLLVA VVNISYGWTV LKNKDYKRRY LSPSGVEKVR KHLSRKYVAS
     RNNTQTFKKH YFSNTWAVHI DPPDNDVADR IAKKHGFTNI GKIGNIEGHY HFKHEEIGER
     ELEKARHKTA LLNLEDEVKF AEQQKILERV KRDGIPNDPY FKDMWYLLNT GQASGPAGVD
     MNVVPVWKKN ITGRGIVISV LDDGLDWTHP DLEANYDQTA SIVLNDNDND PMPRDSDADN
     CHGTRCAGEA AAIANNGICG TGVAYNAKIG GVRMLDGQAT DALEASALGF RGDHIDIYIN
     CWGPKDDGKT FGKPGPMAAK ALRLGAEQGR NRLGSIFVWA TGNGGLTDDD CNCDGYTTSI
     FTISIGCIGD HGLSAYYTEK CSSTLAVTFN GASHKEGREN KMVTTDLYHQ CTEEFKGTSA
     SAPLAAGIIA LTLEANPLLT WRDVQALIVH TAQITSPVDE GWKRNGAGFH FNHKFGFGRL
     DANAMVNAAQ SWKNLPAQRK CTAASGFDHQ DIPRGDSLFI NIPTVACESS SAQIAKVEHV
     VLTVSFVHRR RGDVSIDLIS PKDTKSQMLS PRKYDDSDEG LDEWSFMTVY NWGENPKGIW
     RLKITDNPNQ DDVMNLFNGD NTDDVESLEE RVIDTQTKQN KAEWEKMRKE NPYFDVPYPT
     GVRKDKVLGS TEINDNSFDT PHTETFKIIR NHIPEVNLQN NDNMNTLNFD PVTGRKKNSI
     NKKIINSRKR NFLTFRNFLK KSKKVQVQQE ETGTQRVQVN AGYENPRISC ESGYTTCSGV
     LINYKLTFYG TGE