NECB_HYDVU
ID NECB_HYDVU Reviewed; 710 AA.
AC P29145;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=PC3-like endoprotease variant B;
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 B;
CC IsoId=P29145-1; Sequence=Displayed;
CC Name=Variant A;
CC IsoId=P29146-1; 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; M95932; AAA29215.1; -; mRNA.
DR PIR; B46184; B46184.
DR AlphaFoldDB; P29145; -.
DR SMR; P29145; -.
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_0000027075"
FT CHAIN 153..710
FT /note="PC3-like endoprotease variant B"
FT /id="PRO_0000027076"
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 REGION 668..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 699
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 710 AA; 79321 MW; 4AE42DC15B2067FD 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 NPYFDVPYPN
GVRKNKVTIE GSTQDHVKPK EGAKEPWGNY RNTNNINNNS STAFKRKKKQ
