ID Q7YT66_9VEST Unreviewed; 398 AA.
AC Q7YT66;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=PC2 {ECO:0000313|EMBL:AAP41214.1};
DE Flags: Fragment;
OS Haliotis rubra (blacklip abalone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX NCBI_TaxID=36100 {ECO:0000313|EMBL:AAP41214.1};
RN [1] {ECO:0000313|EMBL:AAP41214.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pleuro-pedal ganglia {ECO:0000313|EMBL:AAP41214.1};
RA Hanna P.J., Cummins S.F.;
RT "Molecular analysis of prohormone convertases in Haliotis rubra (Blacklip
RT abalone).";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AY237916; AAP41214.1; -; mRNA.
DR AlphaFoldDB; Q7YT66; -.
DR MEROPS; S08.109; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016486; P:peptide hormone processing; IEA:UniProt.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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 PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 313..398
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 17
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 58
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP41214.1"
FT NON_TER 398
FT /evidence="ECO:0000313|EMBL:AAP41214.1"
SQ SEQUENCE 398 AA; 42864 MW; 9CAEBE3594FCD793 CRC64;
AWEMGYTGTD VTTAIMDDGI DYLHPDLRHN YSAEASYDFS SNDPYPYPRY TDTWFNSHGT
RCAGEVSAAR DNGVCGVGVA YGSKVAGLRM LDQPFMTDLI EANAMGHMPN LIDIYSASGR
PTDDGKTVDG PRNLTMRAIV NGVNNGRNGK GNIYVWSSGD GGPNDDCNCD GYAASMWTIS
INSATNDGQT AGYDESCSST LASTFSNGKA TSRDAGVATT DLYGNCTASH SGTSAAAPEA
AGVFALALDA NRNLTWRDIQ HLTVLTSKRN SLYDSNGVHE WKYNGAGLEF NHLFGYGVLD
AAAMVDLART WKGLPERFHC TAGSDSTERY FSICNPIRIT IDTDGCAGSD SEVNYLEHVQ
SFVTCESTFR GTVTIYLTSP MNATSMILSQ RPNDDDSK
//
