ID A0A2G8K6F1_STIJA Unreviewed; 879 AA.
AC A0A2G8K6F1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative proprotein convertase subtilisin/kexin type 7 {ECO:0000313|EMBL:PIK43525.1};
GN ORFNames=BSL78_19623 {ECO:0000313|EMBL:PIK43525.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK43525.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK43525.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK43525.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK43525.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIK43525.1}.
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DR EMBL; MRZV01000843; PIK43525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8K6F1; -.
DR STRING; 307972.A0A2G8K6F1; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 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 InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR PANTHER; PTHR42884:SF28; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 7; 1.
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; 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 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 471..606
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 189..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 396
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 879 AA; 96872 MW; A17DF9EEDFC10B45 CRC64;
MFLQFLPRVV HKELTPGEIQ ISSSAMQNTL SWGVKLQTTS HRKHSNNRTR LDLLADEIAY
GASLRNHGQV GELYGHYLFM HKLFLEALNG TLDSSWIKSI QEETELILRN DPSVEWAHRQ
WIRRRSKRSV VEFEDPMYPK QWHLHNTKTR GMDINVTDIW LHNITGEGVV VAVIDDGLEW
TNPDIRDNYS PQGSCDLNSG DDNPMPELHP NGKNENRHGT RCAGEIAAVA NKKCGVGVAF
GAKVAGIRLL DGPMTDSLEA TAFNKHMQVN DIYSCSWGPD DDGKTVDGPH PLALAALQHG
VNSGRRGRGS VFVVASGNGG RNQDNCNYDG YANSMYTITI GAINEVGLMP YYAEECSALL
GVTFSSGTNK EHRNIVTTDW TLGKDKGCTN GHTGTSAAAP LAAGLIALSL QAKPCLSWRD
VQHLIVYSSF MVDPEHGDWS DNAAGFHHSH KHGFGEIKAW RLVNAAKVWR SVPWLTSLSS
SRMSVYKTIP ANNSPLVLNY KVTNSSAQFN EIATLEHVLV TVSLTHPSRG SLRIELISPS
GTTSVLATPR KLDVSPDGLK GWTFSTVRCW GEQPSGDWIL KIFDTGQSGE GILQEWKLVL
YGSMISPEEV QQRRQTVEDA MSGVYLDANL TEPCSFYWNP AVNEDQLLTT KTMRMLLLVS
ALITILAAYY TLEQAFCNQE DKDKYLEEYI DLERTRLERS KSSSNGDISS NNVAETRLVP
LAGDQVINNV ELTIETENSL IVAAEISPLS QKGSEEVDNS GRTGGADSSG KHRQEDEVIC
VDNSKPMSQV HKHSKEKLSE TVAYSSSNCE ALSAVNLGFA LEPFEDGTES GDLGLLSDQS
AIYKLERTQP SGTINNILSS HGNEENIDEI SECEPFLKS
//
