ID A0A1U8K442_GOSHI Unreviewed; 761 AA.
AC A0A1U8K442;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Subtilisin-like protease SBT1.7 {ECO:0000313|RefSeq:XP_016697280.1};
GN Name=LOC107913264 {ECO:0000313|RefSeq:XP_016697280.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016697280.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016697280.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016697280.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR RefSeq; XP_016697280.1; XM_016841791.1.
DR AlphaFoldDB; A0A1U8K442; -.
DR STRING; 3635.A0A1U8K442; -.
DR PaxDb; 3635-A0A1U8K442; -.
DR GeneID; 107913264; -.
DR KEGG; ghi:107913264; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000189702; Chromosome 21.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF469; SUBTILISIN-LIKE PROTEASE SBT1.7; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000189702};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..761
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010573982"
FT DOMAIN 33..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 132..582
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 385..458
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 658..758
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 199..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 543
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 761 AA; 80743 MW; E38C3F30F2A955A6 CRC64;
MEMVKCFMIV LILGLCHVSM VAPLEEKKSH RKTYIVHMAK SEMPPSFQHH THWYDSSLKS
VSGSAAMLYT YDNVIHGFST QLTDKEAEQL ESQPGILAVL PEVRYELHTT RTPEFLGLSQ
AAALFPESES ASEVVIGVLD TGVWPESKSF ADTGLGPIPS SWKGACESGT NFTSANCNKK
LIGARYFAKG YEAALGAIDE TKESRSPRDD DGHGTHTAST AAGSVVEGAS LFGYAQGTAR
GMATRARVAV YKVCWMGGCF SSDILAAMEK AIDDNVNVLS MSLGGGMSDY YRDSVAIGSF
AAMEKGILVS CSAGNAGPAP YSLSNLAPWI TTVGAGTLDR DFPAFVSLGN GKNFSGVSLY
RGSPLPGKML PFVYAGNASN ATNGNLCMMD TLIPEKVAGK IVLCDRGMNA RVQKGAVVKA
AGGIGMVLSN TAANGEELVA DAHLLPATAV GQKSGDAIRD YLFSNPNPTV TILFEGTKVG
IEPSPVVAAF SSRGPNSITS EILKPDMIAP GVNILAGWSG AVGPTGLATD TRRVDFNIIS
GTSMSCPHVS GLAGLLKAAH PDWSPAAIRS ALMTTAYTEY KNKQKMQDIA TGKPSTPFDH
GAGHVDPVSA LNPGLVYDLT AEDYLGFLCA LNYTEFQIRS LARRNFSCDA SKRYRVTDLN
YPSFAVNFDS IMGGSNVVKH TRTLTNVGSP GTYKVSVSPE TPGVKISVEP QTLSFSQANE
KKSYTVTFSG SSQPTGTNVF ARLEWSDMKY TVGSPIAISW T
//
