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Database: UniProt
Entry: A0A2J6LNG0_LACSA
LinkDB: A0A2J6LNG0_LACSA
Original site: A0A2J6LNG0_LACSA 
ID   A0A2J6LNG0_LACSA        Unreviewed;       442 AA.
AC   A0A2J6LNG0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Cysteine protease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LSAT_5X25740 {ECO:0000313|EMBL:PLY88863.1};
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY88863.1};
RN   [1] {ECO:0000313|EMBL:PLY88863.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28401891; DOI=10.1038/ncomms14953;
RA   Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA   Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA   Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT   "Genome assembly with in vitro proximity ligation data and whole-genome
RT   triplication in lettuce.";
RL   Nat. Commun. 8:14953-14953(2017).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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:PLY88863.1}.
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DR   EMBL; NBSK01002922; PLY88863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6LNG0; -.
DR   STRING; 4236.A0A2J6LNG0; -.
DR   EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_5X25740_mrna; cds-PLY88863.1; gene-LSAT_5X25740.
DR   Gramene; rna-gnl|WGS:NBSK|LSAT_5X25740_mrna; cds-PLY88863.1; gene-LSAT_5X25740.
DR   OrthoDB; 5472443at2759; -.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 2.10.25.160; Granulin; 1.
DR   InterPro; IPR000118; Granulin.
DR   InterPro; IPR037277; Granulin_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF414; OS05G0508300 PROTEIN; 1.
DR   Pfam; PF00396; Granulin; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00277; GRAN; 1.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57277; Granulin repeat; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Protease {ECO:0000256|ARBA:ARBA00022807}; Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..442
FT                   /note="Cysteine protease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018532869"
FT   DOMAIN          30..87
FT                   /note="Cathepsin propeptide inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00848"
FT   DOMAIN          120..335
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
FT   DOMAIN          352..409
FT                   /note="Granulins"
FT                   /evidence="ECO:0000259|SMART:SM00277"
FT   REGION          420..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   442 AA;  49219 MW;  8592BC4CEF0D75A5 CRC64;
     MGWLWWISAL FFFFLFPLTS LSTSYTSDLF RQWCQQHGKS YSTEEENLYR FNVFEDNYAY
     IIRHNSNSNS SYTLSLNSFA DLTHHEFKLA RLRGLSASAA SDDLIRLNRG SSLIESSSYL
     PKSLDWRDKG AVTNVKDQGS CGACWSFSAT GAMEGINQIV TGSLISLSEQ ELVDCDKSFN
     SGCEGGLMDY AYEFVIKNKG IDTEDDYPYQ AKQTSCNKNK RKRNIVTIDG YNDIPENNED
     QLLKAVANQP VSVGICGSER AFQLYSKGIF TGPCSTALDH AVLIVGYDSK DGVDYWIIKN
     SWGNSWGING YMYMARNTGD SHGLCGINML ASYPIKTSPN PPPSPTPKPV KCNLFSWCSE
     GETCCCASNF LGICLKWTCC ELNAAVCCKD HRHCCPSDYP ICDSERNLCL KQTNNGTLAI
     QPKKNSDSGN SGGRSTLHKQ YF
//
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