ID A0A165ZBU3_DAUCS Unreviewed; 344 AA.
AC A0A165ZBU3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Cysteine protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=DCAR_012792 {ECO:0000313|EMBL:KZM99846.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM99846.1};
RN [1] {ECO:0000313|EMBL:KZM99846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM99846.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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:KZM99846.1}.
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DR EMBL; LNRQ01000004; KZM99846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ZBU3; -.
DR STRING; 79200.A0A165ZBU3; -.
DR EnsemblPlants; KZM99846; KZM99846; DCAR_012792.
DR Gramene; KZM99846; KZM99846; DCAR_012792.
DR Proteomes; UP000077755; Chromosome 4.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR000118; Granulin.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_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:SF937; CYSTEINE PROTEINASE RD21A; 1.
DR Pfam; PF00396; Granulin; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
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; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..344
FT /note="Cysteine protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018728512"
FT DOMAIN 44..101
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 132..322
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT DOMAIN 254..311
FT /note="Granulins"
FT /evidence="ECO:0000259|SMART:SM00277"
SQ SEQUENCE 344 AA; 37746 MW; F87BD177DE94C069 CRC64;
MKMILSLLSL SLLAAAVTAA DMSIITYDQT HAVGSTDDVI MAAYESWLVK HGKSYNALGE
KEQRFQIFKD NFLYIDEQNA VKDRSFKLGL NRFADLTNEE YRSKYTGIRT KDSRKKVSGK
SQRYASLAGE SLPESVDWRE HGAVASVKDQ GQCGSCWAFS TISAVEGINQ IATGKLITLS
EQELVDCDRS YNEGCNGGLM DDAFQFIINN GGIDSDADYP YTGRDGQCDQ YRSGVNPPNP
GPSPPSPKSP ESVCDEYYTC PMSTTCCCMY EYYGYCFAWG CCPLEGASCC DDGYSCCPHD
YPVCNVRAGT CSMSNNNPLG VKAIQRILAT PNWQHGSKGK KVTA
//