ID A0A176W007_MARPO Unreviewed; 458 AA.
AC A0A176W007;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE26377.1};
GN ORFNames=AXG93_4324s1450 {ECO:0000313|EMBL:OAE26377.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE26377.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE26377.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE26377.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAE26377.1}.
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DR EMBL; LVLJ01002190; OAE26377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176W007; -.
DR OrthoDB; 5472443at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_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:SF741; CATHEPSIN K; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..458
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018572494"
FT DOMAIN 48..107
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 142..357
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT REGION 110..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 49514 MW; AC1EAD2C06475DA0 CRC64;
MAVQISLLLL LVALRCVTGA CAEHTAPGGR GPDGLIDLES EGELRALYES WAVTHGVGRR
SASGEEERFA VFKANVRYIE EHNERARRTN GYRLGLNRFT GMSREEFRSR VGNASVAERG
EQRSATAESG RGDPQGWRKA KLPLLVDWRQ HGAVTGVKDQ GRCGSGWAFS ATGAVEGINK
IATGSLVSLS EQELLDCVAS DSGCDGAGRV DRAFQFIVDN GGIGTEDACP YNANQDVCDP
AVLDSRAVAI DGFEYVAASN EAELKKAVAR QPVSAMIEAT NNDLQFYSSG VFIGKCGSKI
DHAVLIVGYG SRNGRPFWLV KNSWGTSWGE KGYIRIERNG KSVDGKCGIA TMPSFPVKET
SRSWHAFVRK ELLFAMKVPG HGSAFGSNFV LEVALDRCAS SFYALHACFL LVFGHDLVNT
ELLPWQCCSL LFTSFGSALC DVVRSPIADR RMPGLPPA
//
