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Database: UniProt
Entry: A0A0K9P7F4_ZOSMR
LinkDB: A0A0K9P7F4_ZOSMR
Original site: A0A0K9P7F4_ZOSMR 
ID   A0A0K9P7F4_ZOSMR        Unreviewed;       371 AA.
AC   A0A0K9P7F4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:KMZ64944.1};
GN   ORFNames=ZOSMA_342G00180 {ECO:0000313|EMBL:KMZ64944.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ64944.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(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:KMZ64944.1}.
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DR   EMBL; LFYR01001082; KMZ64944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9P7F4; -.
DR   STRING; 29655.A0A0K9P7F4; -.
DR   OMA; NDEFALM; -.
DR   OrthoDB; 5472443at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
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   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
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:SF1017; CLAN CA, FAMILY C1, CATHEPSIN L OR K-LIKE CYSTEINE PEPTIDASE; 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; PS00139; THIOL_PROTEASE_CYS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..371
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018587742"
FT   DOMAIN          38..95
FT                   /note="Cathepsin propeptide inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00848"
FT   DOMAIN          125..341
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   371 AA;  41568 MW;  1C129C022BACCAAB CRC64;
     MAIAVFIFGS MFFAIIMCPL ALASNSIVRP TDEVRRMYES WMVEHGKSYG SKEKETRFQI
     FQSNVQFVDD HNRPENGHSY TVGLNRFADL TNKEYRKIYL SKKPFEDLHG NASTRYSVNE
     GDVNIPASID WRSKGAVTSV KEQGKCGCCW AFTAVGAVEG INQIVTGKLV TLSAQELVDC
     DTGGFNHGCL GGNMYKAFEF IKNNGGIDTD ADYPYKTTQN TCDLNKKNTK IVTIDGYESL
     RPNDENALKN AVVHQPITVG IESYRREFQL YSNGIYQGPC SYNLDHGALV VGYGEADGVK
     YWILKNTWGT DWGEKGYMRI QRDSGNFYGK CGMTRVMSYP VKNAANLKMI DEDSLRIKII
     NDGGESRSLD E
//
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