CUCM1_CUCME
ID CUCM1_CUCME Reviewed; 731 AA.
AC Q39547; Q940D5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cucumisin {ECO:0000303|PubMed:7806492};
DE EC=3.4.21.25 {ECO:0000305|PubMed:7806492};
DE AltName: Allergen=Cuc m 1 {ECO:0000303|PubMed:12801320};
DE Flags: Precursor;
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 111-123 AND 616-622, TISSUE
RP SPECIFICITY, AND PROTEOLYTIC PROCESSING.
RC STRAIN=cv. Reticulatus / Teresa; TISSUE=Fruit;
RX PubMed=7806492; DOI=10.1016/s0021-9258(20)30051-x;
RA Yamagata H., Masuzawa T., Nagaoka Y., Ohnishi T., Iwasaki T.;
RT "Cucumisin, a serine protease from melon fruits, shares structural homology
RT with subtilisin and is generated from a large precursor.";
RL J. Biol. Chem. 269:32725-32731(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Reticulatus / Teresa; TISSUE=Fruit;
RX PubMed=11782472; DOI=10.1074/jbc.m109946200;
RA Yamagata H., Yonesu K., Hirata A., Aizono Y.;
RT "TGTCACA motif is a novel cis-regulatory enhancer element involved in
RT fruit-specific expression of the cucumisin gene.";
RL J. Biol. Chem. 277:11582-11590(2002).
RN [3]
RP PROTEIN SEQUENCE OF 111-118, AND ALLERGEN.
RX PubMed=12801320; DOI=10.1046/j.1365-2222.2003.01680.x;
RA Cuesta-Herranz J., Pastor C., Figueredo E., Vidarte L., De las Heras M.,
RA Duran C., Fernandez-Caldas E., de Miguel J., Vivanco F.;
RT "Identification of Cucumisin (Cuc m 1), a subtilisin-like endopeptidase, as
RT the major allergen of melon fruit.";
RL Clin. Exp. Allergy 33:827-833(2003).
RN [4]
RP PROTEIN SEQUENCE OF 466-468 AND 652-654, AND GLYCOSYLATION AT ASN-466 AND
RP ASN-652.
RX AGRICOLA=IND87003744;
RA Kaneda M., Kamikubo Y., Tominaga N.;
RT "Amino acid sequences of glycopeptides from Cucumisin.";
RL Agric. Biol. Chem. 50:2413-2414(1986).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 111-731, GLYCOSYLATION AT ASN-466
RP AND ASN-652, DISULFIDE BONDS, ACTIVE SITE, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Prince;
RX PubMed=22841692; DOI=10.1016/j.jmb.2012.07.013;
RA Murayama K., Kato-Murayama M., Hosaka T., Sotokawauchi A., Yokoyama S.,
RA Arima K., Shirouzu M.;
RT "Crystal structure of cucumisin, a subtilisin-like endoprotease from
RT Cucumis melo L.";
RL J. Mol. Biol. 423:386-396(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 111-731 AND 23-110, GLYCOSYLATION
RP AT ASN-466 AND ASN-652, AND DISULFIDE BONDS.
RA Murayama K., Kato-Murayama M., Yokoyama S., Arima K., Shirouzu M.;
RT "Crystal structure of Cucumisin complexed with pro-peptide.";
RL Submitted (MAR-2015) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity.; EC=3.4.21.25;
CC Evidence={ECO:0000305|PubMed:7806492};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Melting point at 81 degrees Celsius. {ECO:0000269|Ref.6};
CC -!- SUBUNIT: Monomer and dimer. {ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in fruits. Expressed in
CC sarcocarp (at protein level). {ECO:0000269|PubMed:11782472,
CC ECO:0000269|PubMed:7806492}.
CC -!- PTM: The C-terminal propeptide is autocleaved.
CC {ECO:0000269|PubMed:7806492}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:12801320}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; D32206; BAA06905.1; -; mRNA.
DR EMBL; AY055805; AAL25196.1; -; Genomic_DNA.
DR PIR; A55800; A55800.
DR PDB; 3VTA; X-ray; 2.75 A; A/B=111-731.
DR PDB; 4YN3; X-ray; 1.95 A; A=111-731, B=23-110.
DR PDBsum; 3VTA; -.
DR PDBsum; 4YN3; -.
DR AlphaFoldDB; Q39547; -.
DR SMR; Q39547; -.
DR Allergome; 255; Cuc m 1.
DR Allergome; 3229; Cuc m 1.0101.
DR MEROPS; S08.092; -.
DR iPTMnet; Q39547; -.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR BRENDA; 3.4.21.25; 1735.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
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; PTHR10795; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Autocatalytic cleavage; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..110
FT /note="Activation peptide"
FT /id="PRO_0000027003"
FT CHAIN 111..615
FT /note="Cucumisin"
FT /id="PRO_0000027004"
FT PROPEP 616..731
FT /id="PRO_0000027005"
FT DOMAIN 34..110
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 114..584
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000305|Ref.6"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000305|Ref.6"
FT ACT_SITE 525
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000305|Ref.6"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22841692, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.6, ECO:0007744|PDB:3VTA,
FT ECO:0007744|PDB:4YN3"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22841692, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.6, ECO:0007744|PDB:3VTA,
FT ECO:0007744|PDB:4YN3"
FT DISULFID 166..174
FT /evidence="ECO:0000269|PubMed:22841692, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:3VTA, ECO:0007744|PDB:4YN3"
FT DISULFID 245..250
FT /evidence="ECO:0000269|PubMed:22841692, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:3VTA, ECO:0007744|PDB:4YN3"
FT DISULFID 380..397
FT /evidence="ECO:0000269|PubMed:22841692, ECO:0000269|Ref.6,
FT ECO:0007744|PDB:3VTA, ECO:0007744|PDB:4YN3"
FT CONFLICT 118
FT /note="L -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4YN3"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3VTA"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:4YN3"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:4YN3"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:3VTA"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:4YN3"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:3VTA"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 438..448
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3VTA"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 524..541
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 547..556
FT /evidence="ECO:0007829|PDB:4YN3"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:4YN3"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 580..583
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 594..597
FT /evidence="ECO:0007829|PDB:4YN3"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:3VTA"
FT STRAND 635..640
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 647..657
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 663..670
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 675..686
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 692..701
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 704..718
FT /evidence="ECO:0007829|PDB:4YN3"
FT STRAND 720..728
FT /evidence="ECO:0007829|PDB:4YN3"
SQ SEQUENCE 731 AA; 78820 MW; 93270A9433A366ED CRC64;
MSSSLIFKLF FFSLFFSNRL ASRLDSDDDG KNIYIVYMGR KLEDPDSAHL HHRAMLEQVV
GSTFAPESVL HTYKRSFNGF AVKLTEEEAE KIASMEGVVS VFLNEMNELH TTRSWDFLGF
PLTVPRRSQV ESNIVVGVLD TGIWPESPSF DDEGFSPPPP KWKGTCETSN NFRCNRKIIG
ARSYHIGRPI SPGDVNGPRD TNGHGTHTAS TAAGGLVSQA NLYGLGLGTA RGGVPLARIA
AYKVCWNDGC SDTDILAAYD DAIADGVDII SLSVGGANPR HYFVDAIAIG SFHAVERGIL
TSNSAGNGGP NFFTTASLSP WLLSVAASTM DRKFVTQVQI GNGQSFQGVS INTFDNQYYP
LVSGRDIPNT GFDKSTSRFC TDKSVNPNLL KGKIVVCEAS FGPHEFFKSL DGAAGVLMTS
NTRDYADSYP LPSSVLDPND LLATLRYIYS IRSPGATIFK STTILNASAP VVVSFSSRGP
NRATKDVIKP DISGPGVEIL AAWPSVAPVG GIRRNTLFNI ISGTSMSCPH ITGIATYVKT
YNPTWSPAAI KSALMTTASP MNARFNPQAE FAYGSGHVNP LKAVRPGLVY DANESDYVKF
LCGQGYNTQA VRRITGDYSA CTSGNTGRVW DLNYPSFGLS VSPSQTFNQY FNRTLTSVAP
QASTYRAMIS APQGLTISVN PNVLSFNGLG DRKSFTLTVR GSIKGFVVSA SLVWSDGVHY
VRSPITITSL V
