[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Leaf; DOI=10.1093/protein/8.1.59; PubMed=7770454 [NCBI, ExPASy, EBI, Israel, Japan] Taylor M.A., Baker K.C., Briggs G.S., Connerton I.F., Cummings N.J., Pratt K.A., Revell D.F., Freedman R.B., Goodenough P.W.; "Recombinant pro-regions from papain and papaya proteinase IV-are selective high affinity inhibitors of the mature papaya enzymes."; Protein Eng. 8:59-62(1995).
[2]	PROTEIN SEQUENCE OF 133-348. DOI=10.1016/0014-5793(89)81627-8; PubMed=2591528 [NCBI, ExPASy, EBI, Israel, Japan] Ritonja A., Buttle D.J., Rawlings N.D., Turk V., Barrett A.J.; "Papaya proteinase IV amino acid sequence."; FEBS Lett. 258:109-112(1989).
[3]	PROTEIN SEQUENCE OF 133-150. DOI=10.1016/0005-2795(79)90257-5; PubMed=518921 [NCBI, ExPASy, EBI, Israel, Japan] Lynn K.R., Yaguchi M.; "N-terminal homology in three cysteinyl proteases from Papaya latex."; Biochim. Biophys. Acta 581:363-364(1979).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 287-348. PubMed=3541893 [NCBI, ExPASy, EBI, Israel, Japan] McKee R.A., Adams S., Matthews J.A., Smith C.J., Smith H.; "Molecular cloning of two cysteine proteinases from paw-paw (Carica papaya)."; Biochem. J. 237:105-110(1986).
[5]	SUBSTRATE SPECIFICITY. DOI=10.1016/0014-5793(90)80101-N; PubMed=2404797 [NCBI, ExPASy, EBI, Israel, Japan] Buttle D.J., Ritonja A., Pearl L.H., Turk V., Barrett A.J.; "Selective cleavage of glycyl bonds by papaya proteinase IV."; FEBS Lett. 260:195-197(1990).
[6]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). DOI=10.1021/bi00040a034; PubMed=7548082 [NCBI, ExPASy, EBI, Israel, Japan] O'Hara B.P., Hemmings A.M., Buttle D.J., Pearl L.H.; "Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity."; Biochemistry 34:13190-13195(1995).

Comments

FUNCTION: Thiol protease with a substrate specificity very different from the other thiol proteases.
CATALYTIC ACTIVITY: Preferential cleavage: Gly-|-Xaa, in proteins and in small molecule substrates.
ENZYME REGULATION: Not inhibited by cystatin.
MISCELLANEOUS: Substitution of the conserved Gly residue by Glu-155 could possibly explain the unusual specificity.
SIMILARITY: Belongs to the peptidase C1 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X78056; CAA54974.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03970; CAA27608.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S06837; S06837.
T09798; T09798.

3D structure databases

PDB

1GEC; X-ray; 2.10 A; E=133-348.

[ExPASy / RCSB / EBI]

1GEC; -.

P05994; 38-348.

Protein family/group databases

MEROPS

C01.004; -.

Family and domain databases

InterPro

IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.

PANTHER

PTHR12411; Peptidase_C1A; 1.

Pfam

PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00705; PAPAIN.

ProDom

PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00645; Pept_C1; 1.
SMART graphical view of domain structure.

PROSITE

PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.

Other

P05994; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`Potential.`
`PROPEP`	`19 132`	`114`	`Activation peptide.`	`PRO_0000026412`
`CHAIN`	`133 348`	`216`	`Papaya proteinase 4.`	`PRO_0000026413`
`ACT_SITE`	`157 157`		`By similarity.`
`ACT_SITE`	`291 291`		`By similarity.`
`ACT_SITE`	`311 311`		`By similarity.`
`DISULFID`	`154 195`
`DISULFID`	`188 227`
`DISULFID`	`285 336`
`CONFLICT`	`190 190`		`K -> L (in Ref. 2; AA sequence).`
`TURN`	`139 143`	`5`
`STRAND`	`153 155`	`3`
`HELIX`	`157 174`	`18`
`HELIX`	`182 188`	`7`
`STRAND`	`190 192`	`3`
`HELIX`	`200 210`	`11`
`TURN`	`215 217`	`3`
`HELIX`	`229 232`	`4`
`STRAND`	`241 244`	`4`
`HELIX`	`250 257`	`8`
`STRAND`	`262 266`	`5`
`HELIX`	`271 274`	`4`
`STRAND`	`278 281`	`4`
`STRAND`	`291 301`	`11`
`STRAND`	`304 310`	`7`
`STRAND`	`322 326`	`5`
`HELIX`	`335 337`	`3`
`STRAND`	`343 346`	`4`

Sequence information

Length: 348 AA [This is the length of the unprocessed precursor]

Molecular weight: 39024 Da [This is the MW of the unprocessed precursor]

CRC64: 40855EDD37F68A8E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAIICSFSKL LFVAICLFGH MSLSYCDFSI VGYSQDDLTS TERLIQLFNS WMLKHNKNYK 

        70         80         90        100        110        120 
NVDEKLYRFE IFKDNLKYID ERNKMINGYW LGLNEFSDLS NDEFKEKYVG SLPEDYTNQP 

       130        140        150        160        170        180 
YDEEFVNEDI VDLPESVDWR AKGAVTPVKH QGYCESCWAF STVATVEGIN KIKTGNLVEL 

       190        200        210        220        230        240 
SEQELVDCDK QSYGCNRGYQ STSLQYVAQN GIHLRAKYPY IAKQQTCRAN QVGGPKVKTN 

       250        260        270        280        290        300 
GVGRVQSNNE GSLLNAIAHQ PVSVVVESAG RDFQNYKGGI FEGSCGTKVD HAVTAVGYGK 

       310        320        330        340 
SGGKGYILIK NSWGPGWGEN GYIRIRRASG NSPGVCGVYR SSYYPIKN

P05994 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools