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Protein

Phytepsin

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles.By similarity

Catalytic activityi

Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei102 – 1021
Active sitei289 – 2891

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.020.

Names & Taxonomyi

Protein namesi
Recommended name:
Phytepsin (EC:3.4.23.40)
Alternative name(s):
Aspartic proteinase
Cleaved into the following 4 chains:
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Propeptidei28 – 6639Activation peptidePRO_0000025903Add
BLAST
Chaini67 – 377311Phytepsin 32 kDa subunitPRO_0000025904Add
BLAST
Chaini67 – ?Phytepsin 29 kDa subunitPRO_0000025905
Chaini378 – 508131Phytepsin 16 kDa subunitPRO_0000025906Add
BLAST
Chaini422 – 50887Phytepsin 11 kDa subunitPRO_0000025907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi115 ↔ 121Combined sources1 Publication
Disulfide bondi280 ↔ 284Combined sources1 Publication
Disulfide bondi319 ↔ 413Combined sources1 Publication
Disulfide bondi344 ↔ 385Combined sources1 Publication
Disulfide bondi350 ↔ 382Combined sources1 Publication
Glycosylationi399 – 3991N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi427 ↔ 464Combined sources1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei377 – 3782Cleavage
Sitei421 – 4222Cleavage

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP42210.

Expressioni

Tissue specificityi

Embryo and leaf.

Interactioni

Subunit structurei

Heterodimer of two subunits (29 kDa and 11 kDa) processed from the precursor molecule. A large enzyme (32 kDa and 16 kDa) is an intermediate precursor form.1 Publication

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 376Combined sources
Helixi42 – 498Combined sources
Helixi74 – 763Combined sources
Helixi79 – 813Combined sources
Beta strandi84 – 907Combined sources
Turni91 – 944Combined sources
Beta strandi95 – 1028Combined sources
Beta strandi109 – 1124Combined sources
Helixi119 – 1235Combined sources
Helixi129 – 1313Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi149 – 16214Combined sources
Beta strandi165 – 17713Combined sources
Helixi182 – 1854Combined sources
Beta strandi187 – 1937Combined sources
Helixi197 – 1993Combined sources
Helixi201 – 2033Combined sources
Helixi207 – 2115Combined sources
Turni212 – 2154Combined sources
Beta strandi218 – 2258Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi247 – 25913Combined sources
Beta strandi262 – 2676Combined sources
Beta strandi270 – 2723Combined sources
Turni279 – 2824Combined sources
Beta strandi284 – 2885Combined sources
Beta strandi294 – 2974Combined sources
Helixi299 – 30911Combined sources
Helixi317 – 3259Combined sources
Helixi327 – 3359Combined sources
Helixi340 – 3467Combined sources
Helixi379 – 39719Combined sources
Helixi402 – 41211Combined sources
Beta strandi419 – 4213Combined sources
Helixi427 – 4304Combined sources
Beta strandi436 – 4405Combined sources
Beta strandi443 – 4475Combined sources
Helixi449 – 4524Combined sources
Beta strandi453 – 4553Combined sources
Helixi459 – 4613Combined sources
Beta strandi464 – 4707Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QDMX-ray2.30A/B/C31-478[»]
ProteinModelPortaliP42210.
SMRiP42210. Positions 31-508.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42210.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 505422Peptidase A1PROSITE-ProRule annotationAdd
BLAST
Domaini314 – 419106Saposin B-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation
Contains 1 saposin B-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

KOiK08245.

Family and domain databases

Gene3Di1.10.225.10. 2 hits.
2.40.70.10. 3 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR011001. Saposin-like.
IPR008139. SaposinB_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 2 hits.
PfamiPF00026. Asp. 1 hit.
PF05184. SapB_1. 1 hit.
PF03489. SapB_2. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SMARTiSM00741. SapB. 1 hit.
[Graphical view]
SUPFAMiSSF47862. SSF47862. 1 hit.
SSF50630. SSF50630. 2 hits.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
PS50015. SAP_B. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42210-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTRGLALAL LAAVLLLQTV LPAASEAEGL VRIALKKRPI DRNSRVATGL
60 70 80 90 100
SGGEEQPLLS GANPLRSEEE GDIVALKNYM NAQYFGEIGV GTPPQKFTVI
110 120 130 140 150
FDTGSSNLWV PSAKCYFSIA CYLHSRYKAG ASSTYKKNGK PAAIQYGTGS
160 170 180 190 200
IAGYFSEDSV TVGDLVVKDQ EFIEATKEPG ITFLVAKFDG ILGLGFKEIS
210 220 230 240 250
VGKAVPVWYK MIEQGLVSDP VFSFWLNRHV DEGEGGEIIF GGMDPKHYVG
260 270 280 290 300
EHTYVPVTQK GYWQFDMGDV LVGGKSTGFC AGGCAAIADS GTSLLAGPTA
310 320 330 340 350
IITEINEKIG AAGVVSQECK TIVSQYGQQI LDLLLAETQP KKICSQVGLC
360 370 380 390 400
TFDGTRGVSA GIRSVVDDEP VKSNGLRADP MCSACEMAVV WMQNQLAQNK
410 420 430 440 450
TQDLILDYVN QLCNRLPSPM GESAVDCGSL GSMPDIEFTI GGKKFALKPE
460 470 480 490 500
EYILKVGEGA AAQCISGFTA MDIPPPRGPL WILGDVFMGP YHTVFDYGKL

RIGFAKAA
Length:508
Mass (Da):54,226
Last modified:November 1, 1995 - v1
Checksum:i87F2C9F93369B962
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56136 mRNA. Translation: CAA39602.1.
PIRiS19697.

Genome annotation databases

KEGGiag:CAA39602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56136 mRNA. Translation: CAA39602.1.
PIRiS19697.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QDMX-ray2.30A/B/C31-478[»]
ProteinModelPortaliP42210.
SMRiP42210. Positions 31-508.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiA01.020.

Proteomic databases

PRIDEiP42210.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA39602.

Phylogenomic databases

KOiK08245.

Miscellaneous databases

EvolutionaryTraceiP42210.

Family and domain databases

Gene3Di1.10.225.10. 2 hits.
2.40.70.10. 3 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR007856. SapB_1.
IPR008138. SapB_2.
IPR011001. Saposin-like.
IPR008139. SaposinB_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 2 hits.
PfamiPF00026. Asp. 1 hit.
PF05184. SapB_1. 1 hit.
PF03489. SapB_2. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SMARTiSM00741. SapB. 1 hit.
[Graphical view]
SUPFAMiSSF47862. SSF47862. 1 hit.
SSF50630. SSF50630. 2 hits.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
PS50015. SAP_B. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D."
    Runeberg-Roos P., Toermaekangas K., Oestman A.
    Eur. J. Biochem. 202:1021-1027(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Kustaa.
    Tissue: Embryo.
  2. "Aspartic proteinase from barley seeds is related to animal cathepsin D."
    Toermaekangas K., Runeberg-Roos P., Oestman A., Tilgmann C., Sarkkinen P., Kervinen J., Mikola L., Kalkkinen N.
    Adv. Exp. Med. Biol. 306:355-359(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Kustaa.
    Tissue: Embryo.
  3. "Plant cells contain two functionally distinct vacuolar compartments."
    Paris N., Stanley C.M., Jones R.L., Rogers J.C.
    Cell 85:563-572(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting."
    Kervinen J., Tobin G.J., Costa J., Waugh D.S., Wlodawer A., Zdanov A.
    EMBO J. 18:3947-3955(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 31-508, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiASPR_HORVU
AccessioniPrimary (citable) accession number: P42210
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.