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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)DescriptionActionsGraphical viewLength
Active sitei1021
Active sitei2891

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
PropeptideiPRO_000002590328 – 66Activation peptideAdd BLAST39
ChainiPRO_000002590467 – 377Phytepsin 32 kDa subunitAdd BLAST311
ChainiPRO_000002590567 – ?Phytepsin 29 kDa subunit
ChainiPRO_0000025906378 – 508Phytepsin 16 kDa subunitAdd BLAST131
ChainiPRO_0000025907422 – 508Phytepsin 11 kDa subunitAdd BLAST87

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Glycosylationi399N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi427 ↔ 464Combined sources1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei377 – 378Cleavage2
Sitei421 – 422Cleavage2

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

1508
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 37Combined sources6
Helixi42 – 49Combined sources8
Helixi74 – 76Combined sources3
Helixi79 – 81Combined sources3
Beta strandi84 – 90Combined sources7
Turni91 – 94Combined sources4
Beta strandi95 – 102Combined sources8
Beta strandi109 – 112Combined sources4
Helixi119 – 123Combined sources5
Helixi129 – 131Combined sources3
Beta strandi141 – 146Combined sources6
Beta strandi149 – 162Combined sources14
Beta strandi165 – 177Combined sources13
Helixi182 – 185Combined sources4
Beta strandi187 – 193Combined sources7
Helixi197 – 199Combined sources3
Helixi201 – 203Combined sources3
Helixi207 – 211Combined sources5
Turni212 – 215Combined sources4
Beta strandi218 – 225Combined sources8
Beta strandi236 – 240Combined sources5
Beta strandi247 – 259Combined sources13
Beta strandi262 – 267Combined sources6
Beta strandi270 – 272Combined sources3
Turni279 – 282Combined sources4
Beta strandi284 – 288Combined sources5
Beta strandi294 – 297Combined sources4
Helixi299 – 309Combined sources11
Helixi317 – 325Combined sources9
Helixi327 – 335Combined sources9
Helixi340 – 346Combined sources7
Helixi379 – 397Combined sources19
Helixi402 – 412Combined sources11
Beta strandi419 – 421Combined sources3
Helixi427 – 430Combined sources4
Beta strandi436 – 440Combined sources5
Beta strandi443 – 447Combined sources5
Helixi449 – 452Combined sources4
Beta strandi453 – 455Combined sources3
Helixi459 – 461Combined sources3
Beta strandi464 – 470Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP42210.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini84 – 505Peptidase A1PROSITE-ProRule annotationAdd BLAST422
Domaini314 – 419Saposin B-typePROSITE-ProRule annotationAdd BLAST106

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

CDDicd06098. phytepsin. 1 hit.
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.
IPR033869. Phytepsin.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QDMX-ray2.30A/B/C31-478[»]
ProteinModelPortaliP42210.
SMRiP42210.
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

CDDicd06098. phytepsin. 1 hit.
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.
IPR033869. Phytepsin.
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...

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: November 30, 2016
This is version 116 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.