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Protein

Endogenous retrovirus group K member 9 Pro protein

Gene

ERVK-9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Retroviral proteases have roles in the processing of the primary translation products and the maturation of the viral particle. Endogenous Pro proteins may have kept, lost or modified their original function during evolution (By similarity).By similarity

Catalytic activityi

Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-|-PIVQ-cleavage site.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei26PROSITE-ProRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA02.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Endogenous retrovirus group K member 9 Pro protein
Alternative name(s):
HERV-K(C6) Pro protein
HERV-K109 Pro protein
HERV-K_6q14.1 provirus ancestral Pro protein (EC:3.4.23.50)
Protease
Proteinase
Short name:
PR
Gene namesi
Name:ERVK-9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:39005. ERVK-9.

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi52000857.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001995391 – 156Endogenous retrovirus group K member 9 Pro proteinAdd BLAST156

Post-translational modificationi

Autoproteolytically processed at the N-terminus. Expected C-terminal autoprocessing not detected. The sequence shown is that of the processed Pro protein (By similarity).By similarity

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PRIDEiP63127.

PTM databases

iPTMnetiP63127.
PhosphoSitePlusiP63127.

Interactioni

Subunit structurei

Active as a homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP63127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 96Peptidase A2PROSITE-ProRule annotationAdd BLAST76
Domaini111 – 156G-patchPROSITE-ProRule annotationAdd BLAST46

Sequence similaritiesi

Contains 1 G-patch domain.PROSITE-ProRule annotation
Contains 1 peptidase A2 domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG063893.
PhylomeDBiP63127.

Family and domain databases

Gene3Di2.40.70.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR000467. G_patch_dom.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
[Graphical view]
PfamiPF01585. G-patch. 1 hit.
PF00077. RVP. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50174. G_PATCH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by ribosomal frameshifting. AlignAdd to basket

Note: This protein is synthesized as Gag-Pro and Gag-Pro-Pol polyprotein. These polyproteins are thought, by similarity with type-B retroviruses, to be generated by -1 frameshifts occurring at the Gag-Pro and Pro-Pol genes boundaries.
Isoform 1 (identifier: P63127-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
WASQVSENRP VCKAIIQGKQ FEGLVDTGAD VSIIALNQWP KNWPKQKAVT
60 70 80 90 100
GLVGIGTASE VYQSMEILHC LGPDNQESTV QPMITSIPLN LWGRDLLQQW
110 120 130 140 150
GAEITMPAPL YSPTSQKIMT KRGYIPGKGL GKNEDGIKIP FEAKINQKRE

GIGYPF
Length:156
Mass (Da):17,194
Last modified:September 13, 2004 - v1
Checksum:iA8693D6F998DF69F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164615 Genomic DNA. Translation: AAD51799.1. Sequence problems.
AL590785 Genomic DNA. No translation available.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164615 Genomic DNA. Translation: AAD51799.1. Sequence problems.
AL590785 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliP63127.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiA02.011.

PTM databases

iPTMnetiP63127.
PhosphoSitePlusiP63127.

Polymorphism and mutation databases

DMDMi52000857.

Proteomic databases

PRIDEiP63127.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiERVK-9.
HGNCiHGNC:39005. ERVK-9.
neXtProtiNX_P63127.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG063893.
PhylomeDBiP63127.

Family and domain databases

Gene3Di2.40.70.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR000467. G_patch_dom.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
[Graphical view]
PfamiPF01585. G-patch. 1 hit.
PF00077. RVP. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
[Graphical view]
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50174. G_PATCH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVPK9_HUMAN
AccessioniPrimary (citable) accession number: P63127
Secondary accession number(s): Q9UKH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: November 2, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, ERV, Reference proteome, Transposable element

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  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.