Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endogenous retrovirus group K member 10 Pro protein

Gene

ERVK-10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Retroviral proteases have roles in 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. This endogenous protein has retained most of the characteristics of retroviral proteases.

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.2 Publications

Activity regulationi

Resistant to a number of clinically useful HIV-1 PR inhibitors. Inhibited by cyclic urea SD146.

Sites

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

GO - Molecular functioni

Keywordsi

Molecular functionAspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.50 2681

Names & Taxonomyi

Protein namesi
Recommended name:
Endogenous retrovirus group K member 10 Pro protein
Alternative name(s):
HERV-K10 Pro protein
HERV-K107 Pro protein
HERV-K_5q33.3 provirus ancestral Pro protein (EC:3.4.23.50)
Protease
Proteinase
Short name:
PR
Gene namesi
Name:ERVK-10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:39004 ERVK-10
neXtProtiNX_P10265

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26D → M: Loss of activity. 2 Publications1

Organism-specific databases

DisGeNETi100616101

Polymorphism and mutation databases

DMDMi52001472

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001995441 – 156Endogenous retrovirus group K member 10 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.

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PRIDEiP10265
ProteomicsDBi52588

PTM databases

iPTMnetiP10265
PhosphoSitePlusiP10265

Interactioni

Subunit structurei

Active as a homodimer.

Structurei

3D structure databases

ProteinModelPortaliP10265
SMRiP10265
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

Phylogenomic databases

HOVERGENiHBG063893
PhylomeDBiP10265

Family and domain databases

CDDicd05482 HIV_retropepsin_like, 1 hit
Gene3Di2.40.70.10, 1 hit
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR000467 G_patch_dom
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR034170 Retropepsin-like_cat_dom
IPR018061 Retropepsins
PfamiView protein in Pfam
PF01585 G-patch, 1 hit
PF00077 RVP, 1 hit
SMARTiView protein in SMART
SM00443 G_patch, 1 hit
SUPFAMiSSF50630 SSF50630, 1 hit
PROSITEiView protein in PROSITE
PS50175 ASP_PROT_RETROV, 1 hit
PS00141 ASP_PROTEASE, 1 hit
PS50174 G_PATCH, 1 hit

Sequence (1+)i

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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P10265-1) [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 KMGYIPGKGL GKNEDGIKVP VEAKINQERE

GIGYPF
Length:156
Mass (Da):17,108
Last modified:September 13, 2004 - v2
Checksum:iD2C94207A21DF68B
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
P10266POK10_HUMAN
Endogenous retrovirus group K membe...
ERVK-10
1,014Annotation score:
P87889GAK10_HUMAN
Endogenous retrovirus group K membe...
ERVK-10
666Annotation score:
P61580NP10_HUMAN
Endogenous retrovirus group K membe...
ERVK-10
75Annotation score:

Sequence cautioni

The sequence AAA88032 differs from that shown. Reason: Erroneous initiation.Curated

Mass spectrometryi

Molecular mass is 18230 Da from positions 1 - 156. Determined by MALDI. Reported mass includes mass of a C-terminal His6 tag, expressed in E.coli.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14123 Genomic DNA Translation: AAA88032.1 Different initiation.
AF164613 Genomic DNA Translation: AAD51796.1 Sequence problems.
AC016577 Genomic DNA No translation available.
PIRiC24483 PRHUER

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14123 Genomic DNA Translation: AAA88032.1 Different initiation.
AF164613 Genomic DNA Translation: AAD51796.1 Sequence problems.
AC016577 Genomic DNA No translation available.
PIRiC24483 PRHUER

3D structure databases

ProteinModelPortaliP10265
SMRiP10265
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP10265
PhosphoSitePlusiP10265

Polymorphism and mutation databases

DMDMi52001472

Proteomic databases

PRIDEiP10265
ProteomicsDBi52588

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

DisGeNETi100616101
GeneCardsiERVK-10
HGNCiHGNC:39004 ERVK-10
neXtProtiNX_P10265
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG063893
PhylomeDBiP10265

Enzyme and pathway databases

BRENDAi3.4.23.50 2681

Family and domain databases

CDDicd05482 HIV_retropepsin_like, 1 hit
Gene3Di2.40.70.10, 1 hit
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR000467 G_patch_dom
IPR001995 Peptidase_A2_cat
IPR021109 Peptidase_aspartic_dom_sf
IPR034170 Retropepsin-like_cat_dom
IPR018061 Retropepsins
PfamiView protein in Pfam
PF01585 G-patch, 1 hit
PF00077 RVP, 1 hit
SMARTiView protein in SMART
SM00443 G_patch, 1 hit
SUPFAMiSSF50630 SSF50630, 1 hit
PROSITEiView protein in PROSITE
PS50175 ASP_PROT_RETROV, 1 hit
PS00141 ASP_PROTEASE, 1 hit
PS50174 G_PATCH, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiVPK10_HUMAN
AccessioniPrimary (citable) accession number: P10265
Secondary accession number(s): Q9UKH6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: September 13, 2004
Last modified: September 12, 2018
This is version 128 of the entry and version 2 of the sequence. See 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, Direct protein sequencing, ERV, Reference proteome, Transposable element

Documents

  1. Human chromosome 5
    Human chromosome 5: 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again