ID   VPK25_HUMAN             Reviewed;         156 AA.
AC   P63125;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Endogenous retrovirus group K member 25 Pro protein;
DE   AltName: Full=HERV-K_11q22.1 provirus ancestral Pro protein;
DE            EC=3.4.23.50;
DE   AltName: Full=Protease;
DE   AltName: Full=Proteinase;
DE            Short=PR;
GN   Name=ERVK-25;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hattori M., Ishii K., Toyoda A., Taylor T.D., Hong-Seog P., Fujiyama A.,
RA   Yada T., Totoki Y., Watanabe H., Sakaki Y.;
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Retroviral proteases have roles in processing of the primary
CC       translation products and the maturation of the viral particle.
CC       Endogenous Pro proteins may have kept, lost or modified their original
CC       function during evolution. This endogenous protein has retained most of
CC       the characteristics of retroviral proteases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Processing at the authentic HIV-1 PR recognition site and
CC         release of the mature p17 matrix and the p24 capsid protein, as a
CC         result of the cleavage of the -SQNY-|-PIVQ- cleavage site.;
CC         EC=3.4.23.50;
CC   -!- SUBUNIT: Active as a homodimer. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=1;
CC         Comment=This protein is synthesized as Gag-Pro and Gag-Pro-Pol
CC         polyprotein. These polyproteins are thought, by similarity with
CC         type-B retroviruses, to be generated by -1 frameshifts occurring at
CC         the Gag-Pro and Pro-Pol genes boundaries.;
CC       Name=1;
CC         IsoId=P63125-1; Sequence=Displayed;
CC   -!- PTM: Autoproteolytically processed at the N-terminus. Expected C-
CC       terminal autoprocessing not detected. The sequence shown is that of the
CC       processed Pro protein (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A2 family. HERV class-II K(HML-2)
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP000776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P63125; -.
DR   SMR; P63125; -.
DR   iPTMnet; P63125; -.
DR   PhosphoSitePlus; P63125; -.
DR   BioMuta; HGNC:39039; -.
DR   DMDM; 52000856; -.
DR   PRIDE; P63125; -.
DR   GeneCards; ERVK-25; -.
DR   HGNC; HGNC:39039; ERVK-25.
DR   neXtProt; NX_P63125; -.
DR   PhylomeDB; P63125; -.
DR   Pharos; P63125; Tdark.
DR   Proteomes; UP000005640; Unplaced.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05482; HIV_retropepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR034170; Retropepsin-like_cat_dom.
DR   InterPro; IPR018061; Retropepsins.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF00077; RVP; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Autocatalytic cleavage; ERV; Hydrolase; Protease;
KW   Reference proteome; Ribosomal frameshifting; Transposable element.
FT   CHAIN           1..156
FT                   /note="Endogenous retrovirus group K member 25 Pro protein"
FT                   /id="PRO_0000199547"
FT   DOMAIN          21..96
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          111..156
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
SQ   SEQUENCE   156 AA;  17077 MW;  319F94FEB816CC81 CRC64;
     WASQVSENRP VCKAIIQGKQ FEGLVDTGAD VSIIALNQWP KNWPKQKAVT GLVGVGTASE
     VYQSTEILHC LGPDNQESTV QPMITSIPLN LWGRDLLQQW GAEITMPAPL YSPTSQKIMT
     KMGYIPGKGL GKNEDGIKIP VEAKINQKRE GIGYPF