ID   VP113_HUMAN             Reviewed;         156 AA.
AC   P63121;
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 113 Pro protein;
DE   AltName: Full=HERV-K113 envelope protein;
DE   AltName: Full=HERV-K_19p13.11 provirus ancestral Pro protein;
DE            EC=3.4.23.50;
DE   AltName: Full=Protease;
DE   AltName: Full=Proteinase;
DE            Short=PR;
GN   Name=HERVK_113;
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].
RX   PubMed=11591322; DOI=10.1016/s0960-9822(01)00455-9;
RA   Turner G., Barbulescu M., Su M., Jensen-Seaman M.I., Kidd K.K., Lenz J.;
RT   "Insertional polymorphisms of full-length endogenous retroviruses in
RT   humans.";
RL   Curr. Biol. 11:1531-1535(2001).
CC   -!- FUNCTION: Retroviral proteases have roles in the processing of the
CC       primary 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.
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=P63121-1; 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   -!- MISCELLANEOUS: Insertional polymorphism. Provirus present in 29% of
CC       tested individuals.
CC   -!- SIMILARITY: Belongs to the peptidase A2 family. HERV class-II K(HML-2)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY037928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P63121; -.
DR   SMR; P63121; -.
DR   iPTMnet; P63121; -.
DR   PhosphoSitePlus; P63121; -.
DR   BioMuta; HERVK_113; -.
DR   DMDM; 52000852; -.
DR   PRIDE; P63121; -.
DR   neXtProt; NX_P63121; -.
DR   PhylomeDB; P63121; -.
DR   Pharos; P63121; Tdark.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; P63121; protein.
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 113 Pro
FT                   protein"
FT                   /id="PRO_0000199540"
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;  17136 MW;  819E241B3704A222 CRC64;
     WASQVSENRP VCKAIIQGKQ FEGLVDTGAD VSIIALNQWP KNWPKQKAVT GLVGISTASE
     VYQSTEILHC LGPDNQESTV QPMITSIPLN LWGRDLLQQW GVEITMPAPL YSPTSQKIMT
     KMGYIPGKGL GKNEDGIKVP VEAKINQERE GIGYPF