ID   VPK19_HUMAN             Reviewed;         156 AA.
AC   P63120;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   14-OCT-2015, entry version 66.
DE   RecName: Full=Endogenous retrovirus group K member 19 Pro protein;
DE   AltName: Full=HERV-K(C19) Pro protein;
DE   AltName: Full=HERV-K_19q12 provirus ancestral Pro protein;
DE            EC=3.4.23.50;
DE   AltName: Full=Protease;
DE   AltName: Full=Proteinase;
DE            Short=PR;
GN   Name=ERVK-19;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10516026;
RA   Toenjes R.R., Czauderna F., Kurth R.;
RT   "Genome wide screening, cloning, chromosomal assignment and expression
RT   of full-length human endogenous retrovirus type K (HERV-K).";
RL   J. Virol. 73:9187-9195(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
CC   -!- FUNCTION: Retroviral proteases have roles in the processing of the
CC       primary translation products and the maturation of the viral
CC       particle. Endogenous Pro proteins may have kept, lost or modified
CC       their original function during evolution.
CC   -!- CATALYTIC ACTIVITY: Processing at the authentic HIV-1 PR
CC       recognition site and release of the mature p17 matrix and the p24
CC       capsid protein, as a result of the cleavage of the -SQNY-|-PIVQ-
CC       cleavage site.
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
CC         at the Gag-Pro and Pro-Pol genes boundaries.;
CC       Name=1;
CC         IsoId=P63120-1; Sequence=Displayed;
CC   -!- PTM: Autoproteolytically processed at the N-terminus. Expected C-
CC       terminal autoprocessing not detected. The sequence shown is that
CC       of the processed Pro protein (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A2 family. HERV class-II
CC       K(HML-2) subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 G-patch domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00092}.
CC   -!- SIMILARITY: Contains 1 peptidase A2 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00275}.
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DR   EMBL; Y17833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC112702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; P63120; -.
DR   SMR; P63120; 9-99.
DR   PRIDE; P63120; -.
DR   GeneCards; ERVK-19; -.
DR   HGNC; HGNC:39026; ERVK-19.
DR   neXtProt; NX_P63120; -.
DR   HOVERGEN; HBG063893; -.
DR   PhylomeDB; P63120; -.
DR   NextBio; 35537778; -.
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   Gene3D; 2.40.70.10; -; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR018061; Pept_A2A_retrovirus_sg.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom.
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; Complete proteome; ERV;
KW   Hydrolase; Protease; Reference proteome; Ribosomal frameshifting;
KW   Transposable element.
FT   CHAIN         1    156       Endogenous retrovirus group K member 19
FT                                Pro protein.
FT                                /FTId=PRO_0000199538.
FT   DOMAIN       21     96       Peptidase A2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00275}.
FT   DOMAIN      111    156       G-patch. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00092}.
FT   ACT_SITE     26     26       {ECO:0000255|PROSITE-ProRule:PRU10094}.
FT   CONFLICT    126    126       L -> P (in Ref. 2). {ECO:0000305}.
SQ   SEQUENCE   156 AA;  17107 MW;  6D7D1ECF2B057AC3 CRC64;
     WASQVSENRP VCKAIIQGKQ FEGLVDTGAD VSIIALNQWP KNWPKQKAVT GLVGIGTASE
     VYQSTEILHC LGPDNQESTV QPMITSIPLN LWGRDLLQQW GAEITMPAPL YSPTSQKIMT
     KMGYILGKGL GKNEDGIKIP VEAKINQKRE GIGYPF
//