ID   VPK7_HUMAN              Reviewed;         156 AA.
AC   P63131; Q9UKI0;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   14-OCT-2015, entry version 67.
DE   RecName: Full=Endogenous retrovirus group K member 7 Pro protein;
DE   AltName: Full=HERV-K(III) Pro protein;
DE   AltName: Full=HERV-K102 Pro protein;
DE   AltName: Full=HERV-K_1q22 provirus ancestral Pro protein;
DE            EC=3.4.23.50;
DE   AltName: Full=Protease;
DE   AltName: Full=Proteinase;
DE            Short=PR;
GN   Name=ERVK-7;
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=10469592; DOI=10.1016/S0960-9822(99)80390-X;
RA   Barbulescu M., Turner G., Seaman M.I., Deinard A.S., Kidd K.K.,
RA   Lenz J.;
RT   "Many human endogenous retrovirus K (HERV-K) proviruses are unique to
RT   humans.";
RL   Curr. Biol. 9:861-868(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
CC   -!- FUNCTION: Retroviral proteases have roles in 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. This endogenous protein
CC       has retained most of the characteristics of retroviral proteases.
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=P63131-1; 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; AF164610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; P63131; -.
DR   SMR; P63131; 9-99.
DR   DMDM; 52000859; -.
DR   PRIDE; P63131; -.
DR   GeneCards; ERVK-7; -.
DR   HGNC; HGNC:31828; ERVK-7.
DR   MIM; 614013; gene.
DR   neXtProt; NX_P63131; -.
DR   HOVERGEN; HBG063893; -.
DR   PhylomeDB; P63131; -.
DR   NextBio; 35537788; -.
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 7
FT                                Pro protein.
FT                                /FTId=PRO_0000199546.
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      6      6       S -> T (in Ref. 1). {ECO:0000305}.
SQ   SEQUENCE   156 AA;  17078 MW;  C49D721F2B056702 CRC64;
     WASQVSENRP VCKAIIQGKQ FEGLVDTGAD VSIIALNQWP KNWPKQKAVT GLVGIGTASE
     VYQSTEILHC LGPDNQESTV QPMITSIPLN LWGRDLLQQW GAEITMPAPL YSPTSQKIMT
     KMGYIPGKGL GKNEDGIKVP VEAKINQERE GIGYPF
//