VPK18_HUMAN
ID VPK18_HUMAN Reviewed; 156 AA.
AC P63123;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Endogenous retrovirus group K member 18 Pro protein;
DE AltName: Full=HERV-K(C1a) Pro protein;
DE AltName: Full=HERV-K110 Pro protein;
DE AltName: Full=HERV-K18 Pro protein;
DE AltName: Full=HERV-K_1q23.3 provirus ancestral Pro protein;
DE EC=3.4.23.50;
DE AltName: Full=Protease;
DE AltName: Full=Proteinase;
DE Short=PR;
GN Name=ERVK-18;
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=10516026; DOI=10.1128/jvi.73.11.9187-9195.1999;
RA Toenjes R.R., Czauderna F., Kurth R.;
RT "Genome wide screening, cloning, chromosomal assignment and expression of
RT full-length human endogenous retrovirus type K (HERV-K).";
RL J. Virol. 73:9187-9195(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11672541; DOI=10.1016/s1074-7613(01)00212-6;
RA Stauffer Y., Marguerat S., Meylan F., Ucla C., Sutkowski N., Huber B.T.,
RA Pelet T., Conrad B.;
RT "Interferon-alpha induced endogenous superantigen: a model linking
RT environment and autoimmunity.";
RL Immunity 15:591-601(2001).
RN [3]
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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 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=P63123-1; 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: Intragenic, in the first intron of CD48 gene.
CC -!- SIMILARITY: Belongs to the peptidase A2 family. HERV class-II K(HML-2)
CC subfamily. {ECO:0000305}.
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DR EMBL; Y18890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF333072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P63123; -.
DR SMR; P63123; -.
DR BioMuta; HGNC:39025; -.
DR PRIDE; P63123; -.
DR GeneCards; ERVK-18; -.
DR HGNC; HGNC:39025; ERVK-18.
DR neXtProt; NX_P63123; -.
DR PhylomeDB; P63123; -.
DR Pharos; P63123; 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; ERV; Hydrolase; Protease; Reference proteome;
KW Ribosomal frameshifting; Transposable element.
FT CHAIN 1..156
FT /note="Endogenous retrovirus group K member 18 Pro protein"
FT /id="PRO_0000199542"
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"
FT CONFLICT 48
FT /note="T -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="I -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="V -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17101 MW; 5A5B1B3B97571E3D CRC64;
WASQVSENRP VCKAVIQGKQ LEGLVDTGAD VSIIALNQWP KNWPKQKTVT GLVGIVTASE
VYQSTEILHC LGPHNQESTV QPMITSIPLN LWGRDLLQQW GAEITMTATL YSPMSQKIMT
KMGYIPGKGL GKNEDGIKVP IEAKINHGRE GTGYPF
