VPK24_HUMAN
ID VPK24_HUMAN Reviewed; 156 AA.
AC P63129; Q9UKI1;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Endogenous retrovirus group K member 24 Pro protein;
DE AltName: Full=HERV-K101 envelope protein;
DE AltName: Full=HERV-K_22q11.21 provirus ancestral Pro protein;
DE EC=3.4.23.50;
DE AltName: Full=Protease;
DE AltName: Full=Proteinase;
DE Short=PR;
GN Name=ERVK-24;
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=10469592; DOI=10.1016/s0960-9822(99)80390-x;
RA Barbulescu M., Turner G., Seaman M.I., Deinard A.S., Kidd K.K., 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=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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=P63129-1; 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}.
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DR EMBL; AF164609; AAD51791.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P63129; -.
DR SMR; P63129; -.
DR MEROPS; A02.011; -.
DR iPTMnet; P63129; -.
DR PhosphoSitePlus; P63129; -.
DR BioMuta; HGNC:39038; -.
DR DMDM; 52000858; -.
DR PRIDE; P63129; -.
DR GeneCards; ERVK-24; -.
DR HGNC; HGNC:39038; ERVK-24.
DR neXtProt; NX_P63129; -.
DR PhylomeDB; P63129; -.
DR Pharos; P63129; 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 24 Pro protein"
FT /id="PRO_0000199545"
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 94..156
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17139 MW; BE3D1ECF2B056716 CRC64;
WASQVSENRP VCKAIIQGKQ FEGLVDTGAD VSIIALNQWP KNWPKQKAVT GLVGIGTASE
VYQSTEILHC LGPDNQESTV QPMITSIPLN LWGRDLLQQW GAEITMPAPL YSPTSQKIMT
KMGYIPGKGL GKNEDGIKIP FEAKINQKRE GIGYPF
