GAK7_HUMAN
ID GAK7_HUMAN Reviewed; 666 AA.
AC P63130; Q9UKI0;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Endogenous retrovirus group K member 7 Gag polyprotein;
DE AltName: Full=HERV-K(III) Gag protein;
DE AltName: Full=HERV-K102 Gag protein;
DE AltName: Full=HERV-K_1q22 provirus ancestral Gag polyprotein;
DE Short=Gag polyprotein;
GN Name=ERVK-7;
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=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: The products of the Gag polyproteins of infectious
CC retroviruses perform highly complex orchestrated tasks during the
CC assembly, budding, maturation, and infection stages of the viral
CC replication cycle. During viral assembly, the proteins form membrane
CC associations and self-associations that ultimately result in budding of
CC an immature virion from the infected cell. Gag precursors also function
CC during viral assembly to selectively bind and package two plus strands
CC of genomic RNA. Endogenous Gag proteins may have kept, lost or modified
CC their original function during evolution.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Note=Cytoplasmic
CC membrane (in a transfection system). {ECO:0000250}.
CC -!- DOMAIN: HERV-K Gag polyprotein contains regions homologous to the
CC matrix (MA), capsid (CA) and nucleocapsid (NC) proteins from infectious
CC retroviruses. Evidence suggests that HERV-K(HML-2) Gag polyprotein can
CC be cleaved into mature MA, CA and NC under certain circumstances.
CC However, the exact boundaries as well as the size of processed Gag
CC proteins have not been precisely determined yet.
CC -!- PTM: Specific enzymatic cleavages may yield mature proteins.
CC {ECO:0000305}.
CC -!- PTM: Myristoylation is essential for retroviral assembly. Alteration of
CC the glycine residue leads to a block in the budding of particles and an
CC accumulation of Gag inside the cell (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein is synthesized as a Gag polypeptide and as
CC a Gag-Pro-Pol polyprotein. The later is the precursor of the Pro and
CC Pol proteins. It is thought, by similarity with type-B retroviruses, to
CC be generated by -1 frameshifts occurring at the Gag-Pro and Pro-Pol
CC genes boundaries.
CC -!- MISCELLANEOUS: This Gag protein is encoded by a human specific
CC provirus.
CC -!- SIMILARITY: Belongs to the beta type-B retroviral Gag protein family.
CC HERV class-II K(HML-2) gag subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD51792.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AL353807; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF164610; AAD51792.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL353807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P63130; -.
DR SMR; P63130; -.
DR IntAct; P63130; 2.
DR BioMuta; HGNC:31828; -.
DR jPOST; P63130; -.
DR MassIVE; P63130; -.
DR PeptideAtlas; P63130; -.
DR PRIDE; P63130; -.
DR GeneCards; ERVK-7; -.
DR HGNC; HGNC:31828; ERVK-7.
DR MIM; 614013; gene.
DR neXtProt; NX_P63130; -.
DR PhylomeDB; P63130; -.
DR Pharos; P63130; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.490; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR003322; B_retro_matrix.
DR InterPro; IPR038124; B_retro_matrix_sf.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF02337; Gag_p10; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Cell membrane; ERV; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Repeat; Transposable element; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..666
FT /note="Endogenous retrovirus group K member 7 Gag
FT polyprotein"
FT /id="PRO_0000186755"
FT ZN_FING 544..561
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 580..597
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 165..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CONFLICT 99
FT /note="K -> E (in Ref. 1; AAD51792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 74111 MW; DFDDE865F85330D1 CRC64;
MGQTKSKIKS KYASYLSFIK ILLKRGGVKV STKNLIKLFQ IIEQFCPWFP EQGTLDLKDW
KRIGKELKQA GRKGNIIPLT VWNDWAIIKA ALEPFQTEKD SVSVSDALGS CIIDCNENTR
KKSQKETEGL HCEYVAEPVM AQSTQNVDYN QLQEVIYPET LKLEGKGPEL VGPSESKPRG
TSHLPAGQVP VTLQPQKQVK ENKTQPPVAY QYWPPAELQY RPPPESQYGY PGMPPAPQGR
APYPQPPTRR LNPTAPPSRQ GSELHEIIDK SRKEGDTEAW QFPVTLEPMP PGEGAQEGEP
PTVEARYKSF SIKMLKDMKE GVKQYGPNSP YMRTLLDSIA HGHRLIPYDW EILAKSSLSP
SQFLQFKTWW IDGVQEQVRR NRAANPPVNI DADQLLGIGQ NWSTISQQAL MQNEAIEQVR
AICLRAWEKI QDPGSTCPSF NTVRQGSKEP YPDFVARLQD VAQKSIADEK ARKVIVELMA
YENANPECQS AIKPLKGKVP AGSDVISEYV KACDGIGGAM HKAMLMAQAI TGVVLGGQVR
TFGGKCYNCG QIGHLKKNCP VLNKQNITIQ ATTTGREPPD LCPRCKKGKH WASQCRSKFD
KNGQPLSGNE QRGQPQAPQQ TGAFPIQPFV PQGFQEQQPP LSQVFQGISQ LPQYNNCPPP
QAAVQQ
