ID   GA113_HUMAN             Reviewed;         666 AA.
AC   P62684;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Endogenous retrovirus group K member 113 Gag polyprotein;
DE   AltName: Full=HERV-K113 Gag protein;
DE   AltName: Full=HERV-K_19p13.11 provirus ancestral Gag polyprotein;
DE            Short=Gag polyprotein;
GN   Name=HERVK_113;
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=11591322; DOI=10.1016/s0960-9822(01)00455-9;
RA   Turner G., Barbulescu M., Su M., Jensen-Seaman M.I., Kidd K.K., Lenz J.;
RT   "Insertional polymorphisms of full-length endogenous retroviruses in
RT   humans.";
RL   Curr. Biol. 11:1531-1535(2001).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=7983737; DOI=10.1128/jvi.69.1.414-421.1995;
RA   Sauter M., Schommer S., Kremmer E., Remberger K., Doelken G., Lemm I.,
RA   Buck M., Best B., Neumann-Haefelin D., Mueller-Lantzsch N.;
RT   "Human endogenous retrovirus K10: expression of Gag protein and detection
RT   of antibodies in patients with seminomas.";
RL   J. Virol. 69:414-421(1995).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=1;
CC         Comment=This protein is synthesized as a Gag polypeptide and as a
CC         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,
CC         to be generated by -1 frameshifts occurring at the Gag-Pro and
CC         Pro-Pol genes boundaries.;
CC       Name=1;
CC         IsoId=P62684-1; Sequence=Displayed;
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: 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   -!- PTM: Specific enzymatic cleavages may yield mature proteins.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: Insertional polymorphism. Provirus present in 29% of
CC       tested individuals.
CC   -!- SIMILARITY: Belongs to the beta type-B retroviral Gag protein family.
CC       HERV class-II K(HML-2) gag subfamily. {ECO:0000305}.
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DR   EMBL; AY037928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P62684; -.
DR   SMR; P62684; -.
DR   IntAct; P62684; 2.
DR   BioMuta; HERVK_113; -.
DR   DMDM; 50400278; -.
DR   jPOST; P62684; -.
DR   MassIVE; P62684; -.
DR   PeptideAtlas; P62684; -.
DR   PRIDE; P62684; -.
DR   neXtProt; NX_P62684; -.
DR   PhylomeDB; P62684; -.
DR   Pharos; P62684; Tdark.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; P62684; protein.
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   1: Evidence at protein level;
KW   Cell membrane; ERV; Lipoprotein; Membrane; Metal-binding; Myristate;
KW   Reference proteome; Repeat; Ribosomal frameshifting; Transposable element;
KW   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 113 Gag
FT                   polyprotein"
FT                   /id="PRO_0000186748"
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          163..189
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..642
FT                   /note="Disordered"
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"
SQ   SEQUENCE   666 AA;  74038 MW;  BCCC8FEBA705743A CRC64;
     MGQTKSKIKS KYASYLSFIK ILLKRGGVKV STKNLIKLFQ IIEQFCPWFP EQGTLDLKDW
     KRIGKELKQA GRKGNIIPLT VWNDWAIIKA ALEPFQTEED SVSVSDAPGS CIIDCNEKTR
     KKSQKETESL HCEYVAEPVM AQSTQNADYN QLQEVIYPET LKLEGKGPEL MGPSESKPRG
     TSPLPAGQVP VTLQPQKQVK ENKTQPPVAY QYWPPAELQY QPPPESQYGY PGMPPAPQGR
     APYPQPPTRR LNPTAPPSRQ GSELHEIIDK SRKEGDTEAW QFPVTLELMP PGEGAQEGEP
     PTVEARYKSF SIKMLKDMKE GVKQYGPNSP YMRTLLDSIA HGHRLIPYDW EILAKSSLSP
     SQFLQFKTWW IDGVQEQVRR NRAANPPVNI DADQLLGIGQ NWSTISQQAL MQNEAIEQVR
     AICLRAWEKI QDPGSTCPSF NTVRQGSKEP YPDFVARLQD VAQKSIADEK ARKVIVELMA
     YENANPECQS AIKPLKGKVP AGSDVISEYV KACDGMGGAM HKAMLMAQAI TGVVLGGQVR
     TFGGKCYNCG QIGHLKKNCP VLNKQNITIQ ATTTGREPPD LCPRCKKGKH WASQCRSKFD
     KNGQPLSGNE QRGQPQAPQQ TGAFPIQPFV PQGFQGQQPP LSQVFQGISQ LPQYNNCPPP
     QAAVQQ