GAK5_HUMAN
ID GAK5_HUMAN Reviewed; 667 AA.
AC Q9HDB9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Endogenous retrovirus group K member 5 Gag polyprotein;
DE AltName: Full=HERV-K(II) Gag protein;
DE AltName: Full=HERV-K_3q12.3 provirus ancestral Gag polyprotein;
DE Short=Gag polyprotein;
GN Name=ERVK-5; Synonyms=ERVK5;
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=11401426; DOI=10.1006/geno.2001.6473;
RA Sugimoto J., Matsuura N., Kinjo Y., Takasu N., Oda T., Jinno Y.;
RT "Transcriptionally active HERV-K genes: identification, isolation, and
RT chromosomal mapping.";
RL Genomics 72:137-144(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=Q9HDB9-1; 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: Intergenic, closest flanking genes being RPL24 and
CC FLJ23047.
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; AB047240; BAB11759.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HDB9; -.
DR SMR; Q9HDB9; -.
DR iPTMnet; Q9HDB9; -.
DR PhosphoSitePlus; Q9HDB9; -.
DR BioMuta; HGNC:13757; -.
DR DMDM; 50400656; -.
DR jPOST; Q9HDB9; -.
DR MassIVE; Q9HDB9; -.
DR PeptideAtlas; Q9HDB9; -.
DR PRIDE; Q9HDB9; -.
DR ProteomicsDB; 81849; -. [Q9HDB9-1]
DR GeneCards; ERVK-5; -.
DR HGNC; HGNC:13757; ERVK-5.
DR MIM; 614012; gene.
DR neXtProt; NX_Q9HDB9; -.
DR InParanoid; Q9HDB9; -.
DR PhylomeDB; Q9HDB9; -.
DR Pharos; Q9HDB9; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9HDB9; 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..667
FT /note="Endogenous retrovirus group K member 5 Gag
FT polyprotein"
FT /id="PRO_0000186751"
FT ZN_FING 543..560
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 166..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 667 AA; 73588 MW; 036A2C9D6647649A CRC64;
MGQTKSKTKS KYASYLSFIK ILLKRGGVRV STKNLIKLFQ IIEQFCPWFP EQGTLDLKDW
KRIGEELKQA GRKGNIIPLT VWNDWAIIKA ALEPFQTKED SVSVSDAPGS CVIDCNEKTG
RKSQKETESL HCEYVTEPVM AQSTQNVDYN QLQGVIYPET LKLEGKGPEL VGPSESKPRG
PSPLPAGQVP VTLQPQTQVK ENKTQPPVAY QYWPPAELQY LPPPESQYGY PGMPPALQGR
APYPQPPTVR LNPTASRSGQ GGTLHAVIDE ARKQGDLEAW RFLVILQLVQ AGEETQVGAP
ARAETRCEPF TMKMLKDIKE GVKQYGSNSP YIRTLLDSIA HGNRLTPYDW ESLAKSSLSS
SQYLQFKTWW IDGVQEQVRK NQATKPTVNI DADQLLGTGP NWSTINQQSV MQNEAIEQVR
AICLRAWGKI QDPGTAFPIN SIRQGSKEPY PDFVARLQDA AQKSITDDNA RKVIVELMAY
ENANPECQSA IKPLKGKVPA GVDVITEYVK ACDGIGGAMH KAMLMAQAMR GLTLGGQVRT
FGKKCYNCGQ IGHLKRSCPV LNKQNIINQA ITAKNKKPSG LCPKCGKGKH WANQCHSKFD
KDGQPLSGNR KRGQPQAPQQ TGAFPVQLFV PQGFQGQQPL QKIPPLQGVS QLQQSNSCPA
PQQAAPQ
