GAK10_HUMAN
ID GAK10_HUMAN Reviewed; 666 AA.
AC P87889; P10263; P10264; Q69385; Q9UKH6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 4.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Endogenous retrovirus group K member 10 Gag polyprotein;
DE AltName: Full=HERV-K10 Gag protein;
DE AltName: Full=HERV-K107 Gag protein;
DE AltName: Full=HERV-K_5q33.3 provirus ancestral Gag polyprotein;
DE Short=Gag polyprotein;
GN Name=ERVK-10;
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=3021993; DOI=10.1128/jvi.60.2.589-598.1986;
RA Ono M., Yasunaga T., Miyata T., Ushikubo H.;
RT "Nucleotide sequence of human endogenous retrovirus genome related to the
RT mouse mammary tumor virus genome.";
RL J. Virol. 60:589-598(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9217052; DOI=10.1006/viro.1997.8614;
RA Toenjes R.R., Boller K., Limbach R., Lugert R., Kurth R.;
RT "Characterization of human endogenous retrovirus type K (HERV-K) virus-like
RT particles generated from recombinant baculoviruses.";
RL Virology 233:280-291(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8506289; DOI=10.1073/pnas.90.10.4480;
RA Loewer R., Boller K., Hasenmaier B., Korbmacher C., Mueller-Lantzsch N.,
RA Loewer J., Kurth R.;
RT "Identification of human endogenous retroviruses with complex mRNA
RT expression and particle formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4480-4484(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
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).
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=P87889-1; 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: This Gag protein is encoded by a human specific
CC provirus.
CC -!- MISCELLANEOUS: Intragenic, in the sixth intron of the SCGD gene.
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=AAA88030.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA88031.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD51796.1; Type=Frameshift; Note=A -1 frameshift presumed to occur within the codons for the last amino acids in the Gag and Pro open reading frames.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M14123; AAA88030.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M14123; AAA88031.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Y10390; CAA71416.1; -; Genomic_DNA.
DR EMBL; AF164613; AAD51796.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X72791; CAA51306.1; -; mRNA.
DR EMBL; AC016577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A24483; FOHUE1.
DR PIR; B24483; FOHUE2.
DR AlphaFoldDB; P87889; -.
DR SMR; P87889; -.
DR IntAct; P87889; 1.
DR BioMuta; HGNC:39004; -.
DR DMDM; 134035263; -.
DR MassIVE; P87889; -.
DR PeptideAtlas; P87889; -.
DR PRIDE; P87889; -.
DR GeneCards; ERVK-10; -.
DR HGNC; HGNC:39004; ERVK-10.
DR neXtProt; NX_P87889; -.
DR PhylomeDB; P87889; -.
DR Pharos; P87889; 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 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 10 Gag
FT polyprotein"
FT /id="PRO_0000186753"
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 164..183
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CONFLICT 55
FT /note="S -> L (in Ref. 5; AC016577)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="A -> V (in Ref. 2; CAA71416)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="L -> P (in Ref. 5; AC016577)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="Q -> P (in Ref. 5; AC016577)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="L -> P (in Ref. 5; AC016577)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="T -> A (in Ref. 4; CAA51306)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="G -> R (in Ref. 4; CAA51306)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="R -> C (in Ref. 2; CAA71416)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="P -> L (in Ref. 5; AC016577)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="S -> L (in Ref. 4; CAA51306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 74139 MW; 7DC295738E81FDCA CRC64;
MGQTKSKIKS KYASYLSFIK ILLKRGGVKV STKNLIKLFQ IIEQFCPWFP EQGTSDLKDW
KRIGKELKQA GRKGNIIPLT VWNDWAIIKA ALEPFQTEED SISVSDAPGS CLIDCNENTR
KKSQKETESL HCEYVAEPVM AQSTQNVDYN QLQEVIYPET LKLEGKGPEL MGPSESKPRG
TSPLPAGQVL VRLQPQKQVK ENKTQPQVAY QYWPLAELQY RPPPESQYGY PGMPPAPQGR
APYHQPPTRR LNPMAPPSRQ GSELHEIIDK SRKEGDTEAW QFPVTLEPMP PGEGAQEGEP
PTVEARYKSF SIKMLKDMKE GVKQYGPNSP YMRTLLDSIA YGHRLIPYDW EILAKSSLSP
SQFLQFKTWW IDGVQEQVRR NRAANPPVNI DADQLLGIGQ NWSTISQQAL MQNEAIEQVR
AICLRAWEKI QDPGSTCPSF NTVRQGSKEP YPDFVARLQD VAQKSIADEK AGKVIVELMA
YENANPECQS AIKPLKGKVP AGSDVISEYV KACDGIGGAM HKAMLMAQAI TGVVLGGQVR
TFGGKCYNCG QIGHLKKNCP VLNKQNITIQ ATTTGREPPD LCPRCKKGKH WASQCRSKFD
KNGQPLSGNE QRGQPQAPQQ TGAFPIQPFV PQGFQGQQPP LSQVFQGISQ LPQYNNCPSP
QAAVQQ
