GAK24_HUMAN
ID GAK24_HUMAN Reviewed; 666 AA.
AC P63145; Q9UKI1;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Endogenous retrovirus group K member 24 Gag polyprotein;
DE AltName: Full=HERV-K101 Gag protein;
DE AltName: Full=HERV-K_22q11.21 provirus ancestral Gag polyprotein;
DE Short=Gag polyprotein;
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).
RN [3]
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=P63145-1; 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: Intergenic, closest flanking gene being PRODH.
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=AAD51791.1; Type=Frameshift; Note=The frameshift occurs probably within the codons for the last amino acids in the Gag and Pro open reading frames.; Evidence={ECO:0000305};
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DR EMBL; AF164609; AAD51791.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AC007326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6SSJ; EM; 2.75 A; A=283-528.
DR PDB; 6SSK; EM; 3.18 A; A/B/C/D/E/F/G/H/I=283-528.
DR PDB; 6SSL; EM; 3.77 A; A/B/C/D/E/F/G/H/I=283-528.
DR PDB; 6SSM; EM; 4.34 A; A/B/C=283-528.
DR PDBsum; 6SSJ; -.
DR PDBsum; 6SSK; -.
DR PDBsum; 6SSL; -.
DR PDBsum; 6SSM; -.
DR AlphaFoldDB; P63145; -.
DR SMR; P63145; -.
DR IntAct; P63145; 1.
DR BioMuta; HGNC:39038; -.
DR EPD; P63145; -.
DR MassIVE; P63145; -.
DR PeptideAtlas; P63145; -.
DR PRIDE; P63145; -.
DR GeneCards; ERVK-24; -.
DR HGNC; HGNC:39038; ERVK-24.
DR neXtProt; NX_P63145; -.
DR PhylomeDB; P63145; -.
DR Pharos; P63145; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P63145; 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 3D-structure; Cell membrane; ERV; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Reference proteome; Repeat; Ribosomal frameshifting;
KW 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 24 Gag
FT polyprotein"
FT /id="PRO_0000186754"
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..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 112
FT /note="L -> I (in Ref. 1; AAD51791)"
FT /evidence="ECO:0000305"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6SSJ"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 330..341
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 347..357
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 360..382
FT /evidence="ECO:0007829|PDB:6SSJ"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:6SSJ"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:6SSJ"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 413..426
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:6SSJ"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 451..465
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 469..482
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 486..492
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:6SSJ"
FT HELIX 505..513
FT /evidence="ECO:0007829|PDB:6SSJ"
SQ SEQUENCE 666 AA; 74040 MW; 8BE2901ED6C916ED CRC64;
MGQTKSKIKS KYASYLSFIK ILLKRGGVKV STKNLIKLFQ IIEQFCPWFP EQGTLDLKDW
KRIGKELKQA GRKGNIIPLT VWNDWAIIKA ALEPFQTEED SVSVSDAPGS CLIDCNEKTR
KKSQKETESL HCEYVAEPVM AQSTQNVDYN QLQEVIYPET LKLEGKGPEL VGPSESKPRG
TSPLPAGQVP VTLQPQKQVK ENKTQPPVAY QYWPPAELQY RPPPESQYGY PGMPPAPQGR
APYPQPPTRR LNPTAPPSRQ GSELHEIIDK SRKEGDTEAW QFPVTLEPMP PGEGAQEGEP
PTVEARYKSF SIKMLKDMKE GVKQYGPNSP YMRTLLDSIA YGHRLIPYDW EILAKSSLSP
SQFLQFKTWW IDGVQEQVRR NRAANPPVNI DADQLLGIGQ NWSTISQQAL MQNEAIEQVR
AICLRAWEKI QDPGSACPSF NTVRQGSKEP YPDFVARLQD VAQKSIADEK ARKVIVELMA
YENANPECQS AIKPLKGKVP AGSDVISEYV KACDGIGGAM HKAMLMAQAI TGVVLGGQVR
TFGGKCYNCG QIGHLKKNCP VLNKQNITIQ ATTTGREPPD LCPRCKKGKH WASQCRSKFD
KNGQPLSGNE QRGQPQAPQQ TGAFPIQPFV PQGFQGQQPP LSQVFQGISQ LPQYNNCPLP
QAAVQQ
