REC16_HUMAN
ID REC16_HUMAN Reviewed; 105 AA.
AC P61578;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Endogenous retrovirus group K member 16 Rec protein;
DE AltName: Full=HERV-K_10p14 provirus Rec protein;
GN Name=ERVK-16;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [2]
RP CHARACTERIZATION.
RX PubMed=15063128; DOI=10.1016/j.virol.2004.01.023;
RA Mayer J., Ehlhardt S., Seifert M., Sauter M., Mueller-Lantzsch N.,
RA Mehraein Y., Zang K.-D., Meese E.U.;
RT "Human endogenous retrovirus HERV-K(HML-2) proviruses with Rec protein
RT coding capacity and transcriptional activity.";
RL Virology 322:190-198(2004).
CC -!- FUNCTION: Retroviral replication requires the nuclear export and
CC translation of unspliced, singly-spliced and multiply-spliced
CC derivatives of the initial genomic transcript. Rec interacts with a
CC highly structured RNA element (RcRE) present in the viral 3'LTR and
CC recruits the cellular nuclear export machinery. This permits export to
CC the cytoplasm of unspliced genomic or incompletely spliced subgenomic
CC viral transcripts (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms homodimers, homotrimers, and homotetramers via a C-
CC terminal domain. Associates with XPO1 and with ZNF145 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm.
CC When in the nucleus, resides in the nucleolus (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Despite functional similarity, Rec shares almost no
CC sequence homology with HIV-1 Rev and HTLV-1 Rex.
CC -!- MISCELLANEOUS: Has a type 2 genome. The HERV-K(HML-2) family contains
CC type 1 and type 2 genomes depending on the absence or presence of 292
CC nucleotides at the 5'-end of the env gene. Rec proteins are translated
CC from a doubly spliced transcript expressed exclusively by HERV-K(HML-2)
CC type 2 proviral genomes. The first exon comprises the 87 N-terminal
CC amino acids of the HERV-K(HMLM-2) type 2 envelope protein. The second
CC exon (18 amino acids) is positioned in the 3' part of the proviral
CC genome.
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DR EMBL; AL392086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P61578; -.
DR SMR; P61578; -.
DR BioMuta; HGNC:39023; -.
DR MassIVE; P61578; -.
DR PRIDE; P61578; -.
DR GeneCards; ERVK-16; -.
DR HGNC; HGNC:39023; ERVK-16.
DR neXtProt; NX_P61578; -.
DR PhylomeDB; P61578; -.
DR Pharos; P61578; Tdark.
DR PRO; PR:P61578; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P61578; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasm; ERV; mRNA transport; Nucleus; Reference proteome; RNA-binding;
KW Transport; Transposable element.
FT CHAIN 1..105
FT /note="Endogenous retrovirus group K member 16 Rec protein"
FT /id="PRO_0000186782"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 13..20
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 50..59
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 10..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 105 AA; 11808 MW; 3634F5D296303B81 CRC64;
MNPSEMQRKA PPRRRRHRNR APSSHKMNKM MMSEEQMKLP STNKAEPLTW AQLNKLTQLA
TKCLENTKMT QTPESMLLAA LMIVSTVSAG VPNSSEETVT IENGP
