ENK24_HUMAN
ID ENK24_HUMAN Reviewed; 588 AA.
AC P61566;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Endogenous retrovirus group K member 24 Env polyprotein;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=HERV-K101 envelope protein;
DE AltName: Full=HERV-K_22q11.21 provirus ancestral Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
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 TISSUE SPECIFICITY.
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 [3]
RP SUBGENOMIC RNA.
RX PubMed=12629516; DOI=10.1038/sj.onc.1206241;
RA Wang-Johanning F., Frost A.R., Jian B., Epp L., Lu D.W., Johanning G.L.;
RT "Quantitation of HERV-K env gene expression and splicing in human breast
RT cancer.";
RL Oncogene 22:1528-1535(2003).
CC -!- FUNCTION: Retroviral envelope proteins mediate receptor recognition and
CC membrane fusion during early infection. Endogenous envelope proteins
CC may have kept, lost or modified their original function during
CC evolution.
CC -!- FUNCTION: SU mediates receptor recognition. {ECO:0000250}.
CC -!- FUNCTION: TM anchors the envelope heterodimer to the viral membrane
CC through one transmembrane domain. The other hydrophobic domain, called
CC fusion peptide, mediates fusion of the viral membrane with the target
CC cell membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The surface (SU) and transmembrane (TM) proteins form a
CC heterodimer. SU and TM are attached by noncovalent interactions or by a
CC labile interchain disulfide bond (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=The surface protein is
CC not anchored to the membrane, but localizes to the extracellular
CC surface through its binding to TM. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Endogenous retrovirus group K member 24 Env
CC polyprotein]: Virion {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in teratocarcinoma cell line.
CC {ECO:0000269|PubMed:11401426}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM
CC proteins. {ECO:0000250}.
CC -!- MISCELLANEOUS: This envelope protein is encoded by a human specific
CC provirus.
CC -!- MISCELLANEOUS: Has a type 1 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 resulting in Env proteins of
CC distinct sizes. Despite their overall retroviral envelope structure
CC HERV-K(HML-2) type 1 envelope proteins lack a predictable signal
CC sequence. Subgenomic RNA transcripts coding for full-length envelope
CC proteins have been detected for both type of genomes.
CC -!- MISCELLANEOUS: Intergenic, closest flanking gene being PRODH.
CC -!- SIMILARITY: Belongs to the beta type-B retroviral envelope protein
CC family. HERV class-II K(HML-2) env subfamily. {ECO:0000305}.
CC -!- CAUTION: No predictable signal peptide. {ECO:0000305}.
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DR EMBL; AF164609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P61566; -.
DR iPTMnet; P61566; -.
DR PhosphoSitePlus; P61566; -.
DR BioMuta; HGNC:39038; -.
DR DMDM; 47605617; -.
DR jPOST; P61566; -.
DR MassIVE; P61566; -.
DR PeptideAtlas; P61566; -.
DR PRIDE; P61566; -.
DR GeneCards; ERVK-24; -.
DR HGNC; HGNC:39038; ERVK-24.
DR neXtProt; NX_P61566; -.
DR PhylomeDB; P61566; -.
DR Pharos; P61566; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR InterPro; IPR000328; GP41-like.
DR InterPro; IPR029104; HERV-K_env.
DR Pfam; PF00517; GP41; 1.
DR Pfam; PF13804; HERV-K_env_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond; ERV;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transposable element; Viral envelope protein; Virion.
FT CHAIN 1..588
FT /note="Endogenous retrovirus group K member 24 Env
FT polyprotein"
FT /id="PRO_0000008523"
FT CHAIN 1..354
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008524"
FT CHAIN 355..588
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008525"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 355..375
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT SITE 354..355
FT /note="Cleavage"
FT /evidence="ECO:0000250"
SQ SEQUENCE 588 AA; 66585 MW; 0C1ED9251CEB8656 CRC64;
MVTPVTWMDN PIEVYVNDSE WVPGPTDDRC PAKPEEEGMM INISIGYRYP PICLGTAPGC
LMPAVQNWLV EVPIVSPISR FTYHMVSGMS LRPRVNYLQD FPYQRSLKFR PKGKPCPKEI
PKESKNTEVL VWEECVANSA VILQNNEFGT IIDWAPRGQF YHNCSGQTQS CPSAQVSPAV
DSDLTESLDK HKHKKLQSFY PWEWGEKGIS TPRPKIISPV SGPEHPELWR LTVASHHIRI
WSGNQTLETR DRKPFYTVDL NSSLTLPLQS CVKPPYMLVV GNIVIKPDSQ TITCENCRLL
TCIDSTFNWQ HRILLVRARE GVWILVSMDR PWEASPSVHI LTEVLKGVLN RSKRFIFTLI
AVIMGLIAVT ATGAVAGVAL HSSVQSVNFV NDWQKNSTRL WNSQSSIDQK LANQINDLRQ
TVIWMGDRLM SLEHRFQLQC DWNTSDFCIT PQIYNESEHH WDMVRHHLQG REDNLTLDIS
KLKEQIFEAS KAHLNLVPGT EAIAGVADGL ANLNPVTWVK TIGSTTIINL ILILVCLFCL
LLVCRCTQQL RRDSDHRERA MMTMAVLSKR KGGNVGKSKR DQIVTVSV
