Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endogenous retrovirus group K member 19 Env polyprotein

Gene

ERVK-19

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties.1 Publication
SU mediates receptor recognition.By similarity
TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity).By similarity

Miscellaneous

ERVK-19 has a type 2 genome. The HERV-K(HML-2) family contains type 1 and type 2 genomes depending on the absence or presence of 292 nucleotides at the 5'-end of the env gene resulting in Env proteins of distinct sizes. Despite their overall retroviral envelope structure HERV-K(HML-2) type 1 envelope proteins lack a predictable signal sequence. Subgenomic RNA transcripts coding for full-length envelope proteins have been detected for both type of genomes.

GO - Molecular functioni

Names & Taxonomyi

Protein namesi
Recommended name:
Endogenous retrovirus group K member 19 Env polyprotein
Alternative name(s):
EnvK3 protein
Envelope polyprotein
HERV-K(C19) envelope protein
HERV-K_19q11 provirus ancestral Env polyprotein
Cleaved into the following 2 chains:
Surface protein
Short name:
SU
Transmembrane protein
Short name:
TM
Gene namesi
Name:ERVK-19
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:39026. ERVK-19.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini90 – 632ExtracellularSequence analysisAdd BLAST543
Transmembranei633 – 653HelicalSequence analysisAdd BLAST21
Topological domaini654 – 699CytoplasmicSequence analysisAdd BLAST46

Keywords - Cellular componenti

Cell membrane, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Organism-specific databases

DisGeNETi100862685.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 89Sequence analysisAdd BLAST89
ChainiPRO_000000850390 – 699Endogenous retrovirus group K member 19 Env polyproteinAdd BLAST610
ChainiPRO_000000850490 – 465Surface proteinBy similarityAdd BLAST376
ChainiPRO_0000008505466 – 699Transmembrane proteinBy similarityAdd BLAST234

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi100N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi128N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi153N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi274N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi355N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi372N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi461N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi507N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi554N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi566N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi585N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Specific enzymatic cleavages in vivo yield the mature SU and TM proteins.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei465 – 466CleavageBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

EPDiO71037.
PRIDEiO71037.

PTM databases

iPTMnetiO71037.
PhosphoSitePlusiO71037.

Interactioni

Subunit structurei

The surface (SU) and transmembrane (TM) proteins form a heterodimer. SU and TM are attached by noncovalent interactions or by a labile interchain disulfide bond (By similarity).By similarity

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni466 – 486Fusion peptideSequence analysisAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi13 – 20Poly-Arg8
Compositional biasi94 – 99Poly-Ala6

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG051479.
PhylomeDBiO71037.

Family and domain databases

CDDicd09909. HIV-1-like_HR1-HR2. 1 hit.
InterProiView protein in InterPro
IPR000328. GP41-like.
IPR029104. HERV-K_env.
PfamiView protein in Pfam
PF00517. GP41. 1 hit.
PF13804. HERV-K_env_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O71037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPSEMQRKA PPRRRRHRNR APLTHKMNKM VTSEEQMKLP STKKAEPPTW
60 70 80 90 100
AQLKKLTQLA TKYLENTKVT QTPESMLLAA LMIVSMVVSL PMPAGAAAAN
110 120 130 140 150
YTYWAYVPFP PLIRAVTWMD NPIEVYVNDS VWVPGPTDDH CPAKPEEEGM
160 170 180 190 200
MINISIGYRY PPICLGRAPG CLMPAVQNWL VEVPTVSPIS RFTYHMVSGM
210 220 230 240 250
SLRPRVNYLQ DFSYQRSFKF RPKGKPCPKE IPKESKNTEV LVWEECVANS
260 270 280 290 300
AVILQNNEFG TIIDWAPRGQ FYHNCSGQTQ SCPSAQVSPA VDSDLTESLD
310 320 330 340 350
KHKHKKLQSF YPWEWGEKGI STPRPKIISP VSGPEHPELW RLTVASHHIR
360 370 380 390 400
IWSGNQTLET RDRKPFYTVD LNSSVTVPLQ SCIKPPYMLV VGNIVIKPDS
410 420 430 440 450
QTITCENCRL LTCIDSTFNW QHRILLVRAR EGVWIPVSMD RPWETSPSIH
460 470 480 490 500
TLTEVLKGVL NRSKRFIFTL IAVIMGLIAV TATAAVAGVA LHSSVQSVNF
510 520 530 540 550
VNDWQKNSTR LWNSQSSIDQ KLANQINDLR QTVIWMGDRL MSLEHRFQLQ
560 570 580 590 600
CDWNTSDFSI TPQIYNESEH HWDMVRRHLQ GREDNLTLDI SKLKEQIFEA
610 620 630 640 650
SKAHLNLVPG TEAIAGVADG LANLNPVTWV KTIGSTTIIN LILILVCLFC
660 670 680 690
LLLVCRCTQQ LRRDSDHRER AMMTMAVLSK RKGGNVGKSK RDQIVTVSV
Length:699
Mass (Da):79,252
Last modified:May 24, 2004 - v2
Checksum:i79672A0E9BE58E02
GO

Sequence cautioni

The sequence CAA76883 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17833 Genomic DNA. Translation: CAA76883.1. Different initiation.
X92887 Genomic DNA. Translation: CAA63481.1.
AF023261 Genomic DNA. Translation: AAC16971.1.

Similar proteinsi

Entry informationi

Entry nameiENK19_HUMAN
AccessioniPrimary (citable) accession number: O71037
Secondary accession number(s): Q69386, Q9YNA7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: October 25, 2017
This is version 78 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, ERV, Reference proteome, Transposable element

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families