ERB1_HUMAN » HERV-R(b)_3p24.3 provirus ancestral Env polyprotein

ERB1_HUMAN » HERV-R(b)_3p24.3 provirus ancestral Env polyprotein
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
ERB1_HUMAN » HERV-R(b)_3p24.3 provirus ancestral Env polyprotein » Envelope polyprotein;HERV-R(b) Env protein;
Hydrophobic Thickness 32.4 ± 1.2 Å
Tilt Angle 3 ± 1°
ΔGtransfer -41.4 kcal/mol
ΔGfold -13.8 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 448-473 (446-475)
Pathways none
PDB none
OPM none
Complexes none
Interactions none
Domains

AA: 199-441, PDBID: 1XNL, Subunit A, Seq Identity:83%, ENV polyprotein (coat polyprotein)

UniProt annotation for ERB1_HUMAN » HERV-R(b)_3p24.3 provirus ancestral Env polyprotein
FUNCTION: 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.

TISSUE SPECIFICITY: Low expression in placenta and testis.

DOMAIN: Contains the CKS-17 immunosuppressive domain present in many retroviral envelope proteins. As a synthetic peptide, it inhibits immune function in vitro and in vivo (By similarity).

UniProt features for ERB1_HUMAN » HERV-R(b)_3p24.3 provirus ancestral Env polyprotein
SIGNAL 1 59 Potential.
CHAIN 60 514 HERV-R(b)_3p24.3 provirus ancestral Env polyprotein.
REGION 60 316 Surface protein (By similarity).
REGION 317 514 Transmembrane protein (By similarity).
REGION 328 348 Fusion peptide (By similarity).
MOTIF 82 85 CXXC (By similarity).
MOTIF 378 394 CKS-17 (By similarity).
MOTIF 395 403 CX6CC (By similarity).
SITE 316 317 Ancestral cleavage site (Potential).
DISULFID 395 402 By similarity.
Amino Acid Sequence for ERB1_HUMAN » HERV-R(b)_3p24.3 provirus ancestral Env polyprotein
MDPLHTIEKV PARRNIHDRG HQGHRMGDGT PGRPKISVQQ MTRFSLIIFF LSAPFVVNAS TSNVFLQWAH SYADGLQQGD PCWVCGSLPV TNTMELPWWV SPLQGKDWVF FQSFIGDLKQ WTGAQMTGVT RKNISEWPIN KTLNEPGHDK PFSVNETRDK VIAFAIPLLD TKVFVQTSRP QNTQYRNGFL QIWDGFIWLT ATKGHLSQIA PLCWEQRNHS LDNWPNTTRV MGWIPPGQCR HTILLQQRDL FATDWSQQPG LNWYAPNGTQ WLCSPNLWPW LPSGWLGCCT LGIPWAQGRW VKTMEVYPYL PHVVNQGTRA IVHRNDHLPT IFMPSVGLGT VIQHIEALAN FTQRALNDSL QSISLMNAEV YYMHEDILQN RMALDILTAA EGGTCALIKT ECCVYIPNNS RNISLALEDT CRQIQVISSS ALSLHDWIAS QFSGRPSWWQ KILIVLATLW SVGIALCCGL YFCRMFSQHI PQTHSIIFQQ ELPLSPPSQE HYQSQRDIFH SNAP