ERB1_HUMAN
ID ERB1_HUMAN Reviewed; 514 AA.
AC P60509;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Endogenous retrovirus group PABLB member 1 Env polyprotein;
DE AltName: Full=Endogenous retrovirus group PABLB member 1;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=HERV-R(b) Env protein;
DE AltName: Full=HERV-R(b)_3p24.3 provirus ancestral Env polyprotein;
DE Includes:
DE RecName: Full=Surface protein domain;
DE Short=SU;
DE Includes:
DE RecName: Full=Transmembrane protein domain;
DE Short=TM;
GN Name=ERVPABLB-1;
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP FUNCTION.
RX PubMed=14557543; DOI=10.1073/pnas.2132646100;
RA Blaise S., de Parseval N., Benit L., Heidmann T.;
RT "Genomewide screening for fusogenic human endogenous retrovirus envelopes
RT identifies syncytin 2, a gene conserved on primate evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13013-13018(2003).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12970426; DOI=10.1128/jvi.77.19.10414-10422.2003;
RA de Parseval N., Lazar V., Casella J.-F., Benit L., Heidmann T.;
RT "Survey of human genes of retroviral origin: identification and
RT transcriptome of the genes with coding capacity for complete envelope
RT proteins.";
RL J. Virol. 77:10414-10422(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. This endogenous envelope protein has lost its original
CC fusogenic properties. {ECO:0000269|PubMed:14557543}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Note=At the origin, this retroviral envelope
CC protein was localized in the virion. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Low expression in placenta and testis.
CC {ECO:0000269|PubMed:12970426}.
CC -!- DOMAIN: Contains the CKS-17 immunosuppressive domain present in many
CC retroviral envelope proteins. As a synthetic peptide, it inhibits
CC immune function in vitro and in vivo (By similarity). {ECO:0000250}.
CC -!- PTM: The CXXC motif is highly conserved across a broad range of
CC retroviral envelope proteins. It is thought to participate in the
CC formation of a labile disulfide bond possibly with the CX6CC motif
CC present in the transmembrane domain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the gamma type-C retroviral envelope protein
CC family. HERV class-I R(b) env subfamily. {ECO:0000305}.
CC -!- CAUTION: The cleavage site does not match the consensus. {ECO:0000305}.
CC -!- CAUTION: CKS-17 sequence does not match the minimal active consensus.
CC {ECO:0000305}.
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DR EMBL; AC093488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016863101.1; XM_017007612.1.
DR RefSeq; XP_016863102.1; XM_017007613.1.
DR RefSeq; XP_016863103.1; XM_017007614.1.
DR AlphaFoldDB; P60509; -.
DR SMR; P60509; -.
DR GlyGen; P60509; 11 sites.
DR BioMuta; HGNC:39042; -.
DR DMDM; 44887882; -.
DR PRIDE; P60509; -.
DR DisGeNET; 105377641; -.
DR GeneCards; ERVPABLB-1; -.
DR HGNC; HGNC:39042; ERVPABLB-1.
DR neXtProt; NX_P60509; -.
DR OrthoDB; 389221at2759; -.
DR Pharos; P60509; Tdark.
DR PRO; PR:P60509; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P60509; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; ERV; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Transposable element.
FT CHAIN 1..514
FT /note="Endogenous retrovirus group PABLB member 1 Env
FT polyprotein"
FT /id="PRO_0000008480"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 60..316
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT REGION 317..514
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT REGION 328..348
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT MOTIF 82..85
FT /note="CXXC"
FT /evidence="ECO:0000250"
FT MOTIF 378..394
FT /note="CKS-17"
FT /evidence="ECO:0000250"
FT MOTIF 395..403
FT /note="CX6CC"
FT /evidence="ECO:0000250"
FT SITE 316..317
FT /note="Ancestral cleavage site"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 395..402
FT /evidence="ECO:0000250"
SQ SEQUENCE 514 AA; 58521 MW; 783EF4AADFD75E84 CRC64;
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
