SYCY2_HUMAN
ID SYCY2_HUMAN Reviewed; 538 AA.
AC P60508;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Syncytin-2;
DE AltName: Full=Endogenous retrovirus group FRD member 1;
DE AltName: Full=Envelope polyprotein;
DE AltName: Full=HERV-FRD;
DE AltName: Full=HERV-FRD_6p24.1 provirus ancestral Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE Flags: Precursor;
GN Name=ERVFRD-1; Synonyms=ERVFRDE1; ORFNames=UNQ6191/PRO20218;
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 MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=14694139; DOI=10.1128/jvi.78.2.1050-1054.2004;
RA Blaise S., Ruggieri A., Dewannieux M., Cosset F.-L., Heidmann T.;
RT "Identification of an envelope protein from the FRD family of human
RT endogenous retroviruses (HERV-FRD) conferring infectivity and functional
RT conservation among simians.";
RL J. Virol. 78:1050-1054(2004).
RN [7]
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).
RN [8]
RP FUNCTION, AND INTERACTION WITH MFSD2A.
RX PubMed=18988732; DOI=10.1073/pnas.0807413105;
RA Esnault C., Priet S., Ribet D., Vernochet C., Bruls T., Lavialle C.,
RA Weissenbach J., Heidmann T.;
RT "A placenta-specific receptor for the fusogenic, endogenous retrovirus-
RT derived, human syncytin-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17532-17537(2008).
RN [9]
RP FUNCTION.
RX PubMed=23492904; DOI=10.1038/srep01462;
RA Sugimoto J., Sugimoto M., Bernstein H., Jinno Y., Schust D.;
RT "A novel human endogenous retroviral protein inhibits cell-cell fusion.";
RL Sci. Rep. 3:1462-1462(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 391-443, AND DISULFIDE BOND.
RX PubMed=16140326; DOI=10.1016/j.jmb.2005.07.058;
RA Renard M., Varela P.F., Letzelter C., Duquerroy S., Rey F.A., Heidmann T.;
RT "Crystal structure of a pivotal domain of human syncytin-2, a 40 million
RT years old endogenous retrovirus fusogenic envelope gene captured by
RT primates.";
RL J. Mol. Biol. 352:1029-1034(2005).
CC -!- FUNCTION: This endogenous retroviral envelope protein has retained its
CC original fusogenic properties and participates in trophoblast fusion
CC and the formation of a syncytium during placenta morphogenesis. The
CC interaction with MFSD2A is apparently important for this process
CC (PubMed:18988732). {ECO:0000269|PubMed:18988732}.
CC -!- FUNCTION: Endogenous envelope proteins may have kept, lost or modified
CC their original function during evolution but this one can still make
CC pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity.
CC Retroviral envelope proteins mediate receptor recognition and membrane
CC fusion during early infection. The surface protein mediates receptor
CC recognition, while the transmembrane protein anchors the envelope
CC heterodimer to the viral membrane through one transmembrane domain. The
CC other hydrophobic domain, called fusion peptide, mediates fusion of the
CC viral membrane with the target cell membrane (PubMed:14694139).
CC {ECO:0000269|PubMed:14694139}.
CC -!- SUBUNIT: The surface and transmembrane proteins form a heterodimer.
CC They are attached by non-covalent interactions or by a labile
CC interchain disulfide bond (By similarity). Interacts with MFSD2A.
CC {ECO:0000250, ECO:0000269|PubMed:18988732}.
CC -!- INTERACTION:
CC P60508; Q92843: BCL2L2; NbExp=3; IntAct=EBI-17973325, EBI-707714;
CC P60508; Q06432: CACNG1; NbExp=3; IntAct=EBI-17973325, EBI-9686780;
CC P60508; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-17973325, EBI-10271156;
CC P60508; Q08426: EHHADH; NbExp=3; IntAct=EBI-17973325, EBI-2339219;
CC P60508; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-17973325, EBI-10976398;
CC P60508; Q92520: FAM3C; NbExp=3; IntAct=EBI-17973325, EBI-2876774;
CC P60508; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-17973325, EBI-11991950;
CC P60508; Q86YW7: GPHB5; NbExp=3; IntAct=EBI-17973325, EBI-11659720;
CC P60508; P30301: MIP; NbExp=3; IntAct=EBI-17973325, EBI-8449636;
CC P60508; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-17973325, EBI-10317425;
CC P60508; Q969Y0: NXPE3; NbExp=3; IntAct=EBI-17973325, EBI-17973370;
CC P60508; P09466: PAEP; NbExp=3; IntAct=EBI-17973325, EBI-465167;
CC P60508; Q01453: PMP22; NbExp=3; IntAct=EBI-17973325, EBI-2845982;
CC P60508; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-17973325, EBI-8652744;
CC P60508; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-17973325, EBI-10262251;
CC P60508; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-17973325, EBI-10290130;
CC P60508; Q03518: TAP1; NbExp=3; IntAct=EBI-17973325, EBI-747259;
CC P60508; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-17973325, EBI-2852148;
CC P60508; Q9NRS4: TMPRSS4; NbExp=3; IntAct=EBI-17973325, EBI-10313040;
CC P60508; O95183: VAMP5; NbExp=3; IntAct=EBI-17973325, EBI-10191195;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. 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|UniProtKB:Q9UQF0}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at higher level in placenta. Expressed at
CC lower level in adrenal, bone marrow, brain, breast, colon, kidney,
CC lung, ovary, peripheral blood lymphocytes, prostate, skin, spleen,
CC testis, thymus, thyroid, trachea. {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: Specific enzymatic cleavages in vivo yield the mature SU and TM
CC proteins. {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 protein. Isomerization of the intersubunit
CC disulfide bond to an SU intrachain disulfide bond is thought to occur
CC upon receptor recognition in order to allow membrane fusion (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: HERV-FRD subgenomic RNA has been observed.
CC -!- MISCELLANEOUS: Ortholog in old-world and new-world monkeys, but not in
CC prosimians.
CC -!- MISCELLANEOUS: The human genome contains a high percentage of proviral-
CC like elements, also called endogenous retroviruses (ERVs) that are the
CC genomic traces of ancient infections of the germline by exogenous
CC retroviruses. Although most of these elements are defective, some have
CC conserved a functional envelope (env) gene, most probably diverted by
CC the host for its benefit.
CC -!- SIMILARITY: Belongs to the gamma type-C retroviral envelope protein
CC family. HERV class-I FRD env subfamily. {ECO:0000305}.
CC -!- CAUTION: CKS-17 sequence does not match the minimal active consensus.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY358244; AAQ88611.1; -; mRNA.
DR EMBL; AK123938; BAC85731.1; -; mRNA.
DR EMBL; AL136139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068585; AAH68585.1; -; mRNA.
DR CCDS; CCDS4519.1; -.
DR RefSeq; NP_997465.1; NM_207582.2.
DR PDB; 1Y4M; X-ray; 1.60 A; A/B/C=391-443.
DR PDB; 6RX3; X-ray; 2.20 A; A/B/C=375-468.
DR PDBsum; 1Y4M; -.
DR PDBsum; 6RX3; -.
DR AlphaFoldDB; P60508; -.
DR SMR; P60508; -.
DR BioGRID; 135715; 15.
DR IntAct; P60508; 22.
DR MINT; P60508; -.
DR STRING; 9606.ENSP00000420174; -.
DR TCDB; 1.G.9.1.2; the syncytin (syncytin) family.
DR GlyGen; P60508; 9 sites.
DR iPTMnet; P60508; -.
DR PhosphoSitePlus; P60508; -.
DR BioMuta; ERVFRD-1; -.
DR DMDM; 44887864; -.
DR MassIVE; P60508; -.
DR PaxDb; P60508; -.
DR PeptideAtlas; P60508; -.
DR PRIDE; P60508; -.
DR ProteomicsDB; 57211; -.
DR TopDownProteomics; P60508; -.
DR Antibodypedia; 24880; 166 antibodies from 22 providers.
DR DNASU; 405754; -.
DR Ensembl; ENST00000472091.2; ENSP00000420174.1; ENSG00000244476.3.
DR Ensembl; ENST00000542862.1; ENSP00000444461.1; ENSG00000244476.3.
DR GeneID; 405754; -.
DR KEGG; hsa:405754; -.
DR MANE-Select; ENST00000472091.2; ENSP00000420174.1; NM_207582.3; NP_997465.1.
DR UCSC; uc003mzt.4; human.
DR CTD; 405754; -.
DR DisGeNET; 405754; -.
DR GeneCards; ERVFRD-1; -.
DR HGNC; HGNC:33823; ERVFRD-1.
DR HPA; ENSG00000244476; Tissue enriched (placenta).
DR MIM; 610524; gene.
DR neXtProt; NX_P60508; -.
DR OpenTargets; ENSG00000244476; -.
DR VEuPathDB; HostDB:ENSG00000244476; -.
DR eggNOG; ENOG502SD08; Eukaryota.
DR GeneTree; ENSGT00940000163436; -.
DR HOGENOM; CLU_506176_0_0_1; -.
DR InParanoid; P60508; -.
DR OMA; SQTPCIQ; -.
DR OrthoDB; 451884at2759; -.
DR PhylomeDB; P60508; -.
DR TreeFam; TF332233; -.
DR PathwayCommons; P60508; -.
DR SignaLink; P60508; -.
DR BioGRID-ORCS; 405754; 9 hits in 1019 CRISPR screens.
DR ChiTaRS; ERVFRD-1; human.
DR EvolutionaryTrace; P60508; -.
DR GeneWiki; HERV-FRD; -.
DR GenomeRNAi; 405754; -.
DR Pharos; P60508; Tbio.
DR PRO; PR:P60508; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P60508; protein.
DR Bgee; ENSG00000244476; Expressed in placenta and 56 other tissues.
DR Genevisible; P60508; HS.
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:0007520; P:myoblast fusion; IMP:MGI.
DR GO; GO:0006949; P:syncytium formation; IDA:UniProtKB.
DR GO; GO:0000768; P:syncytium formation by plasma membrane fusion; IDA:UniProtKB.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cleavage on pair of basic residues;
KW Disulfide bond; ERV; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transposable element;
KW Viral envelope protein; Virion.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..538
FT /note="Syncytin-2"
FT /id="PRO_0000008439"
FT CHAIN 16..350
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008440"
FT CHAIN 351..538
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008441"
FT TOPO_DOM 16..478
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 354..374
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT MOTIF 43..46
FT /note="CXXC"
FT /evidence="ECO:0000305"
FT MOTIF 414..430
FT /note="CKS-17"
FT /evidence="ECO:0000250"
FT MOTIF 431..439
FT /note="CX6CC"
FT /evidence="ECO:0000305"
FT SITE 350..351
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF0"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..439
FT /note="Interchain (between SU and TM chains, or C-46 with
FT C-439); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q9UQF0"
FT DISULFID 43..46
FT /evidence="ECO:0000250|UniProtKB:P23064"
FT DISULFID 431..438
FT /evidence="ECO:0000269|PubMed:16140326"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:6RX3"
FT HELIX 395..423
FT /evidence="ECO:0007829|PDB:1Y4M"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:1Y4M"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:1Y4M"
FT HELIX 445..467
FT /evidence="ECO:0007829|PDB:6RX3"
SQ SEQUENCE 538 AA; 59523 MW; AC4229CB43129F06 CRC64;
MGLLLLVLIL TPSLAAYRHP DFPLLEKAQQ LLQSTGSPYS TNCWLCTSSS TETPGTAYPA
SPREWTSIEA ELHISYRWDP NLKGLMRPAN SLLSTVKQDF PDIRQKPPIF GPIFTNINLM
GIAPICVMAK RKNGTNVGTL PSTVCNVTFT VDSNQQTYQT YTHNQFRHQP RFPKPPNITF
PQGTLLDKSS RFCQGRPSSC STRNFWFRPA DYNQCLQISN LSSTAEWVLL DQTRNSLFWE
NKTKGANQSQ TPCVQVLAGM TIATSYLGIS AVSEFFGTSL TPLFHFHIST CLKTQGAFYI
CGQSIHQCLP SNWTGTCTIG YVTPDIFIAP GNLSLPIPIY GNSPLPRVRR AIHFIPLLAG
LGILAGTGTG IAGITKASLT YSQLSKEIAN NIDTMAKALT TMQEQIDSLA AVVLQNRRGL
DMLTAAQGGI CLALDEKCCF WVNQSGKVQD NIRQLLNQAS SLRERATQGW LNWEGTWKWF
SWVLPLTGPL VSLLLLLLFG PCLLNLITQF VSSRLQAIKL QTNLSAGRHP RNIQESPF
