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Pre-glycoprotein polyprotein GP complex (Pre-GP-C) [Cleaved into: Stable signal peptide (SSP); Glycoprotein G1 (GP1); Glycoprotein G2 (GP2)]

 GLYC_LYCVA              Reviewed;         498 AA.
P09991; Q27V72; Q49K87;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
23-MAY-2018, entry version 95.
RecName: Full=Pre-glycoprotein polyprotein GP complex {ECO:0000255|HAMAP-Rule:MF_04084};
Short=Pre-GP-C {ECO:0000255|HAMAP-Rule:MF_04084};
Contains:
RecName: Full=Stable signal peptide {ECO:0000255|HAMAP-Rule:MF_04084};
Short=SSP {ECO:0000255|HAMAP-Rule:MF_04084};
Contains:
RecName: Full=Glycoprotein G1 {ECO:0000255|HAMAP-Rule:MF_04084};
Short=GP1 {ECO:0000255|HAMAP-Rule:MF_04084};
Contains:
RecName: Full=Glycoprotein G2 {ECO:0000255|HAMAP-Rule:MF_04084};
Short=GP2 {ECO:0000255|HAMAP-Rule:MF_04084};
Name=GPC {ECO:0000255|HAMAP-Rule:MF_04084}; Synonyms=GP-C;
OrderedLocusNames=Segment S;
Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses; Arenaviridae;
Mammarenavirus.
NCBI_TaxID=11624;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=10036; Mesocricetus auratus (Golden hamster).
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3824905; DOI=10.1016/0042-6822(87)90323-0;
Southern P.J., Singh M.K., Riviere Y., Jacoby D.R., Buchmeier M.J.,
Oldstone M.B.A.;
"Molecular characterization of the genomic S RNA segment from
lymphocytic choriomeningitis virus.";
Virology 157:145-155(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate CTL+, and Isolate CTL-;
PubMed=3259346; DOI=10.1016/0042-6822(88)90566-1;
Salvato M., Shimomaye E., Southern P.J., Oldstone M.B.A.;
"Virus-lymphocyte interactions. IV. Molecular characterization of LCMV
Armstrong (CTL+) small genomic segment and that of its variant, Clone
13 (CTL-).";
Virology 164:517-522(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Armstrong 53b;
PubMed=16051837; DOI=10.1128/JVI.79.16.10451-10459.2005;
Grande-Perez A., Gomez-Mariano G., Lowenstein P.R., Domingo E.;
"Mutagenesis-induced, large fitness variations with an invariant
arenavirus consensus genomic nucleotide sequence.";
J. Virol. 79:10451-10459(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Armstrong-derived variant Cl13;
PubMed=16537369; DOI=10.1073/pnas.0600652103;
Flatz L., Bergthaler A., de la Torre J.C., Pinschewer D.D.;
"Recovery of an arenavirus entirely from RNA polymerase I/II-driven
cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 103:4663-4668(2006).
[5]
FUNCTION IN FUSION.
PubMed=8291229; DOI=10.1006/viro.1994.1057;
Di Simone C., Zandonatti M.A., Buchmeier M.J.;
"Acidic pH triggers LCMV membrane fusion activity and conformational
change in the glycoprotein spike.";
Virology 198:455-465(1994).
[6]
FUNCTION, AND INTERACTION WITH HOST DAG1.
PubMed=9851928; DOI=10.1126/science.282.5396.2079;
Cao W., Henry M.D., Borrow P., Yamada H., Elder J.H., Ravkov E.V.,
Nichol S.T., Compans R.W., Campbell K.P., Oldstone M.B.A.;
"Identification of alpha-dystroglycan as a receptor for lymphocytic
choriomeningitis virus and Lassa fever virus.";
Science 282:2079-2081(1998).
[7]
SUBUNIT.
PubMed=16731928; DOI=10.1128/JVI.00008-06;
Eschli B., Quirin K., Wepf A., Weber J., Zinkernagel R.,
Hengartner H.;
"Identification of an N-terminal trimeric coiled-coil core within
arenavirus glycoprotein 2 permits assignment to class I viral fusion
proteins.";
J. Virol. 80:5897-5907(2006).
[8]
FUNCTION OF STABLE SIGNAL PEPTIDE, AND MUTAGENESIS OF PRO-12; ASP-16;
GLU-17; ASN-20; LYS-33; ASN-37; PHE-49 AND GLY-54.
PubMed=17376927; DOI=10.1128/JVI.02759-06;
Saunders A.A., Ting J.P.C., Meisner J., Neuman B.W., Perez M.,
de la Torre J.C., Buchmeier M.J.;
"Mapping the landscape of the lymphocytic choriomeningitis virus
stable signal peptide reveals novel functional domains.";
J. Virol. 81:5649-5657(2007).
[9]
INTERACTION WITH Z PROTEIN.
PubMed=17581989; DOI=10.1128/JVI.00499-07;
Capul A.A., Perez M., Burke E., Kunz S., Buchmeier M.J.,
de la Torre J.C.;
"Arenavirus Z-glycoprotein association requires Z myristoylation but
not functional RING or late domains.";
J. Virol. 81:9451-9460(2007).
[10]
FUNCTION.
PubMed=17761532; DOI=10.1091/mbc.E07-04-0374;
Rojek J.M., Campbell K.P., Oldstone M.B., Kunz S.;
"Old World arenavirus infection interferes with the expression of
functional alpha-dystroglycan in the host cell.";
Mol. Biol. Cell 18:4493-4507(2007).
[11]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 92-101.
PubMed=29253009; DOI=10.1371/journal.pone.0189584;
Hafstrand I., Badia-Martinez D., Josey B.J., Norstroem M., Buratto J.,
Pellegrino S., Duru A.D., Sandalova T., Achour A.;
"Crystal structures of H-2Db in complex with the LCMV-derived peptides
GP92 and GP392 explain pleiotropic effects of glycosylation on antigen
presentation and immunogenicity.";
PLoS ONE 12:E0189584-E0189584(2017).
-!- FUNCTION: Glycoprotein G2: class I viral fusion protein that
directs fusion of viral and host endosomal membranes, leading to
delivery of the nucleocapsid into the cytoplasm. Membrane fusion
is mediated by irreversible conformational changes induced upon
acidification in the endosome. {ECO:0000255|HAMAP-Rule:MF_04084,
ECO:0000269|PubMed:8291229}.
-!- FUNCTION: Stable signal peptide (SSP): cleaved and functions as a
signal peptide. In addition, it is also retained as the third
component of the GP complex. The SSP is required for efficient
glycoprotein expression, post-translational maturation cleavage of
GP1 and GP2, glycoprotein transport to the cell surface plasma
membrane, formation of infectious virus particles, and acid pH-
dependent glycoprotein-mediated cell fusion. {ECO:0000255|HAMAP-
Rule:MF_04084, ECO:0000269|PubMed:17376927}.
-!- FUNCTION: Glycoprotein G1: interacts with the host receptor (By
similarity). Mediates virus attachment to host receptor alpha-
dystroglycan DAG1. This attachment induces virion internalization
predominantly through clathrin- and caveolin-independent
endocytosis (PubMed:9851928). {ECO:0000255|HAMAP-Rule:MF_04084,
ECO:0000269|PubMed:9851928}.
-!- SUBUNIT: Glycoprotein G1: homotetramer; disulfide-linked (By
similarity). Interacts with host DAG1 (PubMed:9851928).
Glycoprotein G2: homotetramer. GP2 homotetramers bind through
ionic interactions with GP1 homotetramers to form the GP complex
together with the stable signal peptide. The GP-C polyprotein
interacts with the host protease MBTPS1/SKI-1 resulting in the
polyprotein processing (By similarity). GP-complex interacts with
protein Z, which interacts with ribonucleocapsid; these
interactions may induce virion budding (PubMed:17581989).
{ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:16731928,
ECO:0000269|PubMed:17581989, ECO:0000269|PubMed:9851928}.
-!- SUBCELLULAR LOCATION: Glycoprotein G1: Virion membrane
{ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum
membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane
protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus
membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane
protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_04084}.
-!- SUBCELLULAR LOCATION: Glycoprotein G2: Virion membrane
{ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum
membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane
protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus
membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane
protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_04084}. Note=Binding to the stable
signal peptide masks endogenous ER localization signals in the
cytoplasmic domain of G2 to ensure that only the fully assembled,
tripartite GP complex is transported for virion assembly.
{ECO:0000255|HAMAP-Rule:MF_04084}.
-!- SUBCELLULAR LOCATION: Stable signal peptide: Virion membrane
{ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum
membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane
protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus
membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane
protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_04084}.
-!- DOMAIN: The cytoplasmic domain of GP2 plays a role in ER location.
It also contains a zinc-binding domain that allows SSP retention
in the GPC complex by accepting a cysteine from SSP as the fourth
ligand. {ECO:0000255|HAMAP-Rule:MF_04084}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
GP-C polyprotein is cleaved in the endoplasmic reticulum by the
host protease MBTPS1. Only cleaved glycoprotein is incorporated
into virions. {ECO:0000255|HAMAP-Rule:MF_04084}.
-!- PTM: The SSP remains stably associated with the GP complex
following cleavage by signal peptidase and plays crucial roles in
the trafficking of GP through the secretory pathway.
{ECO:0000255|HAMAP-Rule:MF_04084}.
-!- SIMILARITY: Belongs to the arenaviridae GPC protein family.
{ECO:0000255|HAMAP-Rule:MF_04084}.
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EMBL; M20869; AAA46256.1; -; Genomic_RNA.
EMBL; AY847350; AAX49341.1; -; Genomic_RNA.
EMBL; DQ361065; ABC96001.2; -; Genomic_RNA.
PIR; A28920; VGXPLA.
PIR; B26345; VGXPLM.
RefSeq; NP_694851.1; NC_004294.1.
PDB; 5JWD; X-ray; 2.50 A; C=392-400.
PDB; 5JWE; X-ray; 2.40 A; P/Q/R/S=92-101.
PDBsum; 5JWD; -.
PDBsum; 5JWE; -.
ProteinModelPortal; P09991; -.
SMR; P09991; -.
TCDB; 1.G.8.1.1; the arenavirus fusion protein (av-fp) family.
PRIDE; P09991; -.
GeneID; 956591; -.
KEGG; vg:956591; -.
OrthoDB; VOG0900016T; -.
Proteomes; UP000002474; Genome.
Proteomes; UP000121528; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
HAMAP; MF_04084; ARENA_GPC; 1.
InterPro; IPR001535; Arena_glycoprot.
Pfam; PF00798; Arena_glycoprot; 1.
PIRSF; PIRSF004028; GPC_ArenaV; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host endoplasmic reticulum; Host Golgi apparatus;
Host membrane; Host-virus interaction; Lipoprotein; Membrane;
Metal-binding; Myristate; Reference proteome; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell; Zinc.
INIT_MET 1 1 Removed; by host. {ECO:0000255|HAMAP-
Rule:MF_04084}.
CHAIN 2 498 Pre-glycoprotein polyprotein GP complex.
{ECO:0000255|HAMAP-Rule:MF_04084}.
/FTId=PRO_0000356255.
CHAIN 2 58 Stable signal peptide.
{ECO:0000255|HAMAP-Rule:MF_04084}.
/FTId=PRO_0000356256.
CHAIN 59 265 Glycoprotein G1. {ECO:0000255|HAMAP-
Rule:MF_04084}.
/FTId=PRO_0000036603.
CHAIN 266 498 Glycoprotein G2. {ECO:0000255|HAMAP-
Rule:MF_04084}.
/FTId=PRO_0000036604.
TOPO_DOM 2 17 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04084}.
TRANSMEM 18 32 Helical. {ECO:0000255|HAMAP-
Rule:MF_04084}.
TOPO_DOM 33 33 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_04084}.
TRANSMEM 34 53 Helical. {ECO:0000255|HAMAP-
Rule:MF_04084}.
TOPO_DOM 54 58 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04084}.
TOPO_DOM 59 438 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04084}.
TRANSMEM 439 459 Helical. {ECO:0000255|HAMAP-
Rule:MF_04084}.
TOPO_DOM 460 498 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_04084}.
METAL 57 57 Zinc 1. {ECO:0000255|HAMAP-
Rule:MF_04084}.
METAL 461 461 Zinc 2; via tele nitrogen.
{ECO:0000255|HAMAP-Rule:MF_04084}.
METAL 463 463 Zinc 2; via tele nitrogen.
{ECO:0000255|HAMAP-Rule:MF_04084}.
METAL 469 469 Zinc 2. {ECO:0000255|HAMAP-
Rule:MF_04084}.
METAL 473 473 Zinc 1; via pros nitrogen.
{ECO:0000255|HAMAP-Rule:MF_04084}.
METAL 481 481 Zinc 1. {ECO:0000255|HAMAP-
Rule:MF_04084}.
METAL 483 483 Zinc 1. {ECO:0000255|HAMAP-
Rule:MF_04084}.
SITE 58 59 Cleavage; by host signal peptidase.
{ECO:0000255|HAMAP-Rule:MF_04084}.
SITE 265 266 Cleavage; by host MBTPS1.
{ECO:0000255|HAMAP-Rule:MF_04084}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04084}.
DISULFID 92 239 {ECO:0000255|HAMAP-Rule:MF_04084}.
DISULFID 123 160 {ECO:0000255|HAMAP-Rule:MF_04084}.
DISULFID 184 220 {ECO:0000255|HAMAP-Rule:MF_04084}.
DISULFID 285 298 {ECO:0000255|HAMAP-Rule:MF_04084}.
DISULFID 307 316 {ECO:0000255|HAMAP-Rule:MF_04084}.
DISULFID 370 391 {ECO:0000255|HAMAP-Rule:MF_04084}.
VARIANT 176 176 D -> N (in strain: Isolate Armstrong
53b).
VARIANT 260 260 F -> L (in strain: Isolate CTL- and
Isolate Armstrong-derived variant Cl13).
VARIANT 313 313 A -> E (in strain: Isolate Armstrong 53b
and Isolate Armstrong-derived variant
Cl13).
MUTAGEN 12 12 P->A: 99% loss of virus infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 12 12 P->G: 96% loss of virus infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 16 16 D->A: More than 99% loss of infectivity;
when associated with A-17.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 16 16 D->K: More than 99% loss of infectivity;
when associated with K-17.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 17 17 E->A: More than 99% loss of infectivity;
when associated with A-16.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 17 17 E->K: More than 99% loss of infectivity;
when associated with K-16.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 20 20 N->A: 99% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 20 20 N->K: 91% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 20 20 N->Q: 98% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 33 33 K->A: More than 99% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 33 33 K->D: More than 99% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 37 37 N->A: 97% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 37 37 N->K: 92% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 37 37 N->Q: 7% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 49 49 F->A: More than 99% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 49 49 F->L: 95% loss of ionfectivity.
{ECO:0000269|PubMed:17376927}.
MUTAGEN 54 54 G->A: More than 99% loss of infectivity.
{ECO:0000269|PubMed:17376927}.
CONFLICT 177 177 A -> R (in Ref. 2; AAA46256).
SEQUENCE 498 AA; 56131 MW; 11737E3555122CE6 CRC64;
MGQIVTMFEA LPHIIDEVIN IVIIVLIVIT GIKAVYNFAT CGIFALISFL LLAGRSCGMY
GLKGPDIYKG VYQFKSVEFD MSHLNLTMPN ACSANNSHHY ISMGTSGLEL TFTNDSIISH
NFCNLTSAFN KKTFDHTLMS IVSSLHLSIR GNSNYKAVSC DFNNGITIQY NLTFSDAQSA
QSQCRTFRGR VLDMFRTAFG GKYMRSGWGW TGSDGKTTWC SQTSYQYLII QNRTWENHCT
YAGPFGMSRI LLSQEKTKFF TRRLAGTFTW TLSDSSGVEN PGGYCLTKWM ILAAELKCFG
NTAVAKCNVN HDAEFCDMLR LIDYNKAALS KFKEDVESAL HLFKTTVNSL ISDQLLMRNH
LRDLMGVPYC NYSKFWYLEH AKTGETSVPK CWLVTNGSYL NETHFSDQIE QEADNMITEM
LRKDYIKRQG STPLALMDLL MFSTSAYLVS IFLHLVKIPT HRHIKGGSCP KPHRLTNKGI
CSCGAFKVPG VKTVWKRR


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EIAAB34630 Ammonium transporter Rh type C,Oryctolagus cuniculus,Rabbit,Rh family type C glycoprotein,Rh type C glycoprotein,RHCG,Rhesus blood group family type C glycoprotein
EIAAB34610 Ammonium transporter Rh type B,Oryctolagus cuniculus,Rabbit,Rh family type B glycoprotein,Rh type B glycoprotein,RHBG,Rhesus blood group family type B glycoprotein
EIAAB34609 Ammonium transporter Rh type B,Mouse,Mus musculus,Rh family type B glycoprotein,Rh type B glycoprotein,Rhbg,Rhesus blood group family type B glycoprotein
EIAAB34606 Ammonium transporter Rh type B,Rat,Rattus norvegicus,Rh family type B glycoprotein,Rh type B glycoprotein,Rhbg,Rhesus blood group family type B glycoprotein
EIAAB34628 Ammonium transporter Rh type C,Rat,Rattus norvegicus,Rh family type C glycoprotein,Rh type C glycoprotein,Rhcg,Rhesus blood group family type C glycoprotein


 

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