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Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_XMRV3               Reviewed;        1733 AA.
Q2F7J3;
19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 1.
07-APR-2021, entry version 101.
RecName: Full=Gag-Pol polyprotein;
Short=Pr180gag-pol;
Contains:
RecName: Full=Matrix protein p15;
Short=MA;
Contains:
RecName: Full=RNA-binding phosphoprotein p12;
AltName: Full=pp12;
Contains:
RecName: Full=Capsid protein p30;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p10;
Short=NC-pol;
Contains:
RecName: Full=Protease p14;
Short=PR;
EC=3.4.23.-;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H p80;
Short=RT;
EC=2.7.7.49;
EC=2.7.7.7;
EC=3.1.26.4;
Contains:
RecName: Full=Integrase p46;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P03355};
EC=3.1.-.- {ECO:0000250|UniProtKB:P03355};
Name=gag-pol;
Xenotropic MuLV-related virus (isolate VP35) (XMRV).
Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
unclassified Gammaretrovirus.
NCBI_TaxID=356663;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16609730; DOI=10.1371/journal.ppat.0020025;
Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A.,
Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H.,
DeRisi J.L.;
"Identification of a novel Gammaretrovirus in prostate tumors of patients
homozygous for R462Q RNASEL variant.";
PLoS Pathog. 2:E25-E25(2006).
-!- FUNCTION: Matrix protein p15 targets Gag and gag-pol polyproteins to
the plasma membrane via a multipartite membrane binding signal, that
includes its myristoylated N-terminus. Also mediates nuclear
localization of the preintegration complex (By similarity).
{ECO:0000250}.
-!- FUNCTION: Capsid protein p30 forms the spherical core of the virion
that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
-!- FUNCTION: Nucleocapsid protein p10 is involved in the packaging and
encapsidation of two copies of the genome. Binds with high affinity to
conserved UCUG elements within the packaging signal, located near the
5'-end of the genome. This binding is dependent on genome dimerization
(By similarity). {ECO:0000250}.
-!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag
and Gag-Pol polyproteins during or shortly after the release of the
virion from the plasma membrane. Cleavages take place as an ordered,
step-wise cascade to yield mature proteins. This process is called
maturation. Displays maximal activity during the budding process just
prior to particle release from the cell. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H is a multifunctional
enzyme that converts the viral dimeric RNA genome into dsDNA in the
cytoplasm, shortly after virus entry into the cell. This enzyme
displays a DNA polymerase activity that can copy either DNA or RNA
templates, and a ribonuclease H (RNase H) activity that cleaves the RNA
strand of RNA-DNA heteroduplexes in a partially processive 3' to 5'
endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires
many steps. A tRNA binds to the primer-binding site (PBS) situated at
the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to
perform a short round of RNA-dependent minus-strand DNA synthesis. The
reading proceeds through the U5 region and ends after the repeated (R)
region which is present at both ends of viral RNA. The portion of the
RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA
product attached to the tRNA primer. This ssDNA/tRNA hybridizes with
the identical R region situated at the 3' end of viral RNA. This
template exchange, known as minus-strand DNA strong stop transfer, can
be either intra- or intermolecular. RT uses the 3' end of this newly
synthesized short ssDNA to perform the RNA-dependent minus-strand DNA
synthesis of the whole template. RNase H digests the RNA template
except for a polypurine tract (PPT) situated at the 5' end of the
genome. It is not clear if both polymerase and RNase H activities are
simultaneous. RNase H probably can proceed both in a polymerase-
dependent (RNA cut into small fragments by the same RT performing DNA
synthesis) and a polymerase-independent mode (cleavage of remaining RNA
fragments by free RTs). Secondly, RT performs DNA-directed plus-strand
DNA synthesis using the PPT that has not been removed by RNase H as
primers. PPT and tRNA primers are then removed by RNase H. The 3' and
5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate.
Strand displacement synthesis by RT to the PBS and PPT ends produces a
blunt ended, linear dsDNA copy of the viral genome that includes long
terminal repeats (LTRs) at both ends (By similarity). {ECO:0000250}.
-!- FUNCTION: Integrase catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. This enzyme activity takes place after virion entry into a
cell and reverse transcription of the RNA genome in dsDNA. The first
step in the integration process is 3' processing. This step requires a
complex comprising the viral genome, matrix protein and integrase. This
complex is called the pre-integration complex (PIC). The integrase
protein removes 2 nucleotides from each 3' end of the viral DNA,
leaving recessed CA OH's at the 3' ends. In the second step that
requires cell division, the PIC enters cell nucleus. In the third step,
termed strand transfer, the integrase protein joins the previously
processed 3' ends to the 5' ends of strands of target cellular DNA at
the site of integration. The last step is viral DNA integration into
host chromosome (By similarity). {ECO:0000250}.
-!- FUNCTION: Gag-Pol polyprotein plays a role in budding and is processed
by the viral protease during virion maturation outside the cell. During
budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-
like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to
Gag binding host factors. Interaction with HECT ubiquitin ligases
probably link the viral protein to the host ESCRT pathway and
facilitate release (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130,
Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
ChEBI:CHEBI:83828; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
ProRule:PRU00405};
-!- CATALYTIC ACTIVITY:
Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130,
Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
ChEBI:CHEBI:83828; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
ProRule:PRU00405};
-!- CATALYTIC ACTIVITY:
Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for reverse transcriptase polymerase
activity. {ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
{ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Magnesium ions are required for integrase activity. Binds at least
1, maybe 2 magnesium ions. {ECO:0000250};
-!- SUBUNIT: Capsid protein p30 is a homohexamer, that further associates
as homomultimer. The virus core is composed of a lattice formed from
hexagonal rings, each containing six capsid monomers. The protease is a
homodimer, whose active site consists of two apposed aspartic acid
residues. The reverse transcriptase is a monomer (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane
{ECO:0000305}; Lipid-anchor {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Nucleocapsid protein p10]: Virion {ECO:0000305}.
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle release. They can occur individually or in
close proximity within structural proteins. They interacts with sorting
cellular proteins of the multivesicular body (MVB) pathway. Most of
these proteins are class E vacuolar protein sorting factors belonging
to ESCRT-I, ESCRT-II or ESCRT-III complexes. RNA-binding phosphoprotein
p12 contains one L domain: a PPXY motif which potentially interacts
with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is
essential for virus egress. Matrix protein p15 contains one L domain: a
PTAP/PSAP motif, which potentially interacts with the UEV domain of
TSG101. The junction between the matrix protein p15 and RNA-binding
phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which
potentially interacts with PDCD6IP. Both PSAP and LYPX(n)L domains
might play little to no role in budding and possibly drive residual
virus release. contains (By similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages by the viral protease yield mature
proteins. The protease is released by autocatalytic cleavage. The
polyprotein is cleaved during and after budding, this process is termed
maturation (By similarity). {ECO:0000250}.
-!- PTM: Capsid protein p30 is sumoylated; which is required for virus
replication.
-!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
residues. {ECO:0000250}.
-!- MISCELLANEOUS: This protein is translated as a gag-pol fusion protein
by episodic readthrough of the gag protein termination codon.
Readthrough of the terminator codon TAG occurs between the codons for
536-Asp and 538-Gly (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The nucleocapsid protein p10 released from Pol
polyprotein (NC-pol) is a few amino acids shorter than the nucleocapsid
protein p10 released from Gag polyprotein (NC-gag). {ECO:0000250}.
-!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme that
lacks a proof-reading function. High mutations rate is a direct
consequence of this characteristic. RT also displays frequent template
swiching leading to high recombination rate. Recombination mostly
occurs between homologous regions of the two copackaged RNA genomes. If
these two RNA molecules derive from different viral strains, reverse
transcription will give rise to highly recombinated proviral DNAs.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
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EMBL; DQ241301; ABB83225.1; -; Genomic_RNA.
PDB; 3V1O; X-ray; 1.88 A; A=1154-1328.
PDB; 3V1Q; X-ray; 2.00 A; A=1155-1328.
PDB; 3V1R; X-ray; 2.80 A; A=1154-1328.
PDBsum; 3V1O; -.
PDBsum; 3V1Q; -.
PDBsum; 3V1R; -.
SMR; Q2F7J3; -.
Proteomes; UP000008601; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
GO; GO:0019068; P:virion assembly; IEA:InterPro.
Gene3D; 1.10.150.180; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 3.30.70.270; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR043502; DNA/RNA_pol_sf.
InterPro; IPR000840; G_retro_matrix.
InterPro; IPR036946; G_retro_matrix_sf.
InterPro; IPR039464; Gag-pol_Znf-H3C2.
InterPro; IPR003036; Gag_P30.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR040643; MLVIN_C.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR000477; RT_dom.
InterPro; IPR041577; RT_RNaseH_2.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF01140; Gag_MA; 1.
Pfam; PF02093; Gag_p30; 1.
Pfam; PF18697; MLVIN_C; 1.
Pfam; PF00075; RNase_H; 1.
Pfam; PF17919; RT_RNaseH_2; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF00098; zf-CCHC; 1.
Pfam; PF16721; zf-H3C2; 1.
SMART; SM00343; ZnF_C2HC; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 2.
SUPFAM; SSF56672; SSF56672; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS50879; RNASE_H; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Aspartyl protease; Capsid protein; Coiled coil;
DNA integration; DNA recombination; DNA-binding;
DNA-directed DNA polymerase; Endonuclease; Host cell membrane;
Host membrane; Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
Phosphoprotein; Protease; RNA suppression of termination; RNA-binding;
RNA-directed DNA polymerase; Transferase; Ubl conjugation;
Viral genome integration; Viral matrix protein; Viral nucleoprotein;
Virion; Virus entry into host cell; Zinc; Zinc-finger.
INIT_MET 1
/note="Removed; by host"
/evidence="ECO:0000250"
CHAIN 2..1733
/note="Gag-Pol polyprotein"
/evidence="ECO:0000250"
/id="PRO_0000390852"
CHAIN 2..129
/note="Matrix protein p15"
/evidence="ECO:0000250"
/id="PRO_0000390853"
CHAIN 130..213
/note="RNA-binding phosphoprotein p12"
/evidence="ECO:0000250"
/id="PRO_0000390854"
CHAIN 214..476
/note="Capsid protein p30"
/evidence="ECO:0000250"
/id="PRO_0000390855"
CHAIN 477..532
/note="Nucleocapsid protein p10"
/evidence="ECO:0000250"
/id="PRO_0000390856"
CHAIN 533..657
/note="Protease p14"
/evidence="ECO:0000250"
/id="PRO_0000390857"
CHAIN 658..1328
/note="Reverse transcriptase/ribonuclease H p80"
/evidence="ECO:0000250"
/id="PRO_0000390858"
CHAIN 1329..1733
/note="Integrase p46"
/evidence="ECO:0000250"
/id="PRO_0000390859"
DOMAIN 559..629
/note="Peptidase A2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
DOMAIN 739..930
/note="Reverse transcriptase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
DOMAIN 1172..1318
/note="RNase H"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
DOMAIN 1442..1600
/note="Integrase catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
ZN_FING 500..517
/note="CCHC-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
COILED 436..476
/evidence="ECO:0000255"
MOTIF 109..112
/note="PTAP/PSAP motif"
MOTIF 128..132
/note="LYPX(n)L motif"
MOTIF 161..164
/note="PPXY motif"
COMPBIAS 71..191
/note="Pro-rich"
ACT_SITE 564
/note="Protease; shared with dimeric partner"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
METAL 807
/note="Magnesium; catalytic; for reverse transcriptase
activity"
/evidence="ECO:0000250"
METAL 881
/note="Magnesium; catalytic; for reverse transcriptase
activity"
/evidence="ECO:0000250"
METAL 882
/note="Magnesium; catalytic; for reverse transcriptase
activity"
/evidence="ECO:0000250"
METAL 1181
/note="Magnesium; for RNase H activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
METAL 1219
/note="Magnesium; for RNase H activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
METAL 1240
/note="Magnesium; for RNase H activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
METAL 1310
/note="Magnesium; for RNase H activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
METAL 1453
/note="Magnesium; catalytic; for integrase activity"
/evidence="ECO:0000250"
METAL 1512
/note="Magnesium; catalytic; for integrase activity"
/evidence="ECO:0000250"
SITE 129..130
/note="Cleavage; by viral protease p14"
/evidence="ECO:0000250"
SITE 213..214
/note="Cleavage; by viral protease p14"
/evidence="ECO:0000250"
SITE 476..477
/note="Cleavage; by viral protease p14"
/evidence="ECO:0000250"
SITE 532..533
/note="Cleavage; by viral protease p14"
/evidence="ECO:0000250"
SITE 657..658
/note="Cleavage; by viral protease p14"
/evidence="ECO:0000250"
SITE 1328..1329
/note="Cleavage; by viral protease p14"
/evidence="ECO:0000250"
MOD_RES 190
/note="Phosphoserine; by host"
/evidence="ECO:0000250"
LIPID 2
/note="N-myristoyl glycine; by host"
/evidence="ECO:0000250"
STRAND 1167..1169
/evidence="ECO:0007744|PDB:3V1O"
STRAND 1175..1186
/evidence="ECO:0007744|PDB:3V1O"
STRAND 1188..1198
/evidence="ECO:0007744|PDB:3V1O"
STRAND 1200..1209
/evidence="ECO:0007744|PDB:3V1O"
HELIX 1215..1229
/evidence="ECO:0007744|PDB:3V1O"
TURN 1230..1232
/evidence="ECO:0007744|PDB:3V1O"
STRAND 1233..1240
/evidence="ECO:0007744|PDB:3V1O"
HELIX 1242..1249
/evidence="ECO:0007744|PDB:3V1O"
HELIX 1251..1257
/evidence="ECO:0007744|PDB:3V1O"
STRAND 1261..1264
/evidence="ECO:0007744|PDB:3V1O"
STRAND 1268..1270
/evidence="ECO:0007744|PDB:3V1Q"
HELIX 1271..1280
/evidence="ECO:0007744|PDB:3V1O"
STRAND 1283..1291
/evidence="ECO:0007744|PDB:3V1O"
HELIX 1301..1322
/evidence="ECO:0007744|PDB:3V1O"
SEQUENCE 1733 AA; 193803 MW; 35B226FA584B5122 CRC64;
MGQTVTTPLS LTLQHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFNVGW PQDGTFNLGV
ISQVKSRVFC PGPHGHPDQV PYIVTWEALA YDPPPWVKPF VSPKPPPLPT APVLPPGPSA
QPPSRSALYP ALTLSIKSKP PKPQVLPDSG GPLIDLLTED PPPYGVQPSS SARENNEEEA
ATTSEVSPPS PMVSRLRGRR DPPAADSTTS QAFPLRMGGD GQLQYWPFSS SDLYNWKNNN
PSFSEDPGKL TALIESVLIT HQPTWDDCQQ LLGTLLTGEE KQRVLLEAGK AVRGNDGRPT
QLPNEVNAAF PLERPDWDYT TTEGRNHLVL YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN
ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA PDIGRKLERL EDLKSKTLGD
LVREAEKIFN KRETPEEREE RIRREIEEKE ERRRAEDEQR ERERDRRRHR EMSKLLATVV
IGQRQDRQGG ERRRPQLDKD QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLTLGDXGGQ
GQEPPPEPRI TLKVGGQPVT FLVDTGAQHS VLTQNPGPLS DKSAWVQGAT GGKRYRWTTD
RKVHLATGKV THSFLHVPDC PYPLLGRDLL TKLKAQIHFE GSGAQVVGPM GQPLQVLTLN
IENKYRLHET SKEPDVPLGS TWLSDFPQAW AETGGMGLAV RQAPLIIPLK ATSTPVSIKQ
YPMSQEARLG IKPHIQRLLD QGILVPCQSP WNTPLLPVKK PGTNDYRPVQ DLREVNKRVE
DIHPTVPNPY NLLSGLPPSH QWYTVLDLKD AFFCLRLHPT SQPLFAFEWR DPEMGISGQL
TWTRLPQGFK NSPTLFDEAL HRDLADFRIQ HPDLILLQYV DDLLLAATSE QDCQRGTRAL
LQTLGNLGYR ASAKKAQICQ KQVKYLGYLL KEGQRWLTEA RKETVMGQPT PKTPRQLREF
LGTAGFCRLW IPGFAEMAAP LYPLTKTGTL FNWGPDQQKA YQEIKQALLT APALGLPDLT
KPFELFVDEK QGYAKGVLTQ KLGPWRRPVA YLSKKLDPVA AGWPPCLRMV AAIAVLTKDA
GKLTMGQPLV ILAPHAVEAL VKQPPDRWLS NARMTHYQAM LLDTDRVQFG PVVALNPATL
LPLPEKEAPH DCLEILAETH GTRPDLTDQP IPDADYTWYT DGSSFLQEGQ RRAGAAVTTE
TEVIWARALP AGTSAQRAEL IALTQALKMA EGKKLNVYTD SRYAFATAHV HGEIYRRRGL
LTSEGREIKN KNEILALLKA LFLPKRLSII HCPGHQKGNS AEARGNRMAD QAAREAAMKA
VLETSTLLIE DSTPYTPPHF HYTETDLKRL RELGATYNQT KGYWVLQGKP VMPDQSVFEL
LDSLHRLTHP SPQKMKALLD REESPYYMLN RDRTIQYVTE TCTACAQVNA SKAKIGAGVR
VRGHRPGTHW EVDFTEVKPG LYGYKYLLVF VDTFSGWVEA FPTKRETAKV VTKKLLEDIF
PRFGMPQVLG SDNGPAFASQ VSQSVADLLG IDWKLHCAYR PQSSGQVERM NRTIKETLTK
LTLASGTRDW VLLLPLALYR ARNTPGPHGL TPYEILYGAP PPLVNFHDPE MSKLTNSPSL
QAHLQALQAV QQEVWKPLAA AYQDQLDQPV IPHPFRVGDA VWVRRHQTKN LEPRWKGPYT
VLLTTPTALK VDGISAWIHA AHVKAATTPP AGTAWKVQRS QNPLKIRLTR GAP


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15-288-22841 Complement component 1 Q subcomponent-binding protein. mitochondrial - Glycoprotein gC1qBP; C1qBP; GC1q-R protein; Hyaluronan-binding protein 1; Mitochondrial matrix protein p32; p33 Polyclonal 0.05 mg
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