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Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)

 RGCC_HUMAN              Reviewed;         137 AA.
Q9H4X1; Q6NZ48; Q9UL69;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-AUG-2020, entry version 128.
RecName: Full=Regulator of cell cycle RGCC;
AltName: Full=Response gene to complement 32 protein;
Short=RGC-32;
Name=RGCC; Synonyms=C13orf15, RGC32;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, SUBCELLULAR
LOCATION, MUTAGENESIS OF THR-111, PHOSPHORYLATION AT THR-111, AND TISSUE
SPECIFICITY.
TISSUE=Fetal brain;
PubMed=11687586; DOI=10.1074/jbc.m109354200;
Badea T., Niculescu F., Soane L., Fosbrink M., Sorana H., Rus V.,
Shin M.L., Rus H.;
"RGC-32 increases p34CDC2 kinase activity and entry of aortic smooth muscle
cells into S-phase.";
J. Biol. Chem. 277:502-508(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY.
PubMed=15713436; DOI=10.1016/j.yexmp.2004.11.001;
Fosbrink M., Cudrici C., Niculescu F., Badea T.C., David S., Shamsuddin A.,
Shin M.L., Rus H.;
"Overexpression of RGC-32 in colon cancer and other tumors.";
Exp. Mol. Pathol. 78:116-122(2005).
[5]
INTERACTION WITH PLK1, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17146433; DOI=10.1038/sj.onc.1210148;
Saigusa K., Imoto I., Tanikawa C., Aoyagi M., Ohno K., Nakamura Y.,
Inazawa J.;
"RGC32, a novel p53-inducible gene, is located on centrosomes during
mitosis and results in G2/M arrest.";
Oncogene 26:1110-1121(2007).
[6]
FUNCTION.
PubMed=19158077; DOI=10.1074/jbc.m900039200;
Huang W.Y., Li Z.G., Rus H., Wang X., Jose P.A., Chen S.Y.;
"RGC-32 mediates transforming growth factor-beta-induced epithelial-
mesenchymal transition in human renal proximal tubular cells.";
J. Biol. Chem. 284:9426-9432(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-75; SER-97
AND THR-111, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
FUNCTION, AND INDUCTION.
PubMed=22163048; DOI=10.1371/journal.pone.0028638;
Schlick S.N., Wood C.D., Gunnell A., Webb H.M., Khasnis S., Schepers A.,
West M.J.;
"Upregulation of the cell-cycle regulator RGC-32 in Epstein-Barr virus-
immortalized cells.";
PLoS ONE 6:E28638-E28638(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Modulates the activity of cell cycle-specific kinases.
Enhances CDK1 activity. May contribute to the regulation of the cell
cycle. May inhibit growth of glioma cells by promoting arrest of
mitotic progression at the G2/M transition. Fibrogenic factor
contributing to the pathogenesis of renal fibrosis through fibroblast
activation. {ECO:0000269|PubMed:11687586, ECO:0000269|PubMed:17146433,
ECO:0000269|PubMed:19158077, ECO:0000269|PubMed:22163048}.
-!- SUBUNIT: Interacts with SMAD3 (By similarity). Interacts with CDK1 and
PLK1. {ECO:0000250, ECO:0000269|PubMed:17146433}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Note=Cytoplasmic in
unstimulated cells. Nuclear after activation by complement. Associated
with the centrosome during prometaphase and metaphase.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H4X1-1; Sequence=Displayed;
Name=2;
IsoId=Q9H4X1-2; Sequence=VSP_022873;
-!- TISSUE SPECIFICITY: Detected in brain, heart and liver (at protein
level). Highly expressed in liver, skeletal muscle, kidney and
pancreas. Detected at lower levels in heart, brain and placenta.
Detected in aorta endothelial cells. Overexpressed in colon, breast,
prostate, bladder, lung, and ovarian cancer tissues.
{ECO:0000269|PubMed:11687586, ECO:0000269|PubMed:15713436}.
-!- INDUCTION: By Epstein-Barr virus (EBV). Up-regulated in aorta
endothelial cells in response to complement activation.
{ECO:0000269|PubMed:11687586, ECO:0000269|PubMed:22163048}.
---------------------------------------------------------------------------
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EMBL; AF036549; AAF04336.1; -; mRNA.
EMBL; AL354833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC066334; AAH66334.1; -; mRNA.
CCDS; CCDS41880.1; -. [Q9H4X1-1]
RefSeq; NP_054778.2; NM_014059.2. [Q9H4X1-1]
SMR; Q9H4X1; -.
BioGRID; 118805; 10.
IntAct; Q9H4X1; 6.
STRING; 9606.ENSP00000368664; -.
iPTMnet; Q9H4X1; -.
PhosphoSitePlus; Q9H4X1; -.
BioMuta; RGCC; -.
DMDM; 74752653; -.
EPD; Q9H4X1; -.
jPOST; Q9H4X1; -.
MassIVE; Q9H4X1; -.
MaxQB; Q9H4X1; -.
PaxDb; Q9H4X1; -.
PeptideAtlas; Q9H4X1; -.
PRIDE; Q9H4X1; -.
ProteomicsDB; 80878; -. [Q9H4X1-1]
ProteomicsDB; 80879; -. [Q9H4X1-2]
Antibodypedia; 23431; 92 antibodies.
Ensembl; ENST00000379359; ENSP00000368664; ENSG00000102760. [Q9H4X1-1]
GeneID; 28984; -.
KEGG; hsa:28984; -.
UCSC; uc001uyi.3; human. [Q9H4X1-1]
CTD; 28984; -.
DisGeNET; 28984; -.
EuPathDB; HostDB:ENSG00000102760.12; -.
GeneCards; RGCC; -.
HGNC; HGNC:20369; RGCC.
HPA; ENSG00000102760; Tissue enhanced (bone marrow, lung).
MIM; 610077; gene.
neXtProt; NX_Q9H4X1; -.
OpenTargets; ENSG00000102760; -.
PharmGKB; PA134895181; -.
eggNOG; ENOG502S1UB; Eukaryota.
GeneTree; ENSGT00390000011709; -.
HOGENOM; CLU_154700_0_0_1; -.
InParanoid; Q9H4X1; -.
OMA; QRHFHYE; -.
OrthoDB; 1604248at2759; -.
PhylomeDB; Q9H4X1; -.
TreeFam; TF336312; -.
PathwayCommons; Q9H4X1; -.
Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
BioGRID-ORCS; 28984; 5 hits in 873 CRISPR screens.
GeneWiki; C13orf15; -.
GenomeRNAi; 28984; -.
Pharos; Q9H4X1; Tbio.
PRO; PR:Q9H4X1; -.
Proteomes; UP000005640; Chromosome 13.
RNAct; Q9H4X1; protein.
Bgee; ENSG00000102760; Expressed in right lung and 238 other tissues.
Genevisible; Q9H4X1; HS.
GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0030295; F:protein kinase activator activity; IDA:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
GO; GO:0006956; P:complement activation; IMP:BHF-UCL.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0072537; P:fibroblast activation; ISS:UniProtKB.
GO; GO:0071850; P:mitotic cell cycle arrest; IDA:BHF-UCL.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL.
GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IDA:BHF-UCL.
GO; GO:0050710; P:negative regulation of cytokine secretion; IMP:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:0001100; P:negative regulation of exit from mitosis; IDA:BHF-UCL.
GO; GO:0090272; P:negative regulation of fibroblast growth factor production; IDA:BHF-UCL.
GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; IDA:BHF-UCL.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:BHF-UCL.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0050715; P:positive regulation of cytokine secretion; IMP:BHF-UCL.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:BHF-UCL.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IDA:BHF-UCL.
GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; IDA:BHF-UCL.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:BHF-UCL.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
InterPro; IPR029252; RGCC.
PANTHER; PTHR32193; PTHR32193; 1.
Pfam; PF15151; RGCC; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cytoplasm; Cytoskeleton; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1..137
/note="Regulator of cell cycle RGCC"
/id="PRO_0000274701"
COMPBIAS 11..26
/note="Ala-rich"
COMPBIAS 64..109
/note="Ser/Thr-rich"
MOD_RES 67
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9DBX1"
MOD_RES 69
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 71
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 75
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 91
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9Z2P4"
MOD_RES 97
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163"
MOD_RES 111
/note="Phosphothreonine; by CDK1"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:11687586"
VAR_SEQ 6..25
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:11687586"
/id="VSP_022873"
MUTAGEN 111
/note="T->A: Loss of phosphorylation. Reduced stimulation
of CDK1 activity."
/evidence="ECO:0000269|PubMed:11687586"
CONFLICT 3
/note="P -> Q (in Ref. 3; AAH66334)"
/evidence="ECO:0000305"
SEQUENCE 137 AA; 14559 MW; 76265677DBCD9525 CRC64;
MKPPAAQGSP AAAAAAAPAL DSAAAEDLSD ALCEFDAVLA DFASPFHERH FHYEEHLERM
KRRSSASVSD SSGFSDSESA DSLYRNSFSF SDEKLNSPTD STPALLSATV TPQKAKLGDT
KELEAFIADL DKTLASM


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[CDCA8 PESCRG3] Borealin (Cell division cycle-associated protein 8) (Dasra-B) (hDasra-B) (Pluripotent embryonic stem cell-related gene 3 protein)
[RCC1 CHC1] Regulator of chromosome condensation (Cell cycle regulatory protein) (Chromosome condensation protein 1)
[CFI IF] Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]
[] Capsid protein C (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Core protein p19) (Core protein p21) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (NS1) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2-3) (RNA-directed RNA polymerase) (Serine protease NS3) (gp35) (gp68) (gp70) (p21) (p27) (p56) (p68) (p70) (p8)
[POLY] Capsid protein C (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Core protein p19) (Core protein p21) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (NS1) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2-3) (RNA-directed RNA polymerase) (Serine protease NS3) (gp35) (gp68) (gp70) (p21) (p27) (p56) (p68) (p70) (p8)
[] Capsid protein C (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Core protein p19) (Core protein p21) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (NS1) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2-3) (RNA-directed RNA polymerase) (Serine protease NS3) (gp35) (gp68) (gp70) (p21) (p27) (p56) (p68) (p70) (p8)
[] Capsid protein C (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Core protein p19) (Core protein p21) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (NS1) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2-3) (RNA-directed RNA polymerase) (Serine protease NS3) (gp35) (gp68) (gp70) (p21) (p27) (p56) (p68) (p70) (p8)
[RAC1 TC25 MIG5] Ras-related C3 botulinum toxin substrate 1 (EC 3.6.5.2) (Cell migration-inducing gene 5 protein) (Ras-like protein TC25) (p21-Rac1)
[] Capsid protein C (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Core protein p19) (Core protein p21) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (NS1) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2-3) (RNA-directed RNA polymerase) (Serine protease NS3) (gp35) (gp68) (gp70) (p21) (p27) (p56) (p68) (p70) (p8) (Fragment)
[] Capsid protein C (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Core protein p19) (Core protein p21) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (NS1) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2-3) (RNA-directed RNA polymerase) (Serine protease NS3) (gp35) (gp68) (gp70) (p21) (p27) (p56) (p68) (p70) (p8) (Fragment)
[POLY] Capsid protein C (EC 2.7.7.48) (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Core protein p19) (Core protein p21) (Envelope glycoprotein E1) (Envelope glycoprotein E2) (Genome polyprotein) (Gp32) (Hepacivirin) (NS1) (NS3P) (NS5B) (Non-structural protein 4A) (Non-structural protein 4B) (Non-structural protein 5A) (Protease NS2-3) (RNA-directed RNA polymerase) (Serine protease NS3) (gp35) (gp68) (gp70) (p21) (p27) (p56) (p68) (p70) (p8)
[CCAR1 CARP1 DIS] Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Death inducer with SAP domain)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[CDK13 CDC2L CDC2L5 CHED KIAA1791] Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)
[RPA2 REPA2 RPA32 RPA34] Replication protein A 32 kDa subunit (RP-A p32) (Replication factor A protein 2) (RF-A protein 2) (Replication protein A 34 kDa subunit) (RP-A p34)
[Ccar1 Carp1] Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1)
[CFH HF HF1 HF2] Complement factor H (H factor 1)

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