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Histidine-rich glycoprotein (Histidine-proline-rich glycoprotein) (HPRG) (Fragment)

 HRG_RABIT               Reviewed;         526 AA.
Q28640;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
10-MAY-2017, entry version 87.
RecName: Full=Histidine-rich glycoprotein;
AltName: Full=Histidine-proline-rich glycoprotein;
Short=HPRG;
Flags: Precursor; Fragment;
Name=HRG;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 9-23; 301-313 AND
422-429.
TISSUE=Serum;
PubMed=8639676; DOI=10.1021/bi952061t;
Borza D.-B., Tatum F.M., Morgan W.T.;
"Domain structure and conformation of histidine-proline-rich
glycoprotein.";
Biochemistry 35:1925-1934(1996).
[2]
HEME- AND METAL-BINDING.
PubMed=2636901; DOI=10.1002/jmr.300020304;
Morgan W.T., Deaciuc V., Riehm J.P.;
"A heme- and metal-binding hexapeptide from the sequence of rabbit
plasma histidine-rich glycoprotein.";
J. Mol. Recognit. 2:122-126(1989).
[3]
INTERACTION WITH PLG.
PubMed=9102401; DOI=10.1074/jbc.272.9.5718;
Borza D.B., Morgan W.T.;
"Acceleration of plasminogen activation by tissue plasminogen
activator on surface-bound histidine-proline-rich glycoprotein.";
J. Biol. Chem. 272:5718-5726(1997).
[4]
FUNCTION OF HIS/PRO-RICH DOMAIN.
PubMed=12235005;
Juarez J.C., Guan X., Shipulina N.V., Plunkett M.L., Parry G.C.,
Shaw D.E., Zhang J.C., Rabbani S.A., McCrae K.R., Mazar A.P.,
Morgan W.T., Donate F.;
"Histidine-proline-rich glycoprotein has potent antiangiogenic
activity mediated through the histidine-proline-rich domain.";
Cancer Res. 62:5344-5350(2002).
[5]
INTERACTION WITH TPM1.
PubMed=15269838; DOI=10.1267/THRO04080403;
Guan X., Juarez J.C., Qi X., Shipulina N.V., Shaw D.E., Morgan W.T.,
McCrae K.R., Mazar A.P., Donate F.;
"Histidine-proline rich glycoprotein (HPRG) binds and transduces anti-
angiogenic signals through cell surface tropomyosin on endothelial
cells.";
Thromb. Haemost. 92:403-412(2004).
-!- FUNCTION: Plasma glycoprotein that binds a number of ligands such
as heme, heparin, heparan sulfate, thrombospondin, plasminogen,
and divalent metal ions. Inhibits rosette formation. Acts as an
adapter protein and implicated in regulating many processes such
as immune complex and pathogen clearance, cell adhesion,
angiogenesis, coagulation and fibrinolysis. Mediates clearance of
necrotic cells through enhancing the phagocytosis of necrotic
cells in a heparan sulfate-dependent pathway. This process can be
regulated by the presence of certain HRG ligands such as heparin
and zinc ions. Binds to IgG subclasses of immunoglobins containing
kappa and lambda light chains with different affinities regulating
their clearance and inhibiting the formation of insoluble immune
complexes. Binds T-cells and alters the cell morphology Modulates
angiogenesis by blocking the CD6-mediated antiangiongenic effect
of thrombospondins, THBS1 and THBS2 (By similarity). Tethers
plasminogen to the cell surface. {ECO:0000250,
ECO:0000269|PubMed:12235005}.
-!- SUBUNIT: Interacts with THBS1 (via the TSP type I repeats); the
interaction blocks the antiangiogenic effect of THBS1 with CD36
(By similarity). Interacts with THBS2; the interaction blocks the
antiangiogenic effect of THBS2 with CD36. Interacts with HPSE; the
interaction is enhanced at acidic pH, partially inhibits binding
of HPSE to cell surface receptors and modulates its enzymatic
activity. Interacts (via the HRR domain) with TMP1; the
interaction partially mediates the antiangiogenic properties of
HRG. Interacts with kappa and lambda light chains of IgG
molecules. Interacts with ATP5A1; the interaction occurs on the
surface of T-cells and alters their cell morphology in concert
with CONA. Binds IgG molecules containing kappa and lambda light
chains and inhibits the formation of insoluble immunoglobulin
complexes. Interacts with F12; the interaction, which is enhanced
in the presence of zinc ions and inhibited by heparin-binding to
HRG, inhibits factor XII autoactivation and contact-initiated
coagulation (By similarity). Interacts with PLG (via its Kringle
domains); the interaction tethers PLG to the cell surface and
enhances its activation. Interacts (via the HRR domain) with TPM1;
the interaction appears to contribute to the antiangiogenic
properties of the HRR domain. {ECO:0000250,
ECO:0000269|PubMed:15269838, ECO:0000269|PubMed:9102401}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- DOMAIN: The His-rich (HRR) region contains approximately 12 tandem
internal repeats of the 5-residue G[H/P][H/P]PH consensus
sequence. HRR binds heparan sulfate and possesses antiangiogenic,
antibacterial and antifungal properties through binding Candida
cells, and preferentially lysing the ergosterol-containing
liposomes at low pH. The tandem repeats also bind divalent metal
ions and heme.
-!- DOMAIN: The cystatin domains can also bind heparan sulfate.
Binding is enhanced in the presence of zinc ions.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Proteolytic cleavage produces several HRG fragments which are
mostly disulfide-linked and, therefore, not released. On platelet
activation, may release a 33 kDa antiangiogenic peptide which
encompasses the HRR (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; U32189; AAC48516.1; -; mRNA.
UniGene; Ocu.2274; -.
PDB; 4CCV; X-ray; 1.93 A; A=131-245.
PDBsum; 4CCV; -.
ProteinModelPortal; Q28640; -.
SMR; Q28640; -.
STRING; 9986.ENSOCUP00000025254; -.
PRIDE; Q28640; -.
eggNOG; ENOG410IVJP; Eukaryota.
eggNOG; ENOG41117FH; LUCA.
HOGENOM; HOG000090255; -.
InParanoid; Q28640; -.
PMAP-CutDB; Q28640; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
GO; GO:0019865; F:immunoglobulin binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0050832; P:defense response to fungus; ISS:UniProtKB.
GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; ISS:UniProtKB.
GO; GO:0010593; P:negative regulation of lamellipodium assembly; ISS:UniProtKB.
GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:2000504; P:positive regulation of blood vessel remodeling; ISS:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0002839; P:positive regulation of immune response to tumor cell; ISS:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0030193; P:regulation of blood coagulation; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0010755; P:regulation of plasminogen activation; IDA:UniProtKB.
GO; GO:0010543; P:regulation of platelet activation; ISS:UniProtKB.
GO; GO:0043254; P:regulation of protein complex assembly; ISS:UniProtKB.
CDD; cd00042; CY; 1.
InterPro; IPR000010; Cystatin_dom.
Pfam; PF00031; Cystatin; 1.
SMART; SM00043; CY; 2.
1: Evidence at protein level;
3D-structure; Blood coagulation; Complete proteome; Copper;
Direct protein sequencing; Disulfide bond; Fibrinolysis; Glycoprotein;
Hemostasis; Heparin-binding; Reference proteome; Repeat; Secreted;
Signal; Zinc.
SIGNAL <1 8 {ECO:0000255}.
CHAIN 9 526 Histidine-rich glycoprotein.
/FTId=PRO_0000006710.
DOMAIN 9 126 Cystatin 1.
DOMAIN 127 243 Cystatin 2.
REGION 31 74 Interaction with ATP5A1. {ECO:0000250}.
COMPBIAS 251 296 Pro-rich.
COMPBIAS 329 498 His/Pro-rich (HRR).
SITE 303 304 Cleavage; by plasmin.
SITE 421 422 Cleavage; by plasmin.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 310 310 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 485 485 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 14 505 {ECO:0000250}.
DISULFID 68 79 {ECO:0000250}.
DISULFID 95 116 {ECO:0000250}.
DISULFID 193 415 {ECO:0000250}.
DISULFID 207 230 {ECO:0000250}.
DISULFID 272 302 {ECO:0000255}.
NON_TER 1 1
STRAND 134 137 {ECO:0000244|PDB:4CCV}.
HELIX 142 144 {ECO:0000244|PDB:4CCV}.
HELIX 145 157 {ECO:0000244|PDB:4CCV}.
HELIX 160 162 {ECO:0000244|PDB:4CCV}.
STRAND 165 177 {ECO:0000244|PDB:4CCV}.
STRAND 179 192 {ECO:0000244|PDB:4CCV}.
HELIX 193 196 {ECO:0000244|PDB:4CCV}.
STRAND 203 214 {ECO:0000244|PDB:4CCV}.
STRAND 219 221 {ECO:0000244|PDB:4CCV}.
STRAND 224 234 {ECO:0000244|PDB:4CCV}.
HELIX 235 237 {ECO:0000244|PDB:4CCV}.
TURN 239 242 {ECO:0000244|PDB:4CCV}.
SEQUENCE 526 AA; 58877 MW; 810F23D367D93D42 CRC64;
ATLQCSWALT PTDCKTTKPL AEKALDLINK WRRDGYLFQL LRVADAHLDG AESATVYYLV
LDVKETDCSV LSRKHWEDCD PDLTKRPSLD VIGQCKVIAT RYSDEYQTLR LNDFNCTTSS
VSSALANTKD SPVLFDFIED TEPFRKSADK ALEVYKSESE AYASFRVDRV ERVTRVKGGE
RTNYYVDFSV RNCSRSHFHR HPAFGFCRAD LSFDVEASNL ENPEDVIISC EVFNFEEHGN
ISGFRPHLGK TPLGTDGSRD HHHPHKPHKF GCPPPQEGED FSEGPPLQGG TPPLSPPFRP
RCRHRPFGTN ETHRFPHHRI SVNIIHRPPP HGHHPHGPPP HGHHPHGPPP HGHPPHGPPP
RHPPHGPPPH GHPPHGPPPH GHPPHGPPPH GHPPHGPPPH GHPPHGHGFH DHGPCDPPSH
KEGPQDLHQH AMGPPPKHPG KRGPGKGHFP FHWRRIGSVY QLPPLQKGEV LPLPEANFPQ
LLLRNHTHPL KPEIQPFPQV ASERCPEEFN GEFAQLSKFF PSTFPK


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