dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp05462

General Description

Peptide name : Peptidoglycan recognition protein 1

Source/Organism : Rat

Linear/Cyclic : Not found

Chirality : Not found

Sequence Information

Sequence : MLFAWAPFPALLGLADSCCFVVPRSEWKALPSECSKGLKKPVRYVVISHTAGSFCSSPDSCEQQARNVQLYQMKQLGWCDVAYNFLIGEDGHVYEGRGWTIKGDHTGPIWNPMSIGITFMGDYSHRVPAKRALRAALNLLKCGVSEGFLRSNYEVKGHRDVQSTLSPGDQLYEIIQSWDHYRE

Peptide length: 183

C-terminal modification: Not found

N-terminal modification : Not found

Non-natural peptide information: None

Activity Information

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : L929

Cancer type : Not found

Other activity : Not found

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 20590.2822 Dalton

Aliphatic index : 0.767

Instability index : 51.6617

Hydrophobicity (GRAVY) : -0.266

Isoelectric point : 7.6108

Charge (pH 7) : 0.9776

Aromaticity : 0.114

Molar extinction coefficient (cysteine, cystine): (44920, 45295)

Hydrophobic/hydrophilic ratio : 1.15294117

hydrophobic moment : -0.030

Missing amino acid : None

Most occurring amino acid : L

Most occurring amino acid frequency : 16

Least occurring amino acid : M

Least occurring amino acid frequency : 4

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.3, 0.3)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](CCSC)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@@H](NC(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(=O)O)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)CNC(=O)[C@H](CCCNC(=N)N)NC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)CNC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CS)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CS)NC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CS)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CS)NC(=O)[C@H](CS)NC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H]1CCCN1C(=O)[C@H](C)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](C)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)C(C)C)C(C)C)C(C)C)C(C)C)[C@@H](C)CC)[C@@H](C)O)C(C)C)C(C)C)[C@@H](C)CC)C(C)C)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)CC)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCSC)C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(=O)O)C(=O)NCC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)O)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)C(C)C)C(C)C)C(C)C)C(C)C)[C@@H](C)O

Secondary Structure :

Method Prediction
GOR HHHHHCCCHHCCTCTTTEEEECCTTTTTTCHHHHHTTTTCTEEEEEEEEETECEECCTTCHHHHHHHHHHHHHEETTCHHHTTHHEETTTTCEETTTEEEEETCCCCCCCCCTCEEEEEEECCTTCCHHHHHHHHHHHHHTTTCCTTEHHTTTHETEEEEEEEECCCTCCEEEEEEHHHHHTT
Chou-Fasman (CF) HHHHHCCHHHHHHHHCEEEEEECHHHHHCCCCCCCCCCCCEEEEEEECCCCEEECCCCHHHHHHHEEEEEHHHHEECCCEECEEECCCCEEEECCCEEEECCCCCEEEECCEEEEEEECCCCEEECHHHHHHHHHHHHHHEECCCCEECCCCCCCCCCEEEEEECCCCCCEEEEECCCCCCCC
Neural Network (NN) HHCCCCCCCHHHCCCCCCCECCCCCCCCCCCCCCCCCCCCCCEEEEEEECCCCCCCCCCCCCCHHHHHHHHHHHCCCCCCHCCCCCCCCCCCEECCCCEEEECCCCCCCCCCCCCEEEEECCCCCCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEECCCCCCC
Joint/Consensus HHHHHCCCHHHHCCCCCEEEECCCCCCCCCCCCCCCCCCCCEEEEEEEECCEEECCCCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCEECCCEEEEECCCCCCCCCCCCEEEEEECCCCCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCEEEEEECCCCCCEEEEEECCCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Not available.

ADMET Properties: Not available.

Cross Referencing databases

Pubmed Id : 11145837 16641100

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Not available

CancerPPD2 ID : Not available

Reference

1 : Rehman A, et al. The cloning of a rat peptidoglycan recognition protein (PGRP) and its induction in brain by sleep deprivation. Cytokine. 2001; 13:8-17. doi: 10.1006/cyto.2000.0800

2 : Hoffert JD, et al. Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites. Proc Natl Acad Sci U S A. 2006; 103:7159-64. doi: 10.1073/pnas.0600895103

Literature

Paper title : The cloning of a rat peptidoglycan recognition protein (PGRP) and its induction in brain by sleep deprivation.

Doi : https://doi.org/10.1006/cyto.2000.0800

Abstract : Peptidoglycan recognition protein (PGRP) binds to peptidoglycan (PG) or live bacteria and is upregulated by PG. PGRP is a ubiquitous protein involved in innate immunity. Tag7, a novel cytokine, is also induced by bacterial products; tag7 is apoptotic to murine L929 cells in a NF-kappaB-independent manner. Both of these genes are expressed in brain, lymphatic and haematopoietic tissues. We provide evidence that murine PGRP and tag7 encode identical transcripts and have structural relationships to lysozymes. Further, we have cloned the cDNA of rat PGRP and analyzed its expression in brains of sleep-deprived and control rats. The mRNA levels of PGRP/tag7 were measured by RT-PCR and compared to the housekeeping gene porphobilinogen deaminase (PBD). PGRP was constitutively expressed in rat brain. PGRP mRNA was increased by 43% and 17% in the brainstem and hypothalamus, respectively, in sleep-deprived rats compared to controls. The upregulation of PGRP expression by sleep deprivation suggests a role for PGRP in a homeostatic regulation of sleep.

Paper title : Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites.

Doi : https://doi.org/10.1073/pnas.0600895103

Abstract : Protein phosphorylation plays a key role in vasopressin signaling in the renal-collecting duct. Large-scale identification and quantification of phosphorylation events triggered by vasopressin is desirable to gain a comprehensive systems-level understanding of this process. We carried out phosphoproteomic analysis of rat inner medullary collecting duct cells by using a combination of phosphopeptide enrichment by immobilized metal affinity chromatography and phosphorylation site identification by liquid chromatography-mass spectrometry(n) neutral loss scanning. A total of 714 phosphorylation sites on 223 unique phosphoproteins were identified from inner medullary collecting duct samples treated short-term with either calyculin A or vasopressin. A number of proteins involved in cytoskeletal reorganization, vesicle trafficking, and transcriptional regulation were identified. Previously unidentified phosphorylation sites were found for membrane proteins essential to collecting duct physiology, including eight sites among aquaporin-2 (AQP2), aquaporin-4, and urea transporter isoforms A1 and A3. Through label-free quantification of phosphopeptides, we identified a number of proteins that significantly changed phosphorylation state in response to short-term vasopressin treatment: AQP2, Bclaf1, LRRC47, Rgl3, and SAFB2. In the presence of vasopressin, AQP2 monophosphorylated at S256 and diphosphorylated AQP2 (pS256/261) increased in abundance, whereas AQP2 monophosphorylated at S261 decreased, raising the possibility that both sites are involved in vasopressin-dependent AQP2 trafficking. This study reveals the practicality of liquid chromatography-mass spectrometry(n) neutral loss scanning for large-scale identification and quantification of protein phosphorylation in the analysis of cell signaling in a native mammalian system.