Protein : Qrob_P0102040.2 Q. robur
Protein Identifier  ? Qrob_P0102040.2 Organism . Name  Quercus robur
Score  75.0 Score Type  egn
Protein Description  (M=1) PTHR12136:SF41 - PLECKSTRIN HOMOLOGY (PH) AND LIPID-BINDING START DOMAIN-CONTAINING PROTEIN (PTHR12136:SF41) Gene Prediction Quality  validated
Protein length 

Sequence

Length: 991  
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0 Synonyms

1 GO Terms

Identifier Name Description
GO:0008289 lipid binding Interacting selectively and non-covalently with a lipid.

20 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pmum:103332362 1 989 + 989 Gaps:22 100.00 736 70.52 0.0 protein ENHANCED DISEASE RESISTANCE 2-like
blastp_kegg lcl|pper:PRUPE_ppa002022mg 11 989 + 979 Gaps:22 99.86 727 71.49 0.0 hypothetical protein
blastp_kegg lcl|pxb:103936645 1 989 + 989 Gaps:24 100.00 735 70.48 0.0 protein ENHANCED DISEASE RESISTANCE 2-like
blastp_kegg lcl|mdm:103430788 1 989 + 989 Gaps:24 100.00 735 70.20 0.0 protein ENHANCED DISEASE RESISTANCE 2-like
blastp_kegg lcl|fve:101295576 1 989 + 989 Gaps:26 100.00 734 67.85 0.0 uncharacterized protein LOC101295576
blastp_kegg lcl|pper:PRUPE_ppa001967mg 1 989 + 989 Gaps:20 99.86 735 68.26 0.0 hypothetical protein
blastp_kegg lcl|mdm:103440657 1 989 + 989 Gaps:24 100.00 735 67.76 0.0 protein ENHANCED DISEASE RESISTANCE 2-like
blastp_kegg lcl|pmum:103343403 3 989 + 987 Gaps:25 99.86 738 67.71 0.0 protein ENHANCED DISEASE RESISTANCE 2
blastp_kegg lcl|cic:CICLE_v10030795mg 1 989 + 989 Gaps:28 99.87 744 67.56 0.0 hypothetical protein
blastp_kegg lcl|cit:102625473 1 989 + 989 Gaps:28 99.87 744 67.56 0.0 uncharacterized LOC102625473
rpsblast_cdd gnl|CDD|177782 9 986 + 978 Gaps:93 98.19 719 36.12 1e-123 PLN00188 PLN00188 enhanced disease resistance protein (EDR2) Provisional.
rpsblast_cdd gnl|CDD|115696 504 981 + 478 Gaps:18 100.00 215 52.56 6e-79 pfam07059 DUF1336 Protein of unknown function (DUF1336). This family represents the C-terminus (approximately 250 residues) of a number of hypothetical plant proteins of unknown function.
rpsblast_cdd gnl|CDD|176851 171 364 + 194 Gaps:16 92.23 193 34.27 4e-33 cd00177 START Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins. This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15 and related domains such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family specific lipids that bind in this pocket are known these include cholesterol (STARD1/STARD3/ STARD4/STARD5) 25-hydroxycholesterol (STARD5) phosphatidylcholine (STARD2/ STARD7/STARD10) phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments lipid metabolism and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer genetic disorders and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.
rpsblast_cdd gnl|CDD|197591 201 334 + 134 Gaps:3 63.90 205 32.82 2e-18 smart00234 START in StAR and phosphatidylcholine transfer protein. putative lipid-binding domain in StAR and phosphatidylcholine transfer protein.
rpsblast_cdd gnl|CDD|202011 191 334 + 144 Gaps:3 69.76 205 27.97 4e-14 pfam01852 START START domain.
rpsblast_cdd gnl|CDD|176880 227 314 + 88 Gaps:4 37.84 222 38.10 1e-12 cd08871 START_STARD10-like Lipid-binding START domain of mammalian STARD10 and related proteins. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52 PTCP-like and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice in several breast carcinoma cell lines and in 35% of primary human breast cancers and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).
rpsblast_cdd gnl|CDD|176877 208 359 + 152 Gaps:21 70.67 208 25.17 8e-08 cd08868 START_STARD1_3_like Cholesterol-binding START domain of mammalian STARD1 -3 and related proteins. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor cholesterol from the outer to the inner mitochondrial membrane across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH) an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.
rpsblast_cdd gnl|CDD|197590 9 114 + 106 Gaps:6 98.04 102 26.00 3e-07 smart00233 PH Pleckstrin homology domain. Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
rpsblast_cdd gnl|CDD|201053 9 114 + 106 Gaps:9 98.02 101 24.24 3e-07 pfam00169 PH PH domain. PH stands for pleckstrin homology.
rpsblast_cdd gnl|CDD|176270 11 113 + 103 Gaps:8 98.96 96 26.32 4e-07 cd00821 PH Pleckstrin homology (PH) domain. Pleckstrin homology (PH) domain. PH domains are only found in eukaryotes. They share little sequence conservation but all have a common fold which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase tyrosine kinases regulators of G-proteins endocytotic GTPases adaptors as well as cytoskeletal associated molecules and in lipid associated enzymes.

14 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 6 113 108 SSF50729 none none none
PANTHER 1 744 744 PTHR12136 none none none
SMART 8 117 110 SM00233 none Pleckstrin homology domain. IPR001849
Pfam 10 112 103 PF00169 none PH domain IPR001849
Gene3D 160 365 206 G3DSA:3.30.530.20 none none IPR023393
ProSiteProfiles 7 115 109 PS50003 none PH domain profile. IPR001849
Pfam 202 334 133 PF01852 none START domain IPR002913
Pfam 504 711 208 PF07059 none Protein of unknown function (DUF1336) IPR009769
Pfam 774 981 208 PF07059 none Protein of unknown function (DUF1336) IPR009769
PANTHER 1 744 744 PTHR12136:SF41 none none none
ProSiteProfiles 154 368 215 PS50848 none START domain profile. IPR002913
SUPERFAMILY 154 354 201 SSF55961 none none none
SMART 161 365 205 SM00234 none in StAR and phosphatidylcholine transfer protein IPR002913
Gene3D 7 114 108 G3DSA:2.30.29.30 none none IPR011993

0 Localization

7 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2014_rEpiBC*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran2_2014_aSeqBC_A4 Qrob_Chr08 8 v_15999_278 v_AP13YL15_395 32,52 4,22 57,22 lod 2,7561 6,7
Bourran2_2014_nFork*_A4 Qrob_Chr08 8 PIE175 s_1CD7GJ_1398 31,22 5,24 57,24 lod 2,6724 6,8
Bourran2_2015_rEpiBC_3P Qrob_Chr08 8 s_A9TNV_543 v_11837_70 9,93 9,83 11,15 lod 3.3 7.3
Champenoux_2015_nSeqBC_A4 Qrob_Chr08 8 v_AD7YD13_501 s_1A7IED_780 43,44 43,42 43,99 lod 3.7 8.9
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL3_d13Cf Qrob_Chr08 8 v_5216_549 v_11625_20 37.08 12,26 54,9 lod 6.5888 0.04

0 Targeting