Protein : Qrob_P0208800.2 Q. robur
Protein Identifier  ? Qrob_P0208800.2 Organism . Name  Quercus robur
Score  4.0 Score Type  egn
Protein Description  (M=8) PTHR10857//PTHR10857:SF24 - COPINE // SUBFAMILY NOT NAMED Gene Prediction Quality  validated
Protein length 

Sequence

Length: 473  
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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0005515 protein binding Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
GO:0005544 calcium-dependent phospholipid binding Interacting selectively and non-covalently with phospholipids, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium.
GO:0060548 negative regulation of cell death Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.

27 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|vvi:100262302 1 472 + 472 Gaps:119 99.16 594 62.82 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250185 1 472 + 472 Gaps:119 99.16 594 62.99 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100263993 1 471 + 471 Gaps:119 98.99 594 62.93 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100250282 1 472 + 472 Gaps:119 99.16 594 62.65 0.0 protein BONZAI 3-like
blastp_kegg lcl|pper:PRUPE_ppa018159mg 1 472 + 472 Gaps:111 99.82 564 63.59 0.0 hypothetical protein
blastp_kegg lcl|vvi:100247065 1 472 + 472 Gaps:119 99.16 594 61.63 0.0 protein BONZAI 3-like
blastp_kegg lcl|vvi:100241932 1 472 + 472 Gaps:119 99.16 594 61.46 0.0 protein BONZAI 3-like
blastp_kegg lcl|pxb:103962883 1 468 + 468 Gaps:119 98.31 593 60.21 0.0 protein BONZAI 3-like
blastp_kegg lcl|pmum:103344705 1 472 + 472 Gaps:127 99.83 580 61.49 0.0 protein BONZAI 3
blastp_kegg lcl|rcu:RCOM_1429710 1 466 + 466 Gaps:123 99.66 581 60.45 0.0 copine putative
blastp_uniprot_sprot sp|Q5XQC7|BON3_ARATH 1 462 + 462 Gaps:120 98.97 584 56.40 0.0 Protein BONZAI 3 OS Arabidopsis thaliana GN BON3 PE 1 SV 1
blastp_uniprot_sprot sp|Q941L3|BON1_ARATH 1 464 + 464 Gaps:125 99.83 578 50.43 2e-178 Protein BONZAI 1 OS Arabidopsis thaliana GN BON1 PE 1 SV 2
blastp_uniprot_sprot sp|Q5S1W2|BON2_ARATH 1 460 + 460 Gaps:128 98.29 586 48.44 3e-173 Protein BONZAI 2 OS Arabidopsis thaliana GN BON2 PE 1 SV 2
blastp_uniprot_sprot sp|Q8IYJ1|CPNE9_HUMAN 14 461 + 448 Gaps:134 96.56 553 33.90 4e-72 Copine-9 OS Homo sapiens GN CPNE9 PE 1 SV 3
blastp_uniprot_sprot sp|Q9DC53|CPNE8_MOUSE 56 461 + 406 Gaps:123 87.18 577 34.79 1e-71 Copine-8 OS Mus musculus GN Cpne8 PE 2 SV 3
blastp_uniprot_sprot sp|Q86YQ8|CPNE8_HUMAN 56 461 + 406 Gaps:123 89.18 564 34.59 6e-71 Copine-8 OS Homo sapiens GN CPNE8 PE 1 SV 2
blastp_uniprot_sprot sp|Q5BJS7|CPNE9_RAT 14 461 + 448 Gaps:134 96.56 553 33.52 8e-71 Copine-9 OS Rattus norvegicus GN Cpne9 PE 2 SV 1
blastp_uniprot_sprot sp|Q1RLL3|CPNE9_MOUSE 39 461 + 423 Gaps:123 94.03 553 33.27 3e-70 Copine-9 OS Mus musculus GN Cpne9 PE 2 SV 1
blastp_uniprot_sprot sp|O75131|CPNE3_HUMAN 56 462 + 407 Gaps:120 93.30 537 32.53 4e-69 Copine-3 OS Homo sapiens GN CPNE3 PE 1 SV 1
blastp_uniprot_sprot sp|Q8BT60|CPNE3_MOUSE 56 462 + 407 Gaps:124 94.00 533 32.73 6e-68 Copine-3 OS Mus musculus GN Cpne3 PE 2 SV 2
rpsblast_cdd gnl|CDD|29232 277 451 + 175 Gaps:79 99.21 254 33.73 2e-49 cd01459 vWA_copine_like VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However the MIDAS motif is not totally conserved in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding..
rpsblast_cdd gnl|CDD|176013 39 234 + 196 Gaps:9 98.33 120 55.93 1e-28 cd04048 C2A_Copine C2 domain first repeat in Copine. There are 2 copies of the C2 domain present in copine a protein involved in membrane trafficking protein-protein interactions and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the first C2 repeat C2A and has a type-I topology.
rpsblast_cdd gnl|CDD|203562 326 417 + 92 Gaps:56 100.00 146 36.99 2e-26 pfam07002 Copine Copine. This family represents a conserved region approximately 180 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking and may also be involved in cell division and growth.
rpsblast_cdd gnl|CDD|176012 183 245 + 63 none 57.27 110 47.62 3e-20 cd04047 C2B_Copine C2 domain second repeat in Copine. There are 2 copies of the C2 domain present in copine a protein involved in membrane trafficking protein-protein interactions and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids inositol polyphosphates and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain such as protein kinase C or membrane trafficking proteins which contain at least two C2 domains such as synaptotagmin 1. However there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues primarily aspartates that serve as ligands for calcium ions. This cd contains the second C2 repeat C2B and has a type-I topology.
rpsblast_cdd gnl|CDD|197596 46 142 + 97 Gaps:14 82.18 101 34.94 5e-07 smart00239 C2 Protein kinase C conserved region 2 (CalB). Ca2+-binding motif present in phospholipases protein kinases C and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids inositol polyphosphates and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
rpsblast_cdd gnl|CDD|201052 185 260 + 76 Gaps:11 76.47 85 38.46 6e-07 pfam00168 C2 C2 domain.
rpsblast_kog gnl|CDD|36541 66 466 + 401 Gaps:122 93.95 529 37.83 1e-100 KOG1327 KOG1327 KOG1327 Copine [Signal transduction mechanisms].

13 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 1 464 464 PTHR10857:SF24 none none IPR031116
Pfam 387 417 31 PF07002 none Copine IPR010734
Pfam 326 382 57 PF07002 none Copine IPR010734
SMART 25 151 127 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
SMART 181 297 117 SM00239 none Protein kinase C conserved region 2 (CalB) IPR000008
ProSiteProfiles 57 136 80 PS50004 none C2 domain profile. IPR000008
Pfam 186 234 49 PF00168 none C2 domain IPR000008
Pfam 46 135 90 PF00168 none C2 domain IPR000008
SUPERFAMILY 57 160 104 SSF49562 none none IPR000008
SUPERFAMILY 186 234 49 SSF49562 none none IPR000008
Gene3D 49 159 111 G3DSA:2.60.40.150 none none IPR000008
PANTHER 1 464 464 PTHR10857 none none none
Gene3D 160 234 75 G3DSA:2.60.40.150 none none IPR000008

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_nLBD*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 34,91 16,12 53,62 lod 2,4961 5,2
Bourran2_2014_rEpiBC*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
Bourran_2000_2002_QTL6_Delta.F Qrob_Chr03 3 s_2HYXJ2_207 s_1AUAXK_317 29.12 6,3 45,37 lod 3.1666 0.026
Bourran2_2014_nLBD_3P Qrob_Chr03 3 s_1ET7H8_604 s_1BYNB5_834 23,73 0 46,72 lod 1,7573 3,8
PM_1999_QTL14_peak_Bud_burst_3P Qrob_Chr03 3 s_2F0SI1_756 v_6056_735 11,78 3,78 50,78 lod 2,5 4,5
Bourran2_2014_nFork*_3P Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,28 7,43 41,48 lod 2,4044 5,5
Bourran2_2014_rEpiBC*_3P Qrob_Chr03 3 s_1A3B3X_1163 s_1DKGMO_450 23,04 4,92 41,12 lod 2,5668 7

0 Targeting