Protein : Qrob_P0321360.2 Q. robur

Protein Identifier  ? Qrob_P0321360.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=8) 3.4.11.2 - Membrane alanyl aminopeptidase. Code Enzyme  EC:3.4.11.2
Gene Prediction Quality  validated Protein length 

Sequence

Length: 246  

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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0008270 zinc ion binding Interacting selectively and non-covalently with zinc (Zn) ions.
GO:0006508 proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0008237 metallopeptidase activity Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

36 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pop:POPTR_0017s06650g 17 238 + 222 Gaps:142 40.77 888 36.74 6e-25 hypothetical protein
blastp_kegg lcl|mdm:103453592 17 238 + 222 Gaps:147 40.34 885 35.57 2e-17 aminopeptidase M1-like
blastp_kegg lcl|fve:101304606 16 238 + 223 Gaps:151 40.36 887 34.36 3e-17 puromycin-sensitive aminopeptidase-like
blastp_kegg lcl|pmum:103327661 15 238 + 224 Gaps:172 47.89 875 33.89 4e-17 aminopeptidase M1-like
blastp_kegg lcl|pxb:103932778 15 238 + 224 Gaps:151 40.30 881 35.77 3e-16 aminopeptidase M1-like
blastp_kegg lcl|pxb:103961541 15 238 + 224 Gaps:151 40.30 881 35.77 2e-15 aminopeptidase M1-like
blastp_kegg lcl|tcc:TCM_029095 17 192 + 176 Gaps:91 28.38 909 38.37 3e-15 Aminopeptidase M1 putative
blastp_kegg lcl|vvi:100244572 10 243 + 234 Gaps:87 35.43 889 42.22 6e-15 puromycin-sensitive aminopeptidase-like
blastp_kegg lcl|ppp:PHYPADRAFT_224579 15 104 + 90 Gaps:33 12.75 918 41.88 3e-14 hypothetical protein
blastp_kegg lcl|smo:SELMODRAFT_446442 15 104 + 90 Gaps:29 12.91 906 43.59 1e-13 hypothetical protein
blastp_pdb 3mdj_C 17 102 + 86 Gaps:29 12.27 921 32.74 3e-09 mol:protein length:921 Endoplasmic reticulum aminopeptidase 1
blastp_pdb 3mdj_B 17 102 + 86 Gaps:29 12.27 921 32.74 3e-09 mol:protein length:921 Endoplasmic reticulum aminopeptidase 1
blastp_pdb 3mdj_A 17 102 + 86 Gaps:29 12.27 921 32.74 3e-09 mol:protein length:921 Endoplasmic reticulum aminopeptidase 1
blastp_pdb 2yd0_A 17 102 + 86 Gaps:29 12.60 897 32.74 3e-09 mol:protein length:897 ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1
blastp_pdb 3qnf_C 17 102 + 86 Gaps:29 11.84 954 32.74 3e-09 mol:protein length:954 Endoplasmic reticulum aminopeptidase 1
blastp_pdb 3qnf_B 17 102 + 86 Gaps:29 11.84 954 32.74 3e-09 mol:protein length:954 Endoplasmic reticulum aminopeptidase 1
blastp_pdb 3qnf_A 17 102 + 86 Gaps:29 11.84 954 32.74 3e-09 mol:protein length:954 Endoplasmic reticulum aminopeptidase 1
blastp_pdb 3se6_B 17 101 + 85 Gaps:27 11.58 967 33.04 7e-08 mol:protein length:967 Endoplasmic reticulum aminopeptidase 2
blastp_pdb 3se6_A 17 101 + 85 Gaps:27 11.58 967 33.04 7e-08 mol:protein length:967 Endoplasmic reticulum aminopeptidase 2
blastp_uniprot_sprot sp|Q8VZH2|APM1_ARATH 15 104 + 90 Gaps:33 13.31 879 38.46 3e-14 Aminopeptidase M1 OS Arabidopsis thaliana GN APM1 PE 1 SV 1
blastp_uniprot_sprot sp|Q6Z6L4|APM1A_ORYSJ 15 104 + 90 Gaps:33 13.33 878 38.46 6e-14 Aminopeptidase M1-A OS Oryza sativa subsp. japonica GN Os02g0218200 PE 2 SV 1
blastp_uniprot_sprot sp|Q9USX1|APE1_SCHPO 13 100 + 88 Gaps:34 13.15 882 38.79 8e-14 Aminopeptidase 1 OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN ape1 PE 3 SV 1
blastp_uniprot_sprot sp|Q0J5V5|APM1B_ORYSJ 15 104 + 90 Gaps:33 13.37 875 39.32 7e-13 Aminopeptidase M1-B OS Oryza sativa subsp. japonica GN Os08g0398700 PE 2 SV 1
blastp_uniprot_sprot sp|Q6K4E7|APM1D_ORYSJ 17 104 + 88 Gaps:33 13.17 873 38.26 1e-12 Aminopeptidase M1-D OS Oryza sativa subsp. japonica GN Os09g0362800 PE 2 SV 1
blastp_uniprot_sprot sp|Q59KZ1|APE2_CANAL 15 100 + 86 Gaps:34 12.34 924 35.96 3e-12 Aminopeptidase 2 OS Candida albicans (strain SC5314 / ATCC MYA-2876) GN APE2 PE 1 SV 2
blastp_uniprot_sprot sp|Q0J2B5|APM1C_ORYSJ 17 104 + 88 Gaps:33 13.10 878 38.26 4e-12 Aminopeptidase M1-C OS Oryza sativa subsp. japonica GN Os09g0362500 PE 2 SV 2
blastp_uniprot_sprot sp|P32454|APE2_YEAST 14 100 + 87 Gaps:34 12.08 952 33.91 4e-11 Aminopeptidase 2 mitochondrial OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN APE2 PE 1 SV 4
blastp_uniprot_sprot sp|P37898|AAP1_YEAST 14 100 + 87 Gaps:34 13.43 856 35.65 6e-11 Alanine/arginine aminopeptidase OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN AAP1 PE 1 SV 2
blastp_uniprot_sprot sp|Q11011|PSA_MOUSE 17 101 + 85 Gaps:28 12.28 920 34.51 3e-10 Puromycin-sensitive aminopeptidase OS Mus musculus GN Npepps PE 1 SV 2
rpsblast_cdd gnl|CDD|189008 20 101 + 82 Gaps:28 24.66 446 33.64 4e-18 cd09601 M1_APN_2 Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3 Endoplasmic reticulum aminopeptidase 1 (ERAP1) Aminopeptidase Q (APQ). This M1 peptidase family includes eukaryotic and bacterial members: aminopeptidase N (APN) aminopeptidase Q (APQ laeverin) endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN CD13 Alanyl aminopeptidase EC 3.4.11.2) a Type II integral membrane protease consists of a small N-terminal cytoplasmic domain a single transmembrane domain and a large extracellular ectodomain that contains the active site. It preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte fibroblast endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain rheumatoid arthritis multiple sclerosis systemic sclerosis systemic lupus erythematosus polymyositis/dermatomyosytis and pulmonary sarcoidosis and is enhanced in tumor cells such as melanoma renal prostate pancreas colon gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1 also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP) adipocyte derived leucine aminopeptidase (A-LAP) or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1) associates with the closely related ER aminopeptidase ERAP2 for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS) an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3 together with factors F1 and F2 degrades the tricorn protease products producing free amino acids thus completing the proteasomal degradation pathway. F3 is homologous to F2 but not F1 and shows a strong preference for glutamate in the P1' position. APQ also known as laeverin is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III endokinin C and kisspeptin-10 all expressed in the placenta in large quantities. APN is a receptor for coronaviruses although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae causing extensive damage. Several different toxins including Cry1Aa Cry1Ab Cry1Ac Cry1Ba Cry1Ca and Cry1Fa have been shown to bind to APNs however a direct role of APN in cytotoxicity has been yet to be firmly established.

9 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 19 67 49 PF01433 none Peptidase family M1 IPR014782
Phobius 47 66 20 TRANSMEMBRANE none Region of a membrane-bound protein predicted to be embedded in the membrane. none
Phobius 1 46 46 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
SUPERFAMILY 16 104 89 SSF55486 none none none
PANTHER 20 104 85 PTHR11533:SF163 none none none
Gene3D 37 69 33 G3DSA:1.10.390.10 none none none
Gene3D 78 104 27 G3DSA:1.10.390.10 none none none
PANTHER 20 104 85 PTHR11533 none none IPR001930
Phobius 67 245 179 CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm. none

0 Localization

2 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_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2014_rEpiBC_3P Qrob_Chr05 5 s_2GDU0O_517 s_1BT8O3_239 25,81 0 55,45 lod 2,2101 5,5

0 Targeting