wanglab/gogpt-training-data huggingface dataset:
Protein: Acyl-protein thioesterase 2 (APT-2) (EC 3.1.2.-) (Lysophospholipase 2) (Lysophospholipase II) (LPL-II) (LysoPLA II) (mLyso II) (Palmitoyl-protein hydrolase) (EC 3.1.2.22) (Q9WTL7)
Organism: Mus musculus (Mouse)
Function: Acts as a acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins, GAP43, ZDHHC6 or HRAS (By similarity). Deacylates GAP43 (By similarity). Mediates depalmitoylation of ZDHHC6 (By similarity). Has lysophospholipase activity. Hydrolyzes prostaglandin glycerol esters (PG-Gs). Hydrolyzes PG-Gs in the following order prostaglandin D2-glycerol ester (PGD2-G) > prostaglandin E2 glycerol ester (PGE2-G) > prostaglandin F2-alpha-glycerol ester (PGF2-alpha-G) (By similarity). Hydrolyzes 1-arachidonoylglycerol but not 2-arachidonoylglycerol or arachidonoylethanolamide (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95372}.
Interaction partners:
- Phospholipase B1, membrane-associated
- Glycerophosphocholine phosphodiesterase GPCPD1
- Patatin-like phospholipase domain-containing protein 6
- Phospholipase A and acyltransferase 3
- Patatin-like phospholipase domain-containing protein 7
- Neuromodulin
Sequence:
MCGNTMSVPLLTDAATVSGAERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAPRIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIEHEMKNGIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWLPLHRNFPQAANGSAKDLAILQCHGELDPMVPVRFGALTAEKLRTVVTPARVQFKTYPGVMHSSCPQEMAAVKEFLEKLLPPV
Protein: Adenylosuccinate synthetase isozyme 2 (AMPSase 2) (AdSS 2) (EC 6.3.4.4) (Adenylosuccinate synthetase, acidic isozyme) (Adenylosuccinate synthetase, liver isozyme) (L-type adenylosuccinate synthetase) (IMP--aspartate ligase 2) (A0A8I6AT75)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03127}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MSISESSPAATSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRCQGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGLDGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLRMCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQQLKGYMERIKPMVRDGVYFLYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAYTTRVGIGAFPTEQDNVSLFLRKKNHVPLTPALAHSCLSLHFCLSLHLHRSFGVLALTKLDILDMFTEIKVGVAYKLDGETIPHFPANQEVLNKVEVQYKTLPGWNTDISNARTFKELPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
Protein: Endoglucanase G (EC 3.2.1.4) (Cellulase G) (Endo-1,4-beta-glucanase G) (EgG) (Q05332)
Organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
Function: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Interaction partners:
- Cellulosomal-scaffolding protein A
- Cellulose 1,4-beta-cellobiosidase
- Beta-glucosidase A
- Thermostable beta-glucosidase B
- Type 3a cellulose-binding domain protein
- Glycosyltransferase 36
- Endoglucanase 1
- Glucanase
- Glycosyltransferase 36
- Cellulose 1,4-beta-cellobiosidase
Sequence:
MKKAKAIFSLVVALMVLAIFCFAQNTGSTATTAAAAVDSNNDDWLHCKGNKIYDMYGNEVWLTGANWFGFNCSENCFHGAWYDVKTILTSIADRGINLLRIPISTELLYSWMIGKPNPVSSVTASNNPPYHVVNPDFYDPETDDVKNSMEIFDIIMGYCKELGIKVMIDIHSPDANNSGHNYELWYGKETSTCGVVTTKMWIDTLVWLADKYKNDDTIIAFDLKNEPHGKRGYTAEVPKLLAKWDNSTDENNWKYAAETCAKAILEVNPKVLIVIEGVEQYPKTEKGYTYDTPDIWGATGDASPWYSAWWGGNLRGVKDYPIDLGPLNSQIVYSPHDYGPSVYAQPWFEKDFTMQTLLDDYWYDTWAYIHDQGIAPILIGEWGGHMDGGKNQKWMTLLRDYIVQNRIHHTFWCINPNSGDTGGLLGNDWSTWDEAKYALLKPALWQTKDGKFIGLDHKIPLGSKGISLGEYYGTPQASDPPATPTATPTKPAASSTPSFIYGDINSDGNVNSTDLGILKRIIVKNPPASANMDAADVNADGKVNSTDYTVLKRYLLRSIDKLPHTT
Protein: Urocortin (P55089)
Organism: Homo sapiens (Human)
Function: Acts in vitro to stimulate the secretion of adrenocorticotropic hormone (ACTH). Binds with high affinity to CRF receptor types 1, 2-alpha, and 2-beta. Plays a role in the establishment of normal hearing thresholds (By similarity). Reduces food intake and regulates ghrelin levels in gastric body and plasma (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Corticotropin-releasing factor receptor 1
- Corticotropin-releasing factor receptor 2
- Corticoliberin
- Urocortin-2
- Urocortin-3
- Corticotropin-releasing factor-binding protein
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Appetite-regulating hormone
- Pro-opiomelanocortin
Sequence:
MRQAGRAALLAALLLLVQLCPGSSQRSPEAAGVQDPSLRWSPGARNQGGGARALLLLLAERFPRRAGPGRLGLGTAGERPRRDNPSLSIDLTFHLLRTLLELARTQSQRERAEQNRIIFDSVGK
Protein: Crd2p (A0A1D8PL78)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MACSAAQCVCAQKSTCSCGKQPALKCNCSKASVENVVPSSNDACACGKRNKSSCTCGANAICDGTRDGETDFTNLK
Protein: Peptide methionine sulfoxide reductase A4, chloroplastic (AtMSRA4) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Protein-methionine-S-oxide reductase) (P54150)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. Prevents the methionine sulfoxidation of the heat shock protein HSP21 and its subsequent inactivation. MSRA family specifically reduces the MetSO S-enantiomer.
Subcellular location: Plastid, chloroplast stroma.
Interaction partners:
- Peptide methionine sulfoxide reductase B6
- Peptide methionine sulfoxide reductase B9
- Peptide methionine sulfoxide reductase B8
- Peptide methionine sulfoxide reductase B5
- Peptide methionine sulfoxide reductase B4
- Peptide methionine sulfoxide reductase B3
- Endoplasmic reticulum transmembrane protein
- Peptide methionine sulfoxide reductase B1, chloroplastic
- At3g03150
- Peptide methionine sulfoxide reductase B7
Sequence:
MQVLVVSPPLIAAASLSKPLNSLSKAALSFSRAKPICPFPQTSRRPISVYKSPMNNLFNRLGFGSRPQAQADPSSAAIAQGPDDDVPSSGQQFAQFGAGCFWGVELAYQRVPGVTKTEVGYSHGIVHNPSYEDVCTGTTGHNEVVRVQYDPKECSFESLLDVFWNRHDPTTLNRQGGDVGTQYRSGIYYYTDEQERIAREAVEKQQKILNKRIVTEILPATKFYRAENYHQQYLAKGGRMGLRQSAEKGCKDPIRCYG
Protein: Sodium/potassium-transporting ATPase subunit alpha-2 (Na(+)/K(+) ATPase alpha-2 subunit) (EC 7.2.2.13) (Sodium pump subunit alpha-2) (P50993)
Organism: Homo sapiens (Human)
Function: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients.
Subcellular location: Membrane {ECO:0000269|PubMed:7711835}; Multi-pass membrane protein {ECO:0000269|PubMed:7711835}. Cell membrane {ECO:0000269|PubMed:7711835}; Multi-pass membrane protein {ECO:0000269|PubMed:7711835}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit beta-3
- Sodium/potassium-transporting ATPase subunit gamma
- Protein ATP1B4
- Phospholemman
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Sodium/potassium-transporting ATPase subunit alpha-4
- Sodium/potassium-transporting ATPase subunit alpha-1
Sequence:
MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPMSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
Protein: Aspartic proteinase 3 (EC 3.4.23.41) (Proprotein convertase) (Yapsin-1) [Cleaved into: Aspartic proteinase 3 subunit alpha; Aspartic proteinase 3 subunit beta] (P32329)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cleaves proteins C-terminally to mono- and paired-basic residues. Involved in the shedding of a subset of GPI-anchored plasma membrane proteins from the cell surface, including itself, GAS1 and MSB2. May also play a role in the maturation of GPI-mannoproteins associated with the cell wall. Can process the alpha-mating factor precursor. Required for cell wall integrity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11737827, ECO:0000269|PubMed:14617149, ECO:0000269|PubMed:7657670, ECO:0000269|PubMed:9417119}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11737827, ECO:0000269|PubMed:14617149, ECO:0000269|PubMed:7657670, ECO:0000269|PubMed:9417119}. Note=GPI-anchored plasma membrane protein (GPI-PMP), peripherally distributed over the entire cell surface.
Interaction partners:
- Kexin
- Aspartic proteinase MKC7
- Signaling mucin MSB2
- Cerevisin
Sequence:
MKLKTVRSAVLSSLFASQVLGKIIPAANKRDDDSNSKFVKLPFHKLYGDSLENVGSDKKPEVRLLKRADGYEEIIITNQQSFYSVDLEVGTPPQNVTVLVDTGSSDLWIMGSDNPYCSSNSMGSSRRRVIDKRDDSSSGGSLINDINPFGWLTGTGSAIGPTATGLGGGSGTATQSVPASEATMDCQQYGTFSTSGSSTFRSNNTYFSISYGDGTFASGTFGTDVLDLSDLNVTGLSFAVANETNSTMGVLGIGLPELEVTYSGSTASHSGKAYKYDNFPIVLKNSGAIKSNTYSLYLNDSDAMHGTILFGAVDHSKYTGTLYTIPIVNTLSASGFSSPIQFDVTINGIGISDSGSSNKTLTTTKIPALLDSGTTLTYLPQTVVSMIATELGAQYSSRIGYYVLDCPSDDSMEIVFDFGGFHINAPLSSFILSTGTTCLLGIIPTSDDTGTILGDSFLTNAYVVYDLENLEISMAQARYNTTSENIEIITSSVPSAVKAPGYTNTWSTSASIVTGGNIFTVNSSQTASFSGNLTTSTASATSTSSKRNVGDHIVPSLPLTLISLLFAFI
Protein: 1,3-beta-glucanosyltransferase (EC 2.4.1.-) (G8B9C5)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU361209}; Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU361209}. Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
Interaction partners:
Sequence:
MRFTQLLPCLLSLSAPIWAKFEDTTPPIEIVGNKFFYSNNGSQFLMRGIAYQEDTSLISNTNLSYKDPLADVEACKRDVEHFKALNTNCLRVYAIDPDLDHDECMELLSEAGIYIIADLSQPKTSINRNDPSWDLDHYERYTEVIDKLSEYSNVLGFFAGNEVTNNKSNTDASPFVKAAVRDMKKYIEDSNGMRKIPVGYSSNDDEDTRIAIADYFACGSVEERADFFGINMYEWCGNSTYATSGYKDRTEEFEHLPVPIFFSEYGCNEKRPRLFTEVQTLYSPLMSDVWSGGIVYMYFEEDNKYGLVSIDGSSVSILDDYKYYSSEINNISPSYARASNEETATSTITCPDTDSTTWQASADLPPTPDKDFCECIAKSFECVVAEDVDEEDYGEIYADVCGRIDCSDISVNGTSGDYGDYSFCSHRDKLSFVLNLYYHDQNENSSACDFNGSASVNRDAESTSSCGVGSSRRSQGTRSATSTNSNSQSTTSGSRSNTNDANNSHIPNMSKFRLVSYVGFVTAIVGGISFVL
Protein: Epididymal secretory glutathione peroxidase (EC 1.11.1.9) (Epididymis-specific glutathione peroxidase-like protein) (EGLP) (Glutathione peroxidase 5) (GPx-5) (GSHPx-5) (O75715)
Organism: Homo sapiens (Human)
Function: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids.
Subcellular location: Secreted.
Interaction partners:
- Glutathione reductase, mitochondrial
- Peroxiredoxin-6
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Glutathione synthetase
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Polyunsaturated fatty acid 5-lipoxygenase
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Probable glutathione peroxidase 8
- Glutathione peroxidase 7
- Polyunsaturated fatty acid lipoxygenase ALOX15B
Sequence:
MTTQLRVVHLLPLLLACFVQTSPKQEKMKMDCHKDEKGTIYDYEAIALNKNEYVSFKQYVGKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPGLKYVRPGGGFVPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSEILGTFKSISWDPVKVHDIRWNFEKFLVGPDGIPVMRWSHRATVSSVKTDILAYLKQFKTK
Protein: Sortase B (EC 3.4.22.-) (Q8Y588)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Function: Transpeptidase that anchors surface proteins to the cell wall (Probable). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable). Catalyzes a cell wall sorting reaction in which a surface protein with the consensus sorting signal NP(Q/K)(T/S)(N/G/S)(D/A) is cleaved between the fourth and fifth residues, and the fourth position is linked to the cell wall (Probable). This is not the major sortase in Listeria, it seems to anchor only 2 proteins, Hbp2 (SvpA) and Hbp1.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- High-affinity heme uptake system protein IsdE
- Lmo2182 protein
- Hemin/hemoglobin-binding protein 1
- Probable heme-iron transport system permease protein IsdF
- Putative competence-damage inducible protein
- Hemin/hemoglobin-binding protein 2
- Lmo0366 protein
- Sortase A
- Heme-degrading monooxygenase
Sequence:
MKIKSFLGKSLTLVVLGVFLFSGWKIGMELYENKHNQTILDDAKAVYTKDAATTNVNGEVRDELRDLQKLNKDMVGWLTIIDTEIDYPILQSKDNDYYLHHNYKNEKARAGSIFKDYRNTNEFLDKNTIIYGHNMKDGSMFADLRKYLDKDFLVAHPTFSYESGLTNYEVEIFAVYETTTDFYYIETEFPETTDFEDYLQKVKQQSVYTSNVKVSGKDRIITLSTCDTEKDYEKGRMVIQGKLVTK
Protein: 1-aminocyclopropane-1-carboxylate synthase 7 (ACC synthase 7) (EC 4.4.1.14) (S-adenosyl-L-methionine methylthioadenosine-lyase 7) (Q9STR4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene.
Interaction partners:
- 1-aminocyclopropane-1-carboxylate oxidase 4
- 1-aminocyclopropane-1-carboxylate oxidase 5
- 1-aminocyclopropane-1-carboxylate oxidase 2
- 1-aminocyclopropane-1-carboxylate oxidase 3
- 5'-methylthioadenosine nucleosidase
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- 1-aminocyclopropane-1-carboxylate oxidase 1
- 1-aminocyclopropane-1-carboxylate oxidase
- S-adenosylmethionine synthase 1
- Aconitate hydratase 1
Sequence:
MGLPLMMERSSNNNNVELSRVAVSDTHGEDSPYFAGWKAYDENPYDESHNPSGVIQMGLAENQVSFDLLETYLEKKNPEGSMWGSKGAPGFRENALFQDYHGLKTFRQAMASFMEQIRGGKARFDPDRIVLTAGATAANELLTFILADPNDALLVPTPYYPGFDRDLRWRTGVKIVPIHCDSSNHFQITPEALESAYQTARDANIRVRGVLITNPSNPLGATVQKKVLEDLLDFCVRKNIHLVSDEIYSGSVFHASEFTSVAEIVENIDDVSVKERVHIVYSLSKDLGLPGFRVGTIYSYNDNVVRTARRMSSFTLVSSQTQHMLASMLSDEEFTEKYIRINRERLRRRYDTIVEGLKKAGIECLKGNAGLFCWMNLGFLLEKKTKDGELQLWDVILKELNLNISPGSSCHCSEVGWFRVCFANMSENTLEIALKRIHEFMDRRRRF
Protein: Galactose-1-phosphate uridylyltransferase (Gal-1-P uridylyltransferase) (EC 2.7.7.12) (UDP-glucose--hexose-1-phosphate uridylyltransferase) (P43424)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in galactose metabolism.
Interaction partners:
- Galactokinase
- UDP-glucose 4-epimerase
- UTP--glucose-1-phosphate uridylyltransferase
- N-acetylgalactosamine kinase
- Galactose mutarotase
- Beta-1,4-galactosyltransferase
- Alpha-lactalbumin
- Beta-1,4-galactosyltransferase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Sequence:
MSQSGADPEQRQQASEADAMAATFRASEHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQLLKTVPRHDPLNPLCPGATRANGEVNPPYDGTFLFDNDFPALQPDAPDPGPSDHPLFRVEAARGVCKVMCFHPWSDVTLPLMSVPEIRAVIDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASNFLPDIAQREERSQQTYHNQHGKPLLLEYGHQELLRKERLVLTSEYWIVLVPFWAVWPFQTLLLPRRHVQRLPELTPAERDDLASTMKKLLTKYDNLFETSFPYSMGWHGAPMGLKTGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRVLPEVHYCLTQKDKETAATA
Protein: SPbeta prophage-derived glycosyltransferase SunS (EC 2.4.1.-) (O31986)
Organism: Bacillus subtilis (strain 168)
Function: Transfers a hexose moiety onto 'Cys-41' of bacteriocin sublancin-168 (SunA). Accepts UDP-glucose (UDP-Glc), UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-galactose (UDP-Gal), UDP-xylose (UDP-Xyl) and GDP-mannose as substrate.
Interaction partners:
- SPbeta prophage-derived sublancin-168-processing and transport ATP-binding protein SunT
- SPbeta prophage-derived disulfide bond formation protein A
- SPbeta prophage-derived disulfide bond formation protein B
- SPbeta prophage-derived bacteriocin sublancin-168
- Sensor histidine kinase YvrG
Sequence:
MKLSDIYLELKKGYADSLLYSDLSLLVNIMEYEKDIDVMSIQSLVAGYEKSDTPTITCGIIVYNESKRIKKCLNSVKDDFNEIIVLDSYSTDDTVDIIKCDFPDVEIKYEKWKNDFSYARNKIIEYATSEWIYFIDADNLYSKENKGKIAKVARVLEFFSIDCVVSPYIEEYTGHLYSDTRRMFRLNGKVKFHGKVHEEPMNYNHSLPFNFIVNLKVYHNGYNPSENNIKSKTRRNINLTEEMLRLEPENPKWLFFFGRELHLLDKDEEAIDYLKKSINNYKKFNDQRHFIDALVLLCTLLLQRNNYVDLTLYLDILETEYPRCVDVDYFRSAILLVDMQNKLTSLSNMIDEALTDERYSAINTTKDHFKRILISLNIQLENWERVKEISGEIKNDNMKKEIKQYLANSLHNIEHVLKGIEV
Protein: Putative pectinesterase (SKU5 similar 16) (O64838)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKQKHLLLLGFLLAYCFSSVFVINAEDPYLFFTWTVTYGTRSPLGVPQQVILINGQFPGPPIEGVTNNNIVVNVINKLDEPFLITWNGIKQRKMSWQDGVLGTNCPIQPKSSWTYHFQLKDQIGTYAYFASTSMHRASGAFGALNVNQRSVIFVPYPKPDADFTLLVSDWYKMGHKELQRRLDSSRALPPPDGLLINGASKGLVFTGQHGKIYRFRISNVGISTSINFRIQGHMMTLVEVEGSHTLQEVYESLDIHVGQSVTVLVTLKAPVKDYFIVASTRFTKPILTTTGILSYQGSKIRPSHPLPIGPTYHIHWSMKQARTIRLNLTANAARPNPQGSFHYGTIPINRTFVLANGRAMINGKLRYTVNRVSYVNPATPLKLADWFNIPGVFNFKTIMNIPTPGPSILGTSVFDVALHEYVEFVFQNNEGSIQSWHLDGTSAYVVGYGSGTWNMAKRRGYNLVDAVSRHTFQVYPMSWTSILVSLDNKGMWNLRSQIWSRRYLGQELYVRVWNNEKSLYTESEPPVNVLFCGKAKHPRLI
Protein: Protein NRT1/ PTR FAMILY 2.9 (AtNPF2.9) (Nitrate transporter 1.9) (Q9M9V7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low-affinity nitrate transporter facilitating nitrate loading into root phloem. Not involved in dipeptides transport, but has a weak glucosinolate transport activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21571952}; Multi-pass membrane protein {ECO:0000269|PubMed:21571952}.
Interaction partners:
- High affinity nitrate transporter 2.7
- Chloride channel protein CLC-a
- High-affinity nitrate transporter 2.1
- Nucleobase-ascorbate transporter 4
- High affinity nitrate transporter 2.4
Sequence:
MEVEKTEKNIAEDDESKIIYRGWKVMPFIIGNETFEKLGIVGSSSNLVIYLTTVFNMKSITAAKVVNIYGGTSNFGTIVAAFLCDSYFGRYKTLSFAMIACFLGSVAMDLTAVIHPLHPAQCAKEIGSVCNGPSIGQIMFLAGAMVLLVIGAGGIRPCNLPFGADQFDPKTKEGKRGIESFFNWYFFTFTFAQMVSLTLIVYVQSNVSWSIGLAIPAILMLLGCIIFFAGSKLYVKVKASGSPIHSITRVIVVAIKKRRLKPVGPNELYNYIASDFKNSKLGHTEQFRFLDKSAIQTQDDKLNKDGSPVDAWKLCSMQQVEEVKCVIRVLPVWLSAALFYLAYIQQTTYTIFQSLQSDRRLGPGSFQIPAGSYTVFLMLGMTIFIPIYDRVLVPFLRKYTGRDGGITQLQRVGAGLFLCITSMMVSAIVEQYRRKVALTKPTLGLAPRKGAISSMSGMWLIPQLVLMGIADALAGVGQMEFYYKQFPENMRSFAGSLYYCGIGLASYLSTFLLSAVHDTTEGFSGGSWLPEDLNKGRLEYFYFLVAGMMTLNLAYFLLVSHWYRYKDVVAKDKDMDKTSAEFDKVSV
Protein: CRIB domain-containing protein RIC4 (ROP-interactive CRIB motif-containing protein 4) (Target of ROP protein RIC4) (Q9FFD5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as downstream effector of Rho-related GTP binding proteins of the 'Rho of Plants' (ROPs) family. Participates in the propagation of ROP GTPase signals in specific cellular responses. Required for actin cortical microfilament assembly. Activated by ARAC4/ROP2 to promote the assembly of cortical actin microfilaments required for lobe formation and lateral expansion of pavement cells. Interaction with, and activation by ARAC4/ROP2 is inhibited by RIC1. Functions as downstream effector of ARAC11/ROP1 to promote the assembly of apical F-actin associated with vesicle accumulation in the tip of the growing pollen tube. Counteracts the ARAC11/ROP1-RIC3 pathway, which activates calcium signaling that leads to apical F-actin disassembly associated with exocytosis, to control actin dynamics and pollen tube apical growth. Downstream of ARAC11/ROP1, is involved in the growth responses to the root-colonizing endophytic fungus P.indica.
Subcellular location: Cell membrane {ECO:0000305|PubMed:11752391, ECO:0000305|PubMed:15766531, ECO:0000305|PubMed:15824136, ECO:0000305|PubMed:21124849}; Peripheral membrane protein {ECO:0000305|PubMed:11752391, ECO:0000305|PubMed:15766531, ECO:0000305|PubMed:15824136, ECO:0000305|PubMed:21124849}.
Interaction partners:
- Rac-like GTP-binding protein ARAC11
- Rac-like GTP-binding protein ARAC4
- Rac-like GTP-binding protein ARAC5
- CRIB domain-containing protein RIC3
- Rac-like GTP-binding protein ARAC3
- Interactor of constitutive active ROPs 1
- Auxin-binding protein 1
- Pollen receptor-like kinase 2
- Rac-like GTP-binding protein ARAC1
- Interactor of constitutive active ROPs 5
Sequence:
MRDRMERLVVLPFSIGCISVSSVAVLSPLSKPHHHHSRQVIREQEEEDNMKNVFKFLAVSKPEISIGINRIFKSFKTISQLFADKDEEKEEVETSGMEIGVPTNVKHVSHIGWESGLTAATGPGKGWEDLIPPELLAAAASKKEINPHLHPTL
Protein: Alpha-2-macroglobulin receptor-associated protein (Alpha-2-MRAP) (Gp330-binding 45 kDa protein) (Low density lipoprotein receptor-related protein-associated protein 1) (RAP) (Q99068)
Organism: Rattus norvegicus (Rat)
Function: Molecular chaperone for LDL receptor-related proteins that may regulate their ligand binding activity along the secretory pathway.
Subcellular location: Rough endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P30533}. Endoplasmic reticulum-Golgi intermediate compartment lumen {ECO:0000250|UniProtKB:P30533}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:P30533}. Golgi apparatus lumen {ECO:0000250|UniProtKB:P30533}. Endosome lumen {ECO:0000250|UniProtKB:P30533}. Cell surface {ECO:0000250|UniProtKB:P30533}. Note=May be associated with receptors at the cell surface. {ECO:0000250|UniProtKB:P30533}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 2
- Prolow-density lipoprotein receptor-related protein 1
- Ral guanine nucleotide dissociation stimulator
- Low-density lipoprotein receptor-related protein
- Rap guanine nucleotide exchange factor 3
- LDL receptor related protein 5
Sequence:
MAPLRDRVSTLPRLQLLVLLLLPLLLVPQPIAGHGGKYSREKNEPEMAAKRESGEEFRMEKLNQLWEKAKRLHLSPVRLAELHSDLKIQERDELNWKKLKVEGLDGDGEKEAKLVHNLNVILARYGLDGRKDTQTVHSNALNEDTQDELGDPRLEKLWHKAKTSGKFSSEELDKLWREFLHYKEKIHEYNVLLDTLSRAEEGYENLLSPSDMTHIKSDTLASKHSELKDRLRSINQGLDRLRKVSHQGYGPATEFEEPRVIDLWDLAQSANFTEKELESFREELKHFEAKIEKHNHYQKQLEISHQKLKHVESIGDPEHISRNKEKYVLLEEKTKELGYKVKKHLQDLSSRVSRARHNEL
Protein: CLAVATA3/ESR (CLE)-related protein 22 [Cleaved into: CLE22p] (Q3E9I4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance.
Subcellular location: [CLE22p]: Secreted, extracellular space {ECO:0000250|UniProtKB:O49519}.
Interaction partners:
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- Membrane-associated kinase regulator 5
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
Sequence:
MGNYYSRRKSRKHITTVALIILLLLLFLFLYAKASSSSPNIHHHSTHGSLKKSGNLDPKLHDLDSNAASSRGSKYTNYEGGGEDVFEDGKRRVFTGPNPLHNR
Protein: Thioredoxin H1 (OsTrxh1) (Phloem sap 13 kDa protein 1) (Q0D840)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Thiol-disulfide oxidoreductase involved in the redox regulation of MAP kinases. Under reducing conditions, inhibits MPK1 and MPK5 kinase activities. Mediates its own transport from cell-to-cell through plasmodesmata. Possesses insulin disulfide bonds reducing activity.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
- Peroxiredoxin-2F, mitochondrial
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Peroxiredoxin-2C
- Thioredoxin reductase NTRB
- Peroxiredoxin-2E-1, chloroplastic
- Peroxiredoxin-2E-2, chloroplastic
Sequence:
MAAEEGVVIACHNKDEFDAQMTKAKEAGKVVIIDFTASWCGPCRFIAPVFAEYAKKFPGAVFLKVDVDELKEVAEKYNVEAMPTFLFIKDGAEADKVVGARKDDLQNTIVKHVGATAASASA