wanglab/gogpt-training-data huggingface dataset:
Protein: Ghrelin O-acyltransferase (EC 2.3.1.-) (Membrane-bound O-acyltransferase domain-containing protein 4) (B1Q005)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (By similarity). In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16) that are not efficient (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C7A3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C7A3}.
Interaction partners:
- Appetite-regulating hormone
- Growth hormone secretagogue receptor type 1
Sequence:
MDWLQFFFLHPVSLYQGAAFPFALLFNYLCITESFPTRARYLFLLAGGGVLALAAMGPYALLIFIPALCAVAMISSLSPQEVHGLTFFFQMGWQTLCHLGLHYKEYYLCEPPPVRFYITLSSLMLLTQRVTSLSLDISEGKVEAAWRGTRSRSSLCEHLWDALPYISYLLFFPALLGGSLCSFQRFQACVQRPRSLYPSISFWALTWRGLQILGLECLKVALRRVVSAGAGLDDCQRLECIYIMWSTAGLFKLTYYSHWILDDSLLHAAGFGSEAGQRPGEERYVPDVDIWTLETTHRISLFARQWNRSTAQWLKRLVFQRSRRWPVLQTFAFSAWWHGLHPGQVFGFLCWSVMVKADYLIHTFANGCIRSWPLRLLYRSLTWAHTQIIIAYVMLAVEGRSFSSLCRLCCSYNSIFPVTYCLLLFLLARRKHKCN
Protein: Monoacylglycerol lipase (MGL) (EC 3.1.1.23) (O07427)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the hydrolysis of exogenous host lipids during chronic infection (Probable). Catalyzes the hydrolysis of both monoacylglycerols (MAG) and diacylglycerols (DAG), with a preference for MAG. It hydrolyzes 2-MAG, 1-3-MAG and MAG with short, medium and long chain fatty acids such as 1-monobutyroyl-rac-glycerol (MC4), 1-mono-octanoyl-rac-glycerol (MC8), 1-monodecanoyl-rac-glycerol (MC10), 1-monolauroyl-rac-glycerol (MC12), 1-monomyristoyl-rac-glycerol (MC14) and 1-mono-oleyl-rac-glycerol (MC18:1). Also able to hydrolyze DAG with short (DiC6) and medium (DiC10) fatty acid chains, but not with longest fatty acid chains. Can also hydrolyze vinyl laurate (VC12), vinyl butyrate (VC4) and vinyl propionate (VC3).
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:17784850}. Secreted {ECO:0000305|PubMed:17784850}.
Interaction partners:
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit G
- Probable lipase/esterase LipG
- NADH-quinone oxidoreductase subunit D
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit I
- Putative quercetin 2,3-dioxygenase Rv0181c
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit B
- Uncharacterized protein
Sequence:
MTTTRTERNFAGIGDVRIVYDVWTPDTAPQAVVVLAHGLGEHARRYDHVAQRLGAAGLVTYALDHRGHGRSGGKRVLVRDISEYTADFDTLVGIATREYPGCKRIVLGHSMGGGIVFAYGVERPDNYDLMVLSAPAVAAQDLVSPVVAVAAKLLGVVVPGLPVQELDFTAISRDPEVVQAYNTDPLVHHGRVPAGIGRALLQVGETMPRRAPALTAPLLVLHGTDDRLIPIEGSRRLVECVGSADVQLKEYPGLYHEVFNEPERNQVLDDVVAWLTERL
Protein: Aromatic amino acid aminotransferase C56E4.03 (EC 2.6.1.57) (O14192)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has aromatic amino acid transaminase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Aspartate aminotransferase, mitochondrial
- Tryptophan synthase
- Putative prephenate dehydratase
- Aspartate aminotransferase, cytoplasmic
- Probable prephenate dehydrogenase [NADP
- Chorismate mutase
- L-2-aminoadipate reductase
- Homoisocitrate dehydrogenase
- Multifunctional tryptophan biosynthesis protein
- Histidinol-phosphate aminotransferase
Sequence:
MAAQPKDLSHHLSVESASRKQSPLKAVALSKSSRNIKIISLAGGLPNPEYFPIREMDAEIPAINSWKKDSSNSGKLDTVSVPMSSSDSDVLPLSVALQYGQGSGAALLSQFLKEHTRIIHNPPYEGWNIIMTTGNTSCLDIALRMLTNRGDSILVEKYSFPSALQSMRPLGLSCIPIDMDQFGFLPESMDDILTNWDATSYGSPKPHVLYTIPTGQNPTGSTLSVERRKQIYTLAQKHDIIILEDEPYYYLQMDAYEGKPEAADKAFTNEQFVKELIPSFLSMDVDGRVIRMDSLSKVVAPGSRVGWFTAQPLFIERGLRAAETATQSASGISQGILYAMFKHWGQDGYLEWLKHIRYSYTLRRNYLLYAMDTYLPKSVCSYIPPVAGMFIWFEVDKSRYIHADKNESIPEIESKIHAEAVEEGVNLACGNWFVVDPRVNDKIFFRVTFAHAELEEFNVAIERFAGVLKNNFKC
Protein: Peroxiredoxin Bcp (EC 1.11.1.24) (Bacterioferritin comigratory protein) (Thioredoxin peroxidase) (Thioredoxin-dependent peroxiredoxin Bcp) (P0AE52)
Organism: Escherichia coli (strain K12)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Interaction partners:
- Glycine cleavage system transcriptional repressor
- Alkyl hydroperoxide reductase C
- Thioredoxin reductase
- Peptide methionine sulfoxide reductase MsrA
- Thioredoxin/glutathione peroxidase BtuE
- Alkyl hydroperoxide reductase subunit F
Sequence:
MNPLKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVDVLGISTDKPEKLSRFAEKELLNFTLLSDEDHQVCEQFGVWGEKSFMGKTYDGIHRISFLIDADGKIEHVFDDFKTSNHHDVVLNWLKEHA
Protein: Uncharacterized protein C17A2.11, mitochondrial (O13761)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVCPSPLRECHPFLQRSFFPSFALSHRDIISTRACLNDNSPAFDRRYHWVWEEDRRCLNLGKTLASTIHHKGGNLSLQWQRGNTTTHIATRWDANKLLLARAILKEKRNILQDKTSVNVNVNKLIPIPKKKVLKNRAKSLLSIKSHVHFHLIPFINFFLLYHQIILSHSLFHISHLISFHFLFFSFLSFPLLSFILFPCFSLFLSSNSFSLASPFSS
Protein: Band 7 domain-containing protein (H2KZ92)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MKPRETVATTSGTDSTPKTTILPAKKDYFHVEANIQNEFGVCGWILTILSYLLIFFTLPISACMCIKVVQEYERAVIFRLGRLMPGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAAREARAKVIVAEGEQKASRALKEAAEVIAESPSALQLRYLQTLNSISAEKNSTIIFPFPIDLLSAFLQRTPPKVDNNFAFPTHKAGGIPSSS
Protein: Calcium/manganese antiporter SLC30A10 (Solute carrier family 30 member 10) (Q3UVU3)
Organism: Mus musculus (Mouse)
Function: Plays a pivotal role in manganese transport. Manganese is an essential cation for the function of several enzymes, including some crucially important for the metabolism of neurotransmitters and other neuronal metabolic pathways. However, elevated levels of manganese are cytotoxic and induce oxidative stress, mitochondrial dysfunction and apoptosis. Acts as manganese efflux transporter and confers protection against manganese-induced cell death. Also acts as zinc transporter involved in zinc homeostasis. Seems to mediate zinc transport into early endosomes and recycling endosomes to prevent zinc toxicity; the function may be regulated by heterodimerization with other zinc transporters of the SLC30A subfamily. The SLC30A3:SLC30A10 heterodimer is involved in zinc transport-dependent regulation of the EGFR/ERK transduction pathway in endosomes. May be involved in regulation of zinc-dependent senescence of vascular smooth muscle cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6XR72}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6XR72}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q6XR72}. Early endosome membrane {ECO:0000250|UniProtKB:Q6XR72}; Multi-pass membrane protein {ECO:0000255}. Note=Localization to the Golgi and plasma membrane is regulated by zinc. {ECO:0000250|UniProtKB:Q6XR72}.
Interaction partners:
- Metal cation symporter ZIP14
- Metal cation symporter ZIP8
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Zinc transporter 6
- Zinc transporter ZIP1
- Zinc transporter ZIP13
- Zinc transporter ZIP5
Sequence:
MGRYSGKTCRLLFMLVLTAAFFVAELVSGYLGNSIALLSDSFNMLSDLISLCVGLGSGYIARRGPRGSSATYGYVRAEVVGALSNAVFLTALCFTIFVEAVLRLARPERIDDPELVLIVGALGLAVNVVGLLIFQDCGACFSRCTRGRRTRPSQQPSQGDPRGALGCPQEAATATAPGSGTAVTLRGSSAGRKQQEGATVFSNVAGDSLNTENEPEETTKKEKKSEALNIRGVLLHVMGDALGSVVVVITAIIFYVQPLRREDPCNWQCYIDPSLTVVMVIIILSSAFPLIKETAVILLQMVPKGVNMEELMSQLSTVPGISSVHEVHIWELISGKIIATLHIKHQKGTEYQDASRKIREIFHHAGIHNVTIQFETLDLKEALEQKDFLLTCSAPCITQSCAKKLCCPPGTLPLALVNGCAEHNGRSSRESYRSIEAPEVAIDVDGCPREQGQTLSKTQERQHYENSTHF
Protein: Ankyrin 1 (A0A8I5ZQ60)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MWTFITQLLVTLVLLGFFLVSCQNVMHIVKGSLCFVLKHIHQELDKELGESGGLSDDEETISTRVVRRRVFLKGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVIVEGPLADPGDLEADIESFMKLTKVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ
Protein: MNDA protein (Q05CU9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVNEYKKILLLKGFELMDDYHFTSIKSLLAYDLGLTTKMQEEYNRIKITDLMEKKFQGVACLDKLIELAKDMPSLKNLVNNLRKEKSKVAKKIKTQEKAPVKKINQEEVGLAAPAPTARNKLTSEARGRIPVAQKRKTPNKEKTEAKRNKVSQEQSKPPGPSGASTSAAVDHPPLPQTSSSTPSNTSFTPNQETQAQRQVDARRNVPQNDPVTVVVLKATAPFKYESPENGKSTMFHATVASKTQYFHVKVFDINLKEKFVRKKVITISDYSECKGVMEIKEASSVSDFNQNFEVPNRIIEKKKKKKKKK
Protein: Ras-related protein RABA4d (AtRABA4d) (Q9LH50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular vesicle trafficking and protein transport. Plays an important role in the regulation of pollen tube tip growth.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000305|PubMed:19208902}; Lipid-anchor {ECO:0000305|PubMed:19208902}. Note=Associated with membrane compartments that localize to the tips of growing pollen tubes.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta 1
- Rho GTPase-activating protein REN1
- Geranylgeranyl transferase type-2 subunit beta 2
- Kinesin-like protein KIN-14E
- CRIB domain-containing protein RIC3
- Myosin-11
- Rop guanine nucleotide exchange factor 12
- Protein RALF-like 15
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Rho GTPase-activating protein 7
Sequence:
MSNLYGDYNQKIDYVFKVVLIGDSAVGKTQLLARFARNEFSVDSKATIGVEFQTKTLVIDNKTVKAQIWDTAGQERYRAVTSAYYRGAVGAMLVYDMTKRQSFDHMAKWLEELRGHADKNIVIMLIGNKCDLGSLRAVPTEDAQEFAQRENLFFMETSALEATNVETAFLTILTEIYRIISKKSLTADDDDADGNSSLLKGTRIIIPSEQESGKRGGCCGKS
Protein: GrpE like 2, mitochondrial (D6RGI6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAVRSLWAGRLRVQRLLAWSAAWESKGWPLPFSTATQRTAGEDCRSEDPPDELGPPLAERALRVKAVKLEKEVQDLTVRYQRAIADCENIRRRTQRCVEDAKIFGERFIYNKNVFGWAQWLMPVIPAL
Protein: Ankyrin repeat-containing protein 06_02 (Ankyrin repeat-containing protein 06_03) (Ankyrin repeat-containing protein 06_04) (B3CTB0)
Organism: Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi)
Interaction partners:
Sequence:
MYKVLPLRARLLYATARNIFSTQNRHILPYIAYKGDIELLQHLIDHGIDVNTTNHWDNTALHVASYHGNIAMVNLLLDNNANPNLQDANLHTPLHFAISNGHIDIVRLLLNHESDVNLISKFNETALDVAWIKYTENLEQSYLATVRLLITHIVRIEHANLVDTSSQGFLHNKGLINESEQLKELEQQCHKEIEEMCSISVGSSSCLSFFDIFVLKKDMNILARCANNPDIVRHQNKFSMYSPFIEKSIEEGEKRAKLLQGAVESIDEIFESNQDASQKSQTSWSHLPPEVRFMILENLDNDDLTKIQRTDVAEAGEAGAEVEAEVGGAHAIYEEE
Protein: tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (Q8IDW3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Tryptophan--tRNA ligase
- Alanine--tRNA ligase
- indole-3-glycerol-phosphate synthase
- Proline--tRNA ligase
- tyrosine--tRNA ligase
- arginine--tRNA ligase
- leucine--tRNA ligase
- leucine--tRNA ligase
- tRNA import protein tRIP
- Tyrosine--tRNA ligase
Sequence:
MDKLKTIYLDSALSIIKGALCIILQIPTSRTTESVKKKANNVGVITVKSILSEPTIHQYDDIKKLIKNKLQECVPFYNYNMNRSFAEKIYGDCIYDNYGLSKEINEINLIILEEWNINCNKNRVLKNTGLIKEITINQFKYSTNKESLEVHFAVSPKYTFEELSTMYKNEKGLYEFLLSPIIKIICNENDKKLLDNMNEECTYLNAEDILPKNKVLPPSGIENIDYERSKDVTPWDVNINNEEGINYNKLIKEFGCSKITENHIKRIEKLTNSKAHHFIRRGIFFSHRDLDFLLNYYEQHKCFYIYTGRGPSSLSMHLGHLIPFYFCKYLQEAFNVPLVIQLSDDEKYLFNQNYSLEYINTLTNENVKDIISVGLNPELTFIFKNTEYAGYLYPTVLSIHKKTTLNQSMNVFGFNHSDNIGKISYPSFQIAPCFSQCFPNFLGKNIPCLVPQGIDQDPYFRLSRDIAVKMALHKPVVVHSVFMPGLQGVNSKMSSTKKKKDDNGKSNSTFDHNNSVIFLTDTPEQIKNKINKYAFSGGGTTIQEHREKGGNLDKDISYQYLRYLLEDDNKLNEIGEKYKKGEMLSGEIKKILIDVLTELVLKHQEKKKSLTDEEISYFFDPNKPSLQKFKNM
Protein: Ectonucleoside triphosphate diphosphohydrolase 1 (EC 3.6.1.5) (ATP diphosphohydrolase) (ATP-DPH) (ATPDase) (Ecto-ATP diphosphohydrolase 1) (Ecto-ATPDase 1) (Ecto-ATPase 1) (Ecto-apyrase) (Lymphoid cell activation antigen) (Nucleoside triphosphate diphosphohydrolase 1) (NTPDase1) (CD antigen CD39) (P49961)
Organism: Homo sapiens (Human)
Function: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.
Subcellular location: Membrane {ECO:0000269|PubMed:10636909, ECO:0000269|PubMed:8955160}; Multi-pass membrane protein {ECO:0000269|PubMed:10636909}. Membrane, caveola {ECO:0000269|PubMed:10636909}.
Interaction partners:
- 5'-nucleotidase
- Adenosine kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleoside triphosphate diphosphohydrolase 6
- Nucleoside diphosphate phosphatase ENTPD5
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleoside triphosphate diphosphohydrolase 2
- P2Y purinoceptor 2
- Ectonucleoside triphosphate diphosphohydrolase 4
- Cancer-related nucleoside-triphosphatase
Sequence:
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTPCTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAFSAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYILSLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFLMVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Protein: Claudin-7-B (Claudin-like protein ZF4A22) (Q9YH92)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space.
Subcellular location: Cell junction, tight junction {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Claudin b
- Claudin
- Claudin
- Tight junction protein 1a
- Tight junction protein 3
- Claudin a.
- Claudin
- Claudin
- Claudin
- Claudin
Sequence:
MAHKGLQLLGFTLSLLGLIGLIIGTIMPQWKMSAYVGDNIITAIAMYQGLWMSCAYQSTGQQQCKVYDSVLQLDSALQATRALMVVAILLTVAGLGVASMGMKCTNCGGDDKVKKSRIAMTGGIILSVGALCSIVACGWFTSQIIRDFYNPFTPVNTKYEFGAAIFIAWAGAFLDIMGGGMLASSCSKGQSSPNYPKSSRPVKSSRPPSSSKEYV
Protein: TraR protein (G0KUD5)
Organism: Streptomyces flavovirens
Interaction partners:
Sequence:
MPYKAPEGKGYADVATHFRTLIKSGELAPGDTLPSVADIRAQFGVAAKTVSRALAVLKSEGLVSSRGALGTVVEKNPIVITGADRLKRMEKNGMRYAPGETSSGHRVMTRSVHDPEICTALTLEPGDEAVIRIRVFRQDDKPTSVGVSVYPPHTVAAVPELGEDVRMVKQFDKLYSERTGREVVKGQRAAHARQASQDELNALRSTPPAHSAIAVMVTTVTFHDDEQALGYWEDVYAPGARVPMGE
Protein: Anon1A3 (Q9U4R0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GVENLPSVAEAKQNHVDEVKPISEEPGNSSEEVPKAEEPLKSSGETSENGAATETAAAPKEPASVMDVDEDETLVENTPSANKEKALDDEKEPEQKSEEHAAAVLESKGQNEPAKEPTPEPMEVDGSSKGSSDTAQVDTPAIENVSAAPETEAAAKTTESSNDVVEVATEGKETVLEVPAAEPKEAESTVESAEELTETSTVVVTEPKEAASSEEEPSKVVDSAEPKEAESNTDESATPVPIDVSTAPASNDVSKPLEIDTTLVKTADSPAKEPQEICEVKKAEINVNGEPKIVNSSAEVGENAAPKVCN
Protein: Ceramide synthase 2 (CerS2) (LAG1 longevity assurance homolog 2) (Sphingosine N-acyltransferase CERS2) (EC 2.3.1.24) (Translocating chain-associating membrane protein homolog 3) (TRAM homolog 3) (Tumor metastasis-suppressor gene 1 protein) (Very-long-chain ceramide synthase CERS2) (EC 2.3.1.297) (Q924Z4)
Organism: Mus musculus (Mouse)
Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward very-long-chain fatty acyl-CoA (chain length C22-C27). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively. Plays a non-redundant role in the synthesis of ceramides with very-long-chain fatty acids in kidney, liver and brain. Regulates the abundance of myelin-specific sphingolipids galactosylceramide and sulfatide that affects myelin sheath architecture and motor neuron functions.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15823095}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Acid ceramidase
- Sphingolipid delta
- 3-ketodihydrosphingosine reductase
- Ceramide glucosyltransferase
- Sphingomyelin phosphodiesterase 2
- Sphingomyelin phosphodiesterase
- Ceramide kinase
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Alkaline ceramidase 3
- Neutral ceramidase
Sequence:
MLQTLYDYFWWERLWLPVNLTWADLEDKDGRVYAKASDLYITLPLALLFLVIRYFFELYVATPLAALLNVKEKTRLRAPPNATLEHFYQTSGKQPKQVEVDLLSRQSGLSGRQVERWFRRRRNQDRPSLLKKFREASWRFTYYLIAFVAGMAVTVDKPWFYDLRKVWEGYPIQSIIPSQYWYYMIELSFYWSLLFSIASDVKRKDFKEQIIHHVATIILLCFSWFANYVRAGTLIMALHDASDYLLESAKMFNYAGWKNTCNNLFIVFAIVFIITRLVIMPFWILHCTMIYPLELYPAFFGYYFFNFMMAVLQMLHIFWAYFILRMAHKFITGKLIEDERSDREETESSEGEETAAGAGAKSRLLANGHPILNNNHPKND
Protein: Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase) (O55098)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNDVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYYDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHGKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVLCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLQHPFVSRVTSNKALRELVAEAKAEVMEEIEDGREDGEEEDAVDAVPPLVNHTQDSANVTQPSLDSNKLLQDSSTPLPPSQPQEPVSGSCSQPSGDGPLQTTSPADGLSKNDNDLKVPVPLRKSRPLSMDARIQMDEEKQIPDQDENPSPAASKSQKANQSRPNSSALETLGGEALTNGGLELPSSVTPSHSKRASDCSNLSTSESMDYGTSLSADLSLNKETGSLSLKGSKLHNKTLKRTRRFVVDGVEVSITTSKIISEDEKKDEEMRFLRRQELRELRLLQKEEHRNQTQLSSKHELQLEQMHKRFEQEINAKKKFYDVELENLERQQKQQVEKMEQDHSVRRKEEAKRIRLEQDRDYAKFQEQLKQMKKEVKSEVEKLPRQQRKESMKQKMEEHSQKKQRLDRDFVAKQKEDLELAMRKLTTENRREICDKERDCLSKKQELLRDREAALWEMEEHQLQERHQLVKQQLKDQYFLQRHDLLRKHEKEREQMQRYNQRMMEQLKVRQQQEKARLPKIQRSDGKTRMAMYKKSLHINGAGSASEQREKIKQFSQQEEKRQKAERLQQQQKHENQMRDMVAQCESNMSELQQLQNEKCHLLVEHETQKLKALDESHNQSLKEWRDKLRPRKKALEEDLNQKKREQEMFFKLSEEAEPRPTTPSKASNFFPYSSGDAS
Protein: Centaurin beta 1A (MIP17913p) (Q9VCQ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD21953p
- Glyoxylate reductase/hydroxypyruvate reductase
Sequence:
MRATIEFEECLKDSPRFRQFVSKEESDIEHLEQRLEKIIKLCNVAVDSGKEYVKNQSAFAMSLWDLQQHFLDNKNAHNALGKLIHCFQEMNKFHTILLDQASRTVLKNLSVFVKDDINQVKDYKGHFLKVSEGYDNALIKNAQASKNRPQEMQEAANILSASKSCFQHTALDYVNYITLAQARKVPSILSTLLDYYQACVTYYHQGFDLCNDFDEFFKNISEDLNALRGDYQQLEKAMQNRHMSVNRYCDSNTNSTSNKIEGYLFKKKSKGFKTWCRRWFYLSDNQLVYRKRSNEDSFSVMEEDLRICSVRPVNEGDRRFCFEVISPTKSHILQADSADMLSLWISALQHSIGAAIQHDSTHHSRPQSTNAPNNSLPAKRRIHWEEFLKIPGNAYCCDCRSPEPRWASINLGITLCIECSGVHRSLGVHYSKVRSLTLDAWESENVKVMMELGNEVVNRIYEARIGDDCGLKKPTEQCEIGVREAWIKAKYVERRFVCGMPKPQELLASETAEVLSIDSGGVVEDGESGGSGIAKRATLSLGGTRKWAVKKLRRRQKQRSIPKTLSDDPSIYNTAKTGDELEDDDDDESINIPSMSLSISRDDLLVIGDDLALDRLETPGILGSDQESTDGESDAESPEELPFSQLDANQLLYMASVVHNLPVMCMAFALGADKMWKNPQDRQRSFLHQAVISGSVMACEFLLLNGAAIDAVDEMGYSALHISTAKGHIAQVYLLLKHKAAYDLSSSDGKKALDIAVDQENADIVTLLRLTQLNDEIGPNDEYNGEDETYKNVMKDFSKLPASQTRVLRQRHDSNTLESQRSSLTNSD
Protein: Anoctamin (D4A915)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU280814}.
Interaction partners:
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Calmodulin-1
- Cystic fibrosis transmembrane conductance regulator
- Bestrophin
- Chloride channel accessory 5
- Bestrophin
- Bestrophin
- Bestrophin
- Solute carrier family 26 member 9
Sequence:
MQDTQDSDISLEGLTREGAPADRECQRGPETIVHEAQDAGTPNSGDATGAVDGEREATMRVPEKYSTLPAEDRSVHIVNICAIEDLGYLPSEGTLLNSLSVDPDAECKYGLYFRDGKRKVDYILVYHHKRASGSRTLARRGLQNDMVLGTRSVRQDQPLPGKGSPVDVGSPEAPMDYHEDDKRFRREEYEGNLLEAGLELERDEDTKIHGVGFVKIHAPWHVLCREAEFLKLKMPTKKVYHISETRGLLKTINSVLQKITDPIQPKVAEHRPQTTKRLSYPFSREKQHLFDLTDRDSFFDSKTRSTIVYEILKRTTCTKAKYSMGQGEGRRKDSALLSKRRKCGKYGITSLLANGVYSAAYPLHDGDYEGDNVEFNDRKLLYEEWASYGVFYKYQPIDLVRKYFGEKVGLYFAWLGAYTQMLIPASIVGVIVFLYGCATVDENIPSMEMCDQRHNITMCPLCDKTCSYWKMSSACATARASHLFDNPATVFFSVFMALWAATFMEHWKRKQMRLNYRWDLTGFEEEEVSSCDHPRAEYEARVLEKSLRKESRNKETDKVKLTWRDRFPAYFTNLVSIIFMIAVTFAIVLGVIIYRISTAAALAMNSSPSVRSNIRVTVTATAVIINLVVIILLDEVYGCIARWLTKIEVPKTEKSFEERLTFKAFLLKFVNSYTPIFYVAFFKGRFVGRPGDYVYIFRSFRMEECAPGGCLMELCIQLSIIMLGKQLIQNNLFEIGIPKMKKFIRYLKLRRQSPSDREEYIKRKQRYEVDFNLEPFAGLTPEYMEMIIQFGFVTLFVASFPLAPLFALLNNIIEIRLDAKKFVTELRRPVAIRAKDIGIWYNILRGVGKLAVIINAFVISFTSDFIPRLVYLYMYSQNGTMHGFVNHTLSSFNVSDFQNGTAPNDPLDLGYEVQICRYKDYREPPWSEHKYDISKDFWAVLAARLAFVIVFQNLVMFMSDFVDWVIPDIPKDISQQIHKEKVLMVELFMREEQGKQQLLDTWMEKEKPRDVPCNNHSPTAHPEAGDSSPVPSYEYHGGAL
Protein: Collectin-12 (Collectin placenta protein 1) (CL-P1) (Scavenger receptor with C-type lectin) (Q8K4Q8)
Organism: Mus musculus (Mouse)
Function: Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells (By similarity). Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells (By similarity).
Subcellular location: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Forms clusters on the cell surface. {ECO:0000250}.
Interaction partners:
Sequence:
MKDDFAEEEEVQSFGYKRFGIQEGTQCTKCKNNWALKFSIVLLYILCALLTITVAILGYKVVEKMDNVTDGMETSHQTYDNKLTAVESDLKKLGDQAGKKALSTNSELSTFRSDILDLRQQLQEITEKTSKNKDTLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQSQMYSQSVVIMNLNNLNLTQVQQRNLISNLQQSVDDTSLAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLSSFTGQMDNITTISQANEQSLKDLQDLHKDTENRTAVKFSQLEERFQVFETDIVNIISNISYTAHHLRTLTSNLNDVRTTCTDTLTRHTDDLTSLNNTLVNIRLDSISLRMQQDMMRSKLDTEVANLSVVMEEMKLVDSKHGQLIKNFTILQGPPGPRGPKGDRGSQGPPGPTGNKGQKGEKGEPGPPGPAGERGTIGPVGPPGERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPPGPPGKDGLPGPQGPPGFQGLQGTVGEPGVPGPRGLPGLPGVPGMPGPKGPPGPPGPSGAMEPLALQNEPTPASEVNGCPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTVGRESHWIGLTDSEQESEWKWLDGSPVDYKNWKAGQPDNWGSGHGPGEDCAGLIYAGQWNDFQCDEINNFICEKEREAVPSSIL
Protein: Kallikrein c (Kallikrein related-peptidase 5) (Q9D140)
Organism: Mus musculus (Mouse)
Interaction partners:
- Serine peptidase inhibitor, Kazal type 5
- Serine protease inhibitor Kazal-type 6
- Kallikrein-8
- Chymotrypsin-like elastase family member 2A
- Filaggrin
- Suppressor of tumorigenicity 14 protein homolog
Sequence:
MARTGHPWKWAMATLITTLVLGVSEPVLAGDVSSCDNPSGTEPSGTNRDLSTDSKSGEDTRSDSSSRIVNGSDCQKDAQPWQGALLLGPNKLYCGAVLISPQWLLTAAHCRKPVFRIRLGHHSMSPVYESGQQMFQGIKSIPHPGYSHPGHSNDLMLIKMNRKIRDSHSVKPVEIACDCATEGTRCMVSGWGTTSSSHNNFPKVLQCLNITVLSEERCKNSYPGQIDKTMFCAGDEEGRDSCQGDSGGPVVCNGKLQGLVSWGDFPCAQRNRPGVYTNLCEFVKWIKDTMNSN
Protein: APETALA2 (E7EAV8)
Organism: Brassica napus (Rape)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MWDLNDAPHQTVRQEESEEFCYSSPGKRVGSFSNSSSSAVVIEDGSDDDEPNRVRANNPLITHQFFPEMESSVGDNGGGGPGSSFPRSHWFGVQFSQSDLATGSSVGKPATVGAVVEPAQPLKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADIDFNIEDYDNDMKQMTNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEVEAARAYDKAAIKCNGKDAVTNFDSSIYDEELNAESSGNPIQHDHNLDLSLGNSVNSKHNGQDMRLKMNQQDSLHSNEILGLGPGMVNYIPDSVHQFPGSSNIHGGGGFSLFPVTENHQFEGRTTANQVLANAAASSGFSPHNHHQIFNSTPTSHQNWLQTNGFQPPLMRPS