wanglab/gogpt-training-data huggingface dataset:
Protein: Odorant receptor 45a (Q9V568)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to hexanol, pentyl acetate, benzyl acetate, and 2-heptanone.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 74a
- Odorant receptor 30a
- Odorant receptor 59a
- Odorant receptor 67b
- Odorant receptor 33b
- Odorant receptor 83a
- Odorant receptor 24a
Sequence:
MDASYFAVQRRALEIVGFDPSTPQLSLKHPIWAGILILSLISHNWPMVVYALQDLSDLTRLTDNFAVFMQGSQSTFKFLVMMAKRRRIGSLIHRLHKLNQAASATPNHLEKIERENQLDRYVARSFRNAAYGVICASAIAPMLLGLWGYVETGVFTPTTPMEFNFWLDERKPHFYWPIYVWGVLGVAAAAWLAIATDTLFSWLTHNVVIQFQLLELVLEEKDLNGGDSRLTGFVSRHRIALDLAKELSSIFGEIVFVKYMLSYLQLCMLAFRFSRSGWSAQVPFRATFLVAIIIQLSSYCYGGEYIKQQSLAIAQAVYGQINWPEMTPKKRRLWQMVIMRAQRPAKIFGFMFVVDLPLLLWVIRTAGSFLAMLRTFER
Protein: Ferric uptake regulation protein (B8CQZ2)
Organism: Shewanella piezotolerans (strain WP3 / JCM 13877)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364037}.
Interaction partners:
- Transcriptional regulator, putative
- DNA-directed RNA polymerase subunit alpha
- Thioredoxin
- Alkyl hydroperoxide reductase C
- Thioredoxin peroxidase
- RNA polymerase sigma factor RpoH
- RNA polymerase sigma factor RpoD
Sequence:
MTDGNQALKKAGLKVTLPRVKILELMQGPENQHISAEDLYKKLLDLGEEIGLATVYRVLNQFDDAGIVTRHHFESGKAVFELATQHHHDHLVCLSCGKVFEFSDDMIEQRQDEIAMKHNIKLTNHSLYLYGVCTNDNCEHGEP
Protein: Basic phospholipase A2 BmjeTX-I (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (P86803)
Organism: Bothrops marajoensis (Marajo lancehead)
Function: Snake venom phospholipase A2 (PLA2) that induces a slight blockade of neuromuscular contraction in an indirectly stimulated chick biventer cervicis nerve-muscle preparation. Does not inhibit contraction of chick biventer cervicic nerve-muscle preparation in response to treatment with acetylcholine or KCl. The neuromuscular blockade is mediated by inhibitory action at the presynaptic motor nerve endings. Lyses skeletal myoblasts and myotubes in vitro, and intramuscular injection causes local muscle necrosis. Induces edema in the mouse foot pad. Induces a transient increase of IL-6 levels. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:20195718}.
Interaction partners:
Sequence:
DLWQFGQMILKETGKIPFPYYGAYGCYCGWGGRGGKPKAGTDRCCYVHDCCYGKLTSCPKTDDRYSYSWLDGTIVCGEDDPCKELCECDKKIAVCFRENLGTYNKKYRYHLKSCKKADKPC
Protein: Ceramide synthase 6 (CerS6) (EC 2.3.1.-) (LAG1 longevity assurance homolog 6) (Sphingoid base N-palmitoyltransferase CERS6) (EC 2.3.1.291) (Q8C172)
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 palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA). Can use other acyl donors, but with less efficiency. N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively. Ceramides generated by CERS6 play a role in inflammatory response. Acts as a regulator of metabolism and hepatic lipid accumulation. Under high fat diet, palmitoyl- (C16:0-) ceramides generated by CERS6 specifically bind the mitochondrial fission factor MFF, thereby promoting mitochondrial fragmentation and contributing to the development of obesity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15823095}; Multi-pass membrane protein {ECO:0000269|PubMed:15823095}.
Interaction partners:
- Acid ceramidase
- Alkaline ceramidase 2
- Sphingomyelin phosphodiesterase 2
- Neutral ceramidase
- Ceramide kinase
- Alkaline ceramidase 1
- Sphingomyelin phosphodiesterase
- Ceramide glucosyltransferase
- Alkaline ceramidase 3
- 3-ketodihydrosphingosine reductase
Sequence:
MAGILAWFWNERFWLPHNVTWADLKNTEEATFPQAEDLYLAFPLAFCIFMVRLIFERFIAKPCAIALNIQANGPQTAQPNAILEKVFTAITKHPDEKRLEGLSKQLDWDVRSIQRWFRQRRNQEKPSTLTRFCESMWRFSFYLYVFSYGVRFLKQTPWLWNTRHCWYNYPYQPLTADLHYYYILELSFYWSLMVSQFTDIKRKDFGIMFLHHLATIFLITFSYVNNMARVGTLVLCLHDSADALLEAAKMANYAKFQKMCDLLFVMFAVVFITTRLGIFPLWVLNTTLFESWEIVGPYPSWWVFNLLLLLLQGLNCFWSYLIVKIACKTVSKGKVSKDDRSDIESSSDDEDSEPPGKKPHSSTTTNGTSGTNGYLLTGPCSVDD
Protein: Sodium/hydrogen exchanger (A0A1B0GV11)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
Sequence:
MDEEIVSEKQAEESHRQDSANLLIFILLLTLTILTIWLFKHRRARFLHETGLAMIYGLLVGLVLRYGIHVPSDVNNVTLSCEVQSSPTTLLVTFDPEVFFNILLPPIIFYAGYSLKRRHFFRNLGSILAYAFLGTAISCFVIGSIMYGCVTLMKVTGQLAGDFYFTDCLLFGAIVSATDPVTVLAIFHELQVDVELYALLFGESVLNDAVAIVLSSSIVAYQPAGDNSHTFDVTAMFKSIGIFLGIFSGSFAMGAATGVVTALVTKFTKLREFQLLETGLFFLMSWSTFLLAEAWGFTGVVAVLFCGITQAHYTYNNLSTESQHRTKQLFELLNFLAENFIFSYMGLTLFTFQNHVFNPTFVVGAFVAIFLGRAANIYPLSLLLNLGRRSKIGSNFQHMMMFAGLRGAMAFALAIRDTATYARQMMFSTTLLIVFFTVWVFGGGTTAMLSCLHIRVGVDSDQEHLGVPENERRTTKAESAWLFRMWYNFDHNYLKPLLTHSGPPLTTTLPACCGPIARCLTSPQAYENQEQLKDDDSDLILNDGDISLTYGDSTVNTEPATSSAPRRFMGNSSEDALDRELAFGDHELVIRGTRLVLPMDDSEPPLNLLDNTRHGPA
Protein: Diphosphoinositol polyphosphate phosphohydrolase 3-alpha (DIPP-3-alpha) (DIPP3-alpha) (hDIPP3alpha) (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha) (Diadenosine hexaphosphate hydrolase (AMP-forming)) (EC 3.6.1.60) (Nucleoside diphosphate-linked moiety X motif 10) (Nudix motif 10) (hAps2) (Q8NFP7)
Organism: Homo sapiens (Human)
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:12121577}.
Interaction partners:
- Autoimmune regulator
- Torsin-1A
- Tumor necrosis factor receptor superfamily member 25
- Diphosphoinositol polyphosphate phosphohydrolase 3-beta
Sequence:
MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGVFEQNQDPKHRTYVYVLTVTELLEDWEDSVSIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSMAPSSPDSDP
Protein: Fatty acid-binding protein 5 (Epidermal-type fatty acid-binding protein) (E-FABP) (Fatty acid-binding protein, epidermal) (Psoriasis-associated fatty acid-binding protein homolog) (PA-FABP) (Q01469)
Organism: Homo sapiens (Human)
Function: Intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids, that regulate the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors. Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (By similarity). May be involved in keratinocyte differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24692551, ECO:0000269|PubMed:8092987}. Nucleus {ECO:0000269|PubMed:24692551}. Synapse {ECO:0000250|UniProtKB:Q05816}. Postsynaptic density {ECO:0000250|UniProtKB:Q05816}. Secreted {ECO:0000250|UniProtKB:Q05816}. Note=Localizes primarily to the cytoplasm. Upon certain ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into nucleus (PubMed:24692551). Secreted by astrocytes, but not by neurons (By similarity). {ECO:0000250|UniProtKB:Q05816, ECO:0000269|PubMed:24692551}.
Interaction partners:
- Peroxisome proliferator-activated receptor delta
- Aspartate aminotransferase, mitochondrial
- Fatty-acid amide hydrolase 1
- Protein S100-A7
- Peroxisome proliferator-activated receptor gamma
- Platelet glycoprotein 4
- Fatty acid-binding protein, adipocyte
- Scavenger receptor class B member 1
- Lysosome membrane protein 2
- Hormone-sensitive lipase
Sequence:
MATVQQLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCNFTDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNVTCTRIYEKVE
Protein: C-C motif chemokine 18 (Alternative macrophage activation-associated CC chemokine 1) (AMAC-1) (CC chemokine PARC) (Dendritic cell chemokine 1) (DC-CK1) (Macrophage inflammatory protein 4) (MIP-4) (Pulmonary and activation-regulated chemokine) (Small-inducible cytokine A18) [Cleaved into: CCL18(1-68); CCL18(3-69); CCL18(4-69)] (P55774)
Organism: Homo sapiens (Human)
Function: Chemotactic factor that attracts lymphocytes but not monocytes or granulocytes. May be involved in B-cell migration into B-cell follicles in lymph nodes. Attracts naive T-lymphocytes toward dendritic cells and activated macrophages in lymph nodes, has chemotactic activity for naive T-cells, CD4+ and CD8+ T-cells and thus may play a role in both humoral and cell-mediated immunity responses.
Subcellular location: Secreted.
Interaction partners:
- Eotaxin
- C-C chemokine receptor type 8
- Membrane-associated phosphatidylinositol transfer protein 3
- C-C chemokine receptor type 1
- C-C chemokine receptor type 5
- C-X-C chemokine receptor type 5
- C-C chemokine receptor type 7
- C-C chemokine receptor type 6
- Interleukin-8
- C-C chemokine receptor type 2
Sequence:
MKGLAAALLVLVCTMALCSCAQVGTNKELCCLVYTSWQIPQKFIVDYSETSPQCPKPGVILLTKRGRQICADPNKKWVQKYISDLKLNA
Protein: Glycolate oxidase subunit GlcE (EC 1.1.99.14) (Glycolate dehydrogenase subunit GlcE) (P52073)
Organism: Escherichia coli (strain K12)
Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is required for E.coli to grow on glycolate as a sole source of carbon. Is also able to oxidize D-lactate ((R)-lactate) with a similar rate. Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:2689218}. Note=Glycolate oxidoreductase activity was shown to be firmly associated with the cytoplasmic membranes. {ECO:0000269|PubMed:2689218}.
Interaction partners:
- Glycolate oxidase subunit GlcD
- Glycolate oxidase iron-sulfur subunit
- Malate synthase G
- Protein GlcG
- Glyoxylate carboligase
- Glyoxylate/hydroxypyruvate reductase B
- Malate synthase A
- Catalase HPII
- Isocitrate lyase
- Phosphoglycolate phosphatase
Sequence:
MLRECDYSQALLEQVNQAISDKTPLVIQGSNSKAFLGRPVTGQTLDVRCHRGIVNYDPTELVITARVGTPLVTIEAALESAGQMLPCEPPHYGEEATWGGMVACGLAGPRRPWSGSVRDFVLGTRIITGAGKHLRFGGEVMKNVAGYDLSRLMVGSYGCLGVLTEISMKVLPRPRASLSLRREISLQEAMSEIAEWQLQPLPISGLCYFDNALWIRLEGGEGSVKAARELLGGEEVAGQFWQQLREQQLPFFSLPGTLWRISLPSDAPMMDLPGEQLIDWGGALRWLKSTAEDNQIHRIARNAGGHATRFSAGDGGFAPLSAPLFRYHQQLKQQLDPCGVFNPGRMYAEL
Protein: 2-component receiver domain protein (Q92RV2)
Organism: Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Interaction partners:
Sequence:
MPLSTRIAPHLPYLRRYARAVTGSQAAGDAYVAAVLEALIDDLELFPAASNDRIGLYKLFCSLFEKLKIDRTQLASPFAWEQRAASNLSLIAPPQRQAFLLVALEGFSTGEAAEIMGLDQGAFGKLLTSASEEISRQIATDVMIIEDEPLIALDIEDMVTSLGHRVTGIARTRREALNLYHQTSPKMVLADIQLADGSSGIDAVNDILTQAAVPVIFITAFPERLLTGKKPEPAFLVTKPFNPETVKALISQALFFDEHAQAGAS
Protein: Protein S100 (S100 calcium-binding protein) (A0A0S2Z4H2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00004369}.
Interaction partners:
Sequence:
MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
Protein: Forkhead box protein G1 (Q568V0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Paired box protein Pax-6
- Empty spiracles homeobox 2.
- GS homeobox 2
- Sonic hedgehog protein
- Empty spiracles homeobox 3.
- Transcription factor Sox-2
- Nuclear receptor subfamily 2 group E member 1
- LIM/homeobox protein Lhx9
- Homeobox protein OTX2
- Homeobox protein EMX1
Sequence:
MLDMGERKEVKMIPKSSFSINSLVPEAVQSDNHHHHHHQQQQHHHRTVHEEEEKTPLPAQVQEQKSENTCAKSDNSSHDSSCTDEKEKQEEKRDAKEGEGGKEGDKKNGKYEKPPFSYNALIMMAIRQSPEKRLTLNGIYEFIMKNFPYYRENKQGWQNSIRHNLSLNKCFVKVPRHYDDPGKGNYWMLDPSSDDVFIGGTTGKLRRRSTTSRAKLAFKRGARLTSTGLTFMDRAGSLYWPMSPFLSLHHPRASSALSYNGASSAYPSHPMSYSTMLTQNSLGNNHSFPASNGLSVDRLVNGEIPYATHHLTAAALAASVPCGLSVPCSGTYSLNPCSVNLLAGQTSYFFPHVPHPSMTSQSSTSMSSRAASSSSPQTASSLPCDSLRPSLSSFSSGLSSGLSDYFTHQNQGSTSNPLIH
Protein: RH04488p (Q7JQK2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSEEKKNGDELNDLLDSALQDFDKSGAGDQKEPSASSDVATNAGPEGSEDPDAFFIEQAKVLADRMNTLFGGPDTPSGDIPPLPQDPDQIMAGFKKMAEAAALTLSGENSATDEDVSKYSDSISQALKGLQEGSENLAAPASENDIASMFGSLNLEGVCILKMKYEFSLLNH
Protein: XTimeless1 (Q3LGB9)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDLYMMNCELLATCSALGFLEGDTYHKEPDCLESIKDLIRYLRHEDDTRDIRQQLGAAQILQNDLVPLVIQHHNDKQLFDAVIRLMVNLTQPALLCFGKVPQDPTFRHHFLQIVSYLQAYKEAFADERLFGVLSEKLYDLLQMEWEQREEEHNLLIERILLLVRNILHVPPDPEEEKSVDDDASIHDRVLWAIHMSGMDDLIKFLASSETEQQWSMHVLETVSLMFRDQIAEHLAATGQARSTAERDTDIKNLEILRQREMAEKKNRALQRGNRHSRFGGSYIVQGLKSIGDKDVIYHKGLQNFKNYTHDLGKEMRRVPKRKQQAKDTEARRRSALNVRLFLKEFCIDFLENCYNRLMYIVKDNLIREKAQQHDETYYLWSMAFFMGFNRLFHFKPELVSETVSIRTFHFIEQNLTNYYEMMLTDKKEATSWARRMHLALKAYQELLSNVHEMDHSKEEAVRESSKIIKNNIFYLMEYRELFLALFRKFDETKQPRSFLKDLVETTHLFLKMLEKFCKGKQTVVVQNRRVNERKKKSSVSGTKAAQPKSIEELEAIWTNVSEQLRTCTLDSANLPDSVVPFDAASEIPVEEQRAEALVRIQDGLFSGHASEALVLLRSAREVWPEGDVFGAAEIEPEEETELLKQILFADLPRSTQAEIEDLGEEEEEEEIEEEELTSVQVSEKEFNVLDYMKRFANSNVVKTYVLLLKNYQQNSAHTNHCVAKMLHRIAYDLKMEALLFQLSVFCTFNKILVDPAASAYKELVVFSKYILNKFFSLAATNNKAYVELLFWKNTNVIREMTEGYRKLGEEESEGNRKRIKWTPEDDEELRSLYLQLKEVEDVDVVDNILANLKPGTRTRKQVINHLVQMGLADSVKDFKNEVKGTRIVLWTEDQELELQSLYEEFKDTDDILGNIMKNVTAKRSKARIIEKLISMGLVFDRKELYKKRRKMGKSSGMSEEEFLHELEFDGKHSVEDVEEDEEEEEESEEEEEQREDLKYKQNAKVQTGGKMEPFTDKKIQHLVHTLQQEGLSGPLLWLQNCLNRTAEDKEEDGSSQAIPLVPLTEDNEDAMENKTFQKLLKKLGIRAPANEQESFWRIPGKLSPEQLRKAASCLVPLAAEVAHDVLASSEEQETNVEQRAEALRALLLARKKKSTVQQELQEEKSPEKSLESHTQKRRPKTAKKRSVMVDSDEENSIENTNEHKESEQLPPDANTETETKLNRPNKSKKRSRIVDSDDDDDGSMTEEQGKEPLELDQKGSLSESDTEENVQPTKKKRLIIEDEDED
Protein: Meckelin (Meckel syndrome type 3 protein homolog) (Transmembrane protein 67) (P0C152)
Organism: Rattus norvegicus (Rat)
Function: Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appropriate number through modulating centrosome duplication. Is a key regulator of stereociliary bundle orientation. Required for epithelial cell branching morphology. Essential for endoplasmic reticulum-associated degradation (ERAD) of surfactant protein C (sftpc) (By similarity). Involved in the negative regulation of canonical Wnt signaling, and activation of the non-canonical cascade stimulated by WNT5A (By similarity). In non-canonical Wnt signaling, it may act as ROR2 coreceptor (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q5HYA8}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19815549}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5HYA8}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000250|UniProtKB:Q5HYA8}.
Interaction partners:
- Tectonic family member 1
- Transmembrane protein 216
- B9 domain-containing protein 1
- Coiled-coil and C2 domain containing 2A
- B9 domain-containing protein 2
- Transmembrane protein 231
- Centrosomal protein 290
- Tectonic-like complex member MKS1
- Jouberin
- Transmembrane protein 17
Sequence:
MVMRTRPLAAMAVRSCFSALTGTVYLLLVLCEVSWAQIFSFPFQRPETCDLNQYFDISALSCAPCGANQRRDALGTSCICLPGYHMISNNGGPSIICKKCPENMKGVTKDGWDCISCPNGLTAEGKCHCPSGHILVERNVSGSLLSQATCELCDGNENSFTKPNALGTRCVRCEPTFVNTSRSCSCSEPHISTGGLCFSNTGNFPQRLISTERYGELGMSSNSEWFTKYLQATAAACWTHSNLTSCQALGNMCVMNMNSYDSTTFDACRLFHYVFEGAAGLTGVHSVPFWRQNLPWLFYGDQPGLASQVLSTTPLPTNFSFKGQNQLKFVAASYDIRGNFIRWQTVKGGVLQLCPDTERRLDAAYSFGTTYQQNCEISLSKLLADFPSPVFYDIYLEYTDEVQHHYLWAIPVLNLNLQHNKLFVNQDSSSSKWLLTRRIFLVDAVSGRENDLGNQPRVIRVATQISLSIRLVPNTKNGNIYTPLLTIAYSDIDIKNAYSQSVKISFSVKYEMNQGDAFVQTDIALGVLGGLAVLSSLLKTAGWKRRIGSPMIDLQTVMKFLLYYAGDLANVFFIITVGTGLYWLIFFKAQKSVSVLLPMPVQEERFVTYVGCAFAMKALQFLHKLISQITIDIFFIDWERPKGKVLKAVEGEGGVRSATVPVSIWRTYFVANEWNEIQTVRKINPLFQVLTTLFFLEVVGFKNLALMDPSSSLSRSLSDYAAPYSRILRYAVATTIWLVIGIVQVVFFAAFYERFIEDKIRQFVDLCSMSNVSVFLLSHRCFGYYIHGRSVHGHADTNMEDMNMNLRREAENLCSQRGLVPNTDGQTFQIAVSSQMRQHYDRIHETLTRRNGPARLLSSSGSTLEQSIKAYHAMNKFLGSFIDHVHKEMDYFIKDKLLLEKILGMEFMEPLEKSIFYNDESHSFSSVLYYGNEATLLIFDLLFFCVVDLACQNFVLASFLTYLQQEIFRFIRNTVGQKNLATKTLVDERFLI
Protein: Mucosal addressin cell adhesion molecule 1 (MAdCAM-1) (rMAdCAM-1) (O70540)
Organism: Rattus norvegicus (Rat)
Function: Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both the integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- L-selectin
- Integrin beta
- Integrin alpha-4
Sequence:
MEPILALLLALGPFQLSRGQSFQVNPPEPEVAVAMGTSLQINCSMSCDKDIARVHWHGLDTNLGNVQTLPGSRVLSVRGMLSDTGTRVCVGSCGSRSFQHSVKILVYAFPDQLEVTPEFLVPGRDQVVSCTAHNIWPAGPDSLSFALLRGEQSLEGAQALETEQEEEMQETEGTPLFQVTQRWLLPSLGTPALPALYCQVTMQLPKLVLTHRRKIPVLQSQTSPEPPSTTSAKPYILTSSHTTKAVSTGLSSVALPSTPLSSEGPCYPEIHQNPEADWELLCEASCGSGVTVHWTLAPGDLAAYHKREAGAQAWLSVLPLGPIPEGWFQCRMDPGGQVTSLYVTGQVIPNPSSMVALWIGSLVLGLLALAFLAYCLWKRYRPGPLPDSSSCTLL
Protein: Uncharacterized membrane protein C30D10.09c (O14355)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- TBC domain-containing protein C23D3.03c
- Probable lipase C14C8.15
- Uncharacterized membrane protein C18H10.18c
- Uncharacterized protein C594.02c
- Putative mannan endo-1,6-alpha-mannosidase C1198.07c
- GTPase-activating protein gyp3
- Putative lysophosphatidic acid:oleoyl-CoA acyltransferase
Sequence:
MQLLMLEQISLASSVVATTVLVAPVLSTIINLLTNFGQRIFIAADSSKSTSMEFLSTIIGAGYPIYKTYLLLELPSKRSQLLPKAFQLRNEEHKSIEEERRRLMAYWCVYGCVTAAESILGRFLSWVPFYSTSKIVFWLWLLNPRTQGAAFIYASYISPFLSDHKAAINNFLEKLVQFTTRQPLVLNAWALVKSLIDKLPKGDVEAPGSDADTKKSK
Protein: Anion exchange protein (Q9VM32)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
MAEKNEYIELPWTMNSSSGDDEAPKDPRTGGEDFTQQFTENDFEVTPPAQRVQFILGEDVDDGTHVSHPLFSEMGMLVKEGDEIEWKETARWIKFEEDVEEGGNRWSKPHVATLSLHSLFELRRLLVNGSVMLDMEAQNLEVMADLVCDHMVSAGTLPPGVKDKVKDALLRRHRHQHEYAKKTRLPIIRSLADMRNHSSSKKKKSNSKHSRPAQNLSSITEDMVKSPSNQSMARPGSGTELSEQQHKGNTHFMRKIPPGAEASNILVGEVDFLERTLSCFIRLSQAVVLGDLTEVPVPTRFVFILLGPPGSQSNFHEIGRAMATLMSDEIFHEVAYRARKRDHLLSGVDEFLDAVTVLPPGEWDPTIRIEPPAAIPSQEVRKRPPELPKEEVDEEEEEARLREENGLSRTGRLFGGLINDIKRKAPWYISDYKDALSMQCVASWIFLYFACLSPIITFGGLLAEATGKHMAAMESLVSGFVCGMGYGFFSGQPLTILGSTGPVLVFESIIYEFCLKMGWDYMTFRFWIGMWVAGICIVLTAIDASALVCYITRFTEENFATLIAFIFIYKAIENVMVIGKNFPVNQGIYDCVCTPPIGSNASVIDYAKYNWDSCESYNGTLVGGDCGTPPTENVFLMSVVLCAGTFLISTVLKEFKNALFFPSIVRQYISDFSVLIAIFAMSFFDYSLGVPTQKLEVPNELKPTLSTRGWLIPPFVEKNPWWSAIIAVFPALLGTILIFMDQQITAVIVNRKENKLKKGCGYHLDLFILSILIAICSMMGLPWFVAATVLSINHVNSLKLESECSAPGEKPQFLGVREQRVTHILIFLTIGVSVLLTPLLGNIPMPVLFGVFLYMGVASLKGLQFFDRILIMFMPAKYQPDYMFLRQVPIKRVHLFTMIQLACLIILWLIKSFSQTSILFPLMLVVMIGIRKALDLVFTRRELKILDDIMPEMTKRAAADDLHKLDAEVGLLARIFPWGKGSRSRVVTKPPGLDDGIVGSGGAVGAGLITCTTSNANEKEFEAQSSLLKK
Protein: Phytochrome A (Protein ELONGATED HYPOCOTYL 8) (Protein FAR RED ELONGATED 1) (Protein FAR RED ELONGATED HYPOCOTYL 2) (P14712)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenetic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion. Involved in the flowering time regulation. Can phosphorylate FHY1 and, possibly, FHL, in red light conditions; this inactivates their co-shuttling to the nucleus. Regulates phototropic responses both in the nucleus (e.g. hypocotyl elongation and cotyledon opening under high-irradiance conditions and seed germination under very-low-fluence conditions) and in the cytoplasm (e.g. negative gravitropism in blue light and red-enhanced phototropism).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:21969386}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:21969386}. Nucleus speckle {ECO:0000269|PubMed:15707897}. Note=Cytoplasmic in darkness, but translocated to the nucleus upon illumination, when associated with PAPP5 into speckles. {ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:21969386}.
Interaction partners:
- Transcription factor PIF3
- Cryptochrome-1
- Cryptochrome-2
- Protein FAR-RED-ELONGATED HYPOCOTYL 1-LIKE
- E3 ubiquitin-protein ligase COP1
- Protein FAR-RED ELONGATED HYPOCOTYL 1
- Transcription factor PIF4
- Transcription factor PIF1
- Phototropin-1
- Protein SUPPRESSOR OF PHYA-105 1
Sequence:
MSGSRPTQSSEGSRRSRHSARIIAQTTVDAKLHADFEESGSSFDYSTSVRVTGPVVENQPPRSDKVTTTYLHHIQKGKLIQPFGCLLALDEKTFKVIAYSENASELLTMASHAVPSVGEHPVLGIGTDIRSLFTAPSASALQKALGFGDVSLLNPILVHCRTSAKPFYAIIHRVTGSIIIDFEPVKPYEVPMTAAGALQSYKLAAKAITRLQSLPSGSMERLCDTMVQEVFELTGYDRVMAYKFHEDDHGEVVSEVTKPGLEPYLGLHYPATDIPQAARFLFMKNKVRMIVDCNAKHARVLQDEKLSFDLTLCGSTLRAPHSCHLQYMANMDSIASLVMAVVVNEEDGEGDAPDATTQPQKRKRLWGLVVCHNTTPRFVPFPLRYACEFLAQVFAIHVNKEVELDNQMVEKNILRTQTLLCDMLMRDAPLGIVSQSPNIMDLVKCDGAALLYKDKIWKLGTTPSEFHLQEIASWLCEYHMDSTGLSTDSLHDAGFPRALSLGDSVCGMAAVRISSKDMIFWFRSHTAGEVRWGGAKHDPDDRDDARRMHPRSSFKAFLEVVKTRSLPWKDYEMDAIHSLQLILRNAFKDSETTDVNTKVIYSKLNDLKIDGIQELEAVTSEMVRLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEAIGKHFLTLVEDSSVEIVKRMLENALEGTEEQNVQFEIKTHLSRADAGPISLVVNACASRDLHENVVGVCFVAHDLTGQKTVMDKFTRIEGDYKAIIQNPNPLIPPIFGTDEFGWCTEWNPAMSKLTGLKREEVIDKMLLGEVFGTQKSCCRLKNQEAFVNLGIVLNNAVTSQDPEKVSFAFFTRGGKYVECLLCVSKKLDREGVVTGVFCFLQLASHELQQALHVQRLAERTAVKRLKALAYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQTSALCQKQLSKILDDSDLESIIEGCLDLEMKEFTLNEVLTASTSQVMMKSNGKSVRITNETGEEVMSDTLYGDSIRLQQVLADFMLMAVNFTPSGGQLTVSASLRKDQLGRSVHLANLEIRLTHTGAGIPEFLLNQMFGTEEDVSEEGLSLMVSRKLVKLMNGDVQYLRQAGKSSFIITAELAAANK