wanglab/gogpt-training-data huggingface dataset:
Protein: Sialin (H(+)/nitrate cotransporter) (H(+)/sialic acid cotransporter) (AST) (Solute carrier family 17 (Anion/sugar transporter), member 5) (Vesicular excitatory amino acid transporter) (VEAT) (Q5Q0U0)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional anion transporter that operates via two distinct transport mechanisms, namely proton-coupled anion cotransport and membrane potential-dependent anion transport (By similarity). Electroneutral proton-coupled acidic monosaccharide symporter, with a sugar to proton stoichiometry of 1:1. Exports glucuronic acid and free sialic acid derived from sialoglycoconjugate degradation out of lysosomes, driven by outwardly directed lysosomal pH gradient. May regulate lysosome function and metabolism of sialylated conjugates that impact oligodendrocyte lineage differentiation and myelinogenesis in the central nervous system (By similarity). Electrogenic proton-coupled nitrate symporter that transports nitrate ions across the basolateral membrane of salivary gland acinar cells, with nitrate to proton stoichiometry of 2:1. May contribute to nitrate clearance from serum by salivary glands, where it is further concentrated and secreted in the saliva (By similarity). Uses membrane potential to drive the uptake of acidic amino acids and peptides into synaptic vesicles. Responsible for synaptic vesicular storage of L-aspartate and L-glutamate in pinealocytes as well as vesicular uptake of N-acetyl-L-aspartyl-L-glutamate neuropeptide, relevant to aspartegic-associated glutamatergic neurotransmission and activation of metabotropic receptors that inhibit subsequent transmitter release (By similarity).
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9NRA2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NRA2}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q9NRA2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NRA2}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NRA2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NRA2}.
Interaction partners:
Sequence:
MRPLLRGPAGNDDEESSDSTPLLPSARQIEAAPACCSARYNLALLAFCGFFVLYALRVNLSVALVDMVDSNSTLTDNRTSKECAEHSAPVKVHHNHTGKKYQWDAETQGWILGSFFYGYIVTQIPGGYMASRIGGKLLLGLGILGTAVFTLFTPLAADLGVVALIVLRALEGLGEGVTFPAMHAMWSSWAPPLERSKLLTISYAGAQLGTVISLPLSGIICYYMNWTYVFYLFGLVGIVWFILWMWIVSDTPETHKTISHYEKEYIVSSLKNQLSSQKVVPWVSILKSLPLWAIVVAHFSYNWTFYTLLTLLPTYMKEILRFNVQENGFLSALPYFGCWLCMIVCGQAADYLRVKWNFSTISVRRIFSLIGMVGPAVFLVAAGFIGCDYSLAVAFLTISTTLGGFASSGFSINHLDIAPSYAGILLGITNTFATIPGMIGPIIAKSLTPDNTIKEWQTVFCIAAAINVFGAIFFTLFAKGEVQNWALSDHHGHGN
Protein: Ribosome control protein 1 domain-containing protein (Q382D3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Small GTP-binding protein RAB6, putative
- Conserved oligomeric Golgi complex subunit 8
- ATP-dependent DEAD/H RNA helicase
- Conserved oligomeric Golgi complex subunit 6
- ADP-ribosylation factor-like protein, putative
- Conserved oligomeric Golgi complex subunit 3
Sequence:
MRFPSGSLAAYPLETYMVVPGERALEVSVCPTGSYAALLSGGHLHFLTCNTDVVVIGSVSICNAMGDKDYATHFLWHPLGEQLVVSTYHGRLLYFNVAIDVHRERCLTQVYRVNSLPIGCAASCVPLTNEVHLEGDAVVSLVSAGHHCFFACTATGLVRVLGWFKKNLLHTYDANFLSGGLHTFSGLDAACREHTSKDLCAGGTPITSIAILDICYSCQLELTGLLLSSGQFLLANSSAGDDFSCDNVVFNGVCVASAGTSRVCINPRHPLAVLATPTGELECKRISDDLSLTVFWIDVKCVTSDEYRGSIRCMVWTDDGEMLCVGYNQSGIMVLHYSGICVYSSHVAEYPRQHGLRPAIGIEGCASLSWCGNQLLIVDPRGLALTVLGFSKVVSSPCAEATAMFTPACTLDGSKLRFIEQQHTDGSLAFSDTVLLNPRYAVENNPITYGAISSDGSVVALAGRNGFLLFDRLARRWRTMRDRKEEREFTCVAQPVWVKDLMVVFPVRLERTHEYELRVYNRVLSKGAMLVRMPLQNKPLRLSECHDEDGDVFVHLFDDSGTLLVWRCVLSSTYPHAKHNLEVSLKLVKRVPLPRMFRNPVNMMAIHPARLSAYRTTSSPCKFRGNRDEALLPYVLFVVSGSNALIALDLNAVMNRVSVRVASEPLVPLTTIFPSGLFHLWVDYTAPLDGAVLLAVSDRGVSILHLSLDTSGGVTSSLCVNEYRVGDSTDPILAPVGLSAYDGCLLTAFADVDASQQTLSSVSHFSVRTVVVPSMYNYRVLGEVIALRSKISSSITKGPIGGASVQSVSFPWDERVLCWIEGMRRNSTLVCNADYLLCTLIDRETSSLSDSEDPCSMLRLTLSLLQRYPEYHRIVVNCLRKLELPCCPVVVDNIGSTKKLFVSCLEESRLEEAAHLLHLIMVDDGEGGKNGSLDTLRQTLVCATRILMLAVSCKKVQLIYTLLPFMALIFKELLVSDDEERLRALFSDAKGQCALAGLRRSTANLSLLLDTEQDFTTLSSPWSFSYDTSEVGMKEIRSLTTFLVSGDSGLSEALEYVTTDCLRSGRLLTLYEIVRGFSLSPYGMMELKLDEVRDPHCGVSSHGEGSSVRGHFPHLPTHGELFLNLFTGIHEEFSLTRSPRCVGNELRRHRSSVVGAEVATTDFTLWTLAQSILYSTPGLPETLRHLRDHFAMWDECVLAINIILMCFTDVVHQLRRHSELVQALQHLLVDERNCGYKSFIRYCLENVS
Protein: Atrochrysone carboxyl ACP thioesterase (ACTE) (EC 3.1.2.-) (Monodictyphenone synthesis protein F) (Q5BH31)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG. The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG. The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone. The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL. The short chain dehydrogenase mdpC converts the tautomers of emodin hydroquinone into the 3-hydroxy-3,4-dihydroan-thracen-1(2H)-one derivative. These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin. Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps.
Interaction partners:
- Atrochrysone carboxylic acid synthase
- Monodictyphenone cluster transcriptional coactivator mdpA
Sequence:
MAQPQQHKGGYKQINKALNICAFEDYLSAQLKHLPQLADVEQLSPRVIRVLGQNAGKGTNTYIVGTGPQRLIIDTGQGIPEWADILDATLKERSISLSHVFLSHWHGDHTGGVPDLLRLYPNLAGAIYKNSPGSDQQPIDDGQVFRVEGATIRAVHGPGHSHDHMCFILEEENAMFTGDNVLGHGTSAVEELGVYMETLRKLNSHHCAVGYPAHGDVITNLPAKIAGELAQKMRREKQVLLTLDRINKESRRTGQVVLVHGDGIDEEVRKMALEPFIDEVLRKLAEDGKVAFEMRGGVKRWFGVGVL
Protein: Cation-dependent mannose-6-phosphate receptor (CD Man-6-P receptor) (CD-MPR) (46 kDa mannose 6-phosphate receptor) (MPR 46) (P20645)
Organism: Homo sapiens (Human)
Function: Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex.
Subcellular location: Lysosome membrane; Single-pass type I membrane protein.
Interaction partners:
- ADP-ribosylation factor-binding protein GGA3
- Cation-independent mannose-6-phosphate receptor
- ADP-ribosylation factor-binding protein GGA1
- ADP-ribosylation factor-binding protein GGA2
- Perilipin-3
- Trans-Golgi network integral membrane protein 2
- Vesicle transport through interaction with t-SNAREs homolog 1A
Sequence:
MFPFYSCWRTGLLLLLLAVAVRESWQTEEKTCDLVGEKGKESEKELALVKRLKPLFNKSFESTVGQGSDTYIYIFRVCREAGNHTSGAGLVQINKSNGKETVVGRLNETHIFNGSNWIMLIYKGGDEYDNHCGKEQRRAVVMISCNRHTLADNFNPVSEERGKVQDCFYLFEMDSSLACSPEISHLSVGSILLVTFASLVAVYVVGGFLYQRLVVGAKGMEQFPHLAFWQDLGNLVADGCDFVCRSKPRNVPAAYRGVGDDQLGEESEERDDHLLPM
Protein: Hyaluronan-binding protein 2 (EC 3.4.21.-) (Plasma hyaluronan-binding protein) [Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form] (Q6L711)
Organism: Rattus norvegicus (Rat)
Function: Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII (By similarity).
Subcellular location: Secreted {ECO:0000250}. Note=Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form. {ECO:0000250}.
Interaction partners:
- WD repeat-containing protein 90
- Hyaluronan synthase 2
- Hyaluronidase.
- Hyaluronidase
- Hyaluronidase
Sequence:
MSVVMLVFRVLLLIALVGNSAIGLSLMPFIAPPDPDWTPDDYYYSYEQSSPDKDASVTQTSPENPDWYYEDDDPCQSNPCEHGGDCIIRGNTFSCSCPAPFSGSRCQTVQNKCKDNPCVQGDCLITQTPPYYRCACKYPYTGPDCSKVLPVCRPNPCQNGGVCSRHRRRSRFSCACPDQYKGRFCEIGPDDCYVGDGYSYRGKVSRTVNQNPCLYWNSHLLLQENYNMFMEDAETHGIADHNFCRNPDGDHKPWCFVKVNSEKVKWEYCNVEVCPESDAANPVGSLQEPVMELPGFDSCGKTEMTEHAVKRIYGGFKSTAGKHPWQVSLQTSLPLTTSMPQGHFCGGSLIHPCWVLTAAHCTDMSTKHLKVVLGDQDLKKTESHEQTFRVEKILKYSQYNERDEIPHNDIALLKLKPVGGHCALESKYVKTVCLPSDPFPSGTECHISGWGVTETGEGSRQLLDAKVKLIANALCNSRQLYDHTIDDSMICAGNLQKPGSDTCQGDSGGPLTCEKDGTYYVYGIVSWGQECGKKPGVYTQVTKFLNWIKTTMHKEAGL
Protein: 3-hydroxy-3-methylglutaryl coenzyme A reductase AN1593 (HMG-CoA reductase) (EC 1.1.1.34) (Pimaradiene biosynthesis cluster protein AN1593) (C8VN86)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: 3-hydroxy-3-methylglutaryl coenzyme A reductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors. The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes. Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene. The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- mevalonate kinase
- 3-hydroxy-3-methylglutaryl coenzyme A reductase
- sterol 14alpha-demethylase
- INSIG domain protein
- Squalene monooxygenase
- RING-type E3 ubiquitin transferase
- Diphosphomevalonate decarboxylase
Sequence:
MPESQIIELGTLGQIPLYSLERALQDPLRAVKLRRQIVSQHQATGNIDFTTDGSALPYEGYDYKAVLGACCENVIGYMPIPVGVAGPIKINGKMVFLPMSTTEGALVASTNRGCMAINAGGGVTALVLGDGMTRAPIVRFPSLEEAGAAKQWLGSDAGFLIIEDAFNASSRFARLQNIKATAVGSDLYIRFTASTGDAMGMNMISKGVEQALEAMQKHGFESMDVVSLSGNFCADKKPAAVNWIEGRGKTVTAQATIPEHAVRETLKTSVEALVELNVSKNLVGSAVAGALGGFNAHAANVVTAIYLATGQDPAQNVQSSNTLTVMKNVNGDLQISVFMPSIEVGTVGGGTVLGPQKAMLHMMGVQGADPEQPGRNAQELALLVAAGVLAGELSLCSALSAGSLVKSHLTHNRKKG
Protein: Calmodulin 2 (F4IJ46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MADQLTDDQISEFKEAFSLFDKDGDGMLHPPFPSIIVGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVDEMIKEADVDGDGQINYEEFVKVMMAK
Protein: Iron-sulfur protein required for NADH dehydrogenase, mitochondrial (IND1 homolog) (IND1-like protein) (Nucleotide-binding protein-like) (O49472)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential during early vegetative growth. Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). Involved in mitochondrial translation activity. May deliver of one or more Fe-S clusters to complex I subunits (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:24179128}.
Interaction partners:
- NifU-like protein 5, mitochondrial
- Iron-sulfur cluster assembly protein 3
- Protein NAR1
- Iron-sulfur cluster assembly protein 1
- NifU-like protein 4, mitochondrial
- Iron-sulfur cluster assembly protein 2
- NifU-like protein 1, chloroplastic
- Monothiol glutaredoxin-S15, mitochondrial
- Lipoyl synthase, mitochondrial
- Iron-sulfur cluster co-chaperone protein HscB homolog
Sequence:
MATVALLRSLRRRELHAAHISAYKFSSASAGGRTTELRLHGVKDIIAVASGKGGVGKSSTAVNLAVALANKCELKIGLLDADVYGPSVPIMMNINQKPQVNQDMKMIPVENYGVKCMSMGLLVEKDAPLVWRGPMVMSALAKMTKGVDWGDLDILVVDMPPGTGDAQISISQNLKLSGAVIVSTPQDVALADANRGISMFDKVRVPILGLVENMSCFVCPHCNEPSFIFGKEGARRTAAKKGLKLIGEIPLEMSIREGSDEGVPVVVSSPGSIVSKAYQDLAQNVVKGLKELRENPDNEIQMKLNVPHSSHSS
Protein: Fibroblast growth factor 21 (Q1ESX2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLFACFFIFFALFPHLRWCMYVPAQNVLLQFGTQVRERLLYTDGLFLEMNPDGSVKGSPEKNLNCVLELRSVKAGETVIQSAATSLYLCVDDQDKLKGQHHYSALDCTFQELLLDGYSFFLSPHTNLPVSLLSKRQKHGNPLSRFLPVSRAEDSRTQEVKQYIQDINLDSDDPLGMGHRSHLQTVFSPSLHTKK
Protein: Myosin heavy chain-like, isoform F (Q0KI66)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFLKPKSFEQSLRGGIVPAVPAAPGSGLNPNFHKGCTGKAHACGTNKSHRAGGSATSASGGSRAGRQTPKAQRKNSISSETISESGSENSNSWPSSSSAAVPATVPPPKPPRLAATKAKEAAAIDCSPVQPPFTPTFERSTKRSLSFRSNNSKTTEAKLTPGASSSIRPPWNISAAAASKYAAAAASAPQSPNPSTRSSFRRRRDAQNAGLHWPAILASSLAASHKNYDAILKQKSRHENGNGGGEEGGAKGVGHDLEADVADASQPERVWLVHRGGFTAAIRLPTASSGRDEENKLSLRLLHNGEQLTVDEDDVEKQNSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAFGLTQPNAPNGGLSPSKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPASCGQQVGATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASECHPGPLISLIDKAPQNHVVRSSQRDLREHDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTNPVLYAVDGWVRHSREHPGIRNAVSLLQDSSREEINRLYIGSLTRGSGAMVFCGSFAGLEGTQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCYLLQHNAGKHTKYTANGSPSSAAGQVSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNKDVSVEQILAVNELDVASYRIGPSQILFRSGVLSELEAKRDVLLSDRIIQLQAFCRGYLARKKMSQRRVQELAVRCIQRNVKAFLAVRDWPWWRLLVRVTPLLNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLRPVHVKRSSQQSLNGSIGGGGGSVVSSTRTVVFEKDDNSPRYADNEVNSNSRKQHKH
Protein: Transcription factor MYB3R-3 (Myb-related protein 3R-3) (Q8H1P9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds 5'-AACGG-3' motifs in gene promoters (By similarity). Transcription repressor that regulates organ growth. Binds to the promoters of G2/M-specific genes and to E2F target genes to prevent their expression in post-mitotic cells and to restrict the time window of their expression in proliferating cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Transcription factor E2FB
- Transcription factor E2FC
- Retinoblastoma-related protein 1
- Histone-binding protein MSI1
- At2g40630/T2P4.2
- Protein ALWAYS EARLY 2
- Protein ALWAYS EARLY 3
- Protein ALWAYS EARLY 1
- Transcription factor-like protein DPB
- Transcription factor-like protein DPA
Sequence:
MSSTFNPAASSPDEEETGEVKIEDQCVENKQSTPASCSSVSEGSAGSSHKSPTIASPATVSPTHRYLGRTSGPIRRAKGGWTPEEDETLRQAVDTFKGKSWKNIAKSFPDRTEVQCLHRWQKVLNPDLIKGPWTHEEDEKIVELVEKYGPAKWSIIAQSLPGRIGKQCRERWHNHLNPDINKDAWTTEEEVALMNAHRSHGNKWAEIAKVLPGRTDNAIKNHWNSSLKKKSEFYLLTGRLPPPTTTRNGVPDSVTKRSSSAQKRVFGSVAQTSSVTTDVNNLAEDGNGQINSSVPVEEVVAASRMTSLNEYARSPQLPNPEPLPENGGAANNGYHLYYTPQIDYYRASEVDTQRMYGNECGCSPSASPVSFFTPPPCRNVHSNGSTPRSPESYLREAGRTYPNTPSIFRKRRPRVVVQDNNNAKKTDEAKEVDQKVNDGKDSSEIQNNGSNAYNLSPPYRIRSKRTAVFKSRQLEFISREEEKADDETKSSEKDMLIDGDSQLLG
Protein: ENAH, actin regulator (A0A8I5ZND4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSHLNFVFYSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQEAGPTLPRQNSQLPAQVQNGPSQEEMEIQRRQLQEQQRQKELERERMERERLERERLERERLERERLEQEQLERQRQEREHVERLERERLERLERERQDRERERERLEQLEREQVEWERERRMSNAAAPASVETPLNPELGDSSASEPGLQAASQPAETPAPQGHVLGPPAPPPPPPLPSGPAYASALPPPPGPPPPPPLPSAGPPPPPPPPPPLPNQVPPPPPPPPAPPLPASGIFSGSMSEDNRPLTGLAAAIAGAKLRKVSRVEDGSFPSGGNTVSVNLASSKTDSGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDRSVSECKNLSLKMWSSKPTRKPWERTNTMNGSKSPVISRRDSPRKNQIVFDNRSYDSLHRPKSTPSSQPSANGVQTEGLDYDRLKQDILDEMRKELAKLKEELIDAIRQELSKSNTA
Protein: Syntaxin 6 N-terminal domain-containing protein (Q57WS2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vesicle transport v-SNARE N-terminal domain-containing protein
- Syntaxin 5
- Vesicle-associated membrane protein, putative
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting complex subunit, putative
- Vacuolar protein sorting-associated protein 45, putative
- Pep3/Vps18/deep orange beta-propeller domain-containing protein
- RING-type domain-containing protein
- Vps53 N-terminal domain-containing protein
- Vacuolar protein sorting-associated protein 54 C-terminal domain-containing protein
Sequence:
MMESMNLEQPPRLNADPWRDMEPKVDAMLGDLLMISERFRRIVNPTVSDADELIEAINSVGGEVETMRVALDTTIERPELFSVDAEELKRRTEKTRSWERDVAKAIELRSKILSNREGQIQDPLESNVMTPNTWVDLDTTHIHPSAQSSHMPMNSCEATTDTSVGVVESQALMPVGIPIREQTVKASEYSTASVEVHTVDDVDDSRSSNSAKKTVLIIFFASSLLVAILVIFF
Protein: Hypoxia-inducible factor 1-alpha (D4A8P8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MEGAGGENEKKNRMSSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDEMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGPVRKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTSSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTESVLKPVESSDMKMTQLFTKVESEDTSCLFDKLKKEPDALTLLAPAAGDTIISLDFGSDDTETEDQQLEDVPLYNDVMFPSSNEKLNINLAMSPLPASETPKPLRSSADPALNQEVALKLESSPESLGLSFTMPQIQDQPASPSDGSTRQSSPEPNSPSEYCFDVDSDMVNVFKLELVEKLFAEDTEAKNPFSAQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESNSPSPPSVSTVTGFQQTQLQKPTITVTAATATTATTTDESKAVTKDNIEDIKILIASPPSTQVPQEMTTAKASAYSGTHSRTTSPDRAGKRVIEKTDKAHPRSLNLSVTLNQRNTVPEEELNPKTIALQNAQRKRKMEHDGSLFQAAGIGTLLQQPGDRAPTMSLSWKRVKGYISSEQDGMEQKTIFLIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN
Protein: Atypical chemokine receptor 4 (C-C chemokine receptor type 11) (C-C CKR-11) (CC-CKR-11) (CCR-11) (CC chemokine receptor-like 1) (CCRL1) (CCX CKR) (Q9NPB9)
Organism: Homo sapiens (Human)
Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CCL2, CCL8, CCL13, CCL19, CCL21 and CCL25. Chemokine-binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization. Plays an important role in controlling the migration of immune and cancer cells that express chemokine receptors CCR7 and CCR9, by reducing the availability of CCL19, CCL21, and CCL25 through internalization. Negatively regulates CXCR3-induced chemotaxis. Regulates T-cell development in the thymus.
Subcellular location: Early endosome {ECO:0000269|PubMed:23341447}. Recycling endosome {ECO:0000269|PubMed:23341447}. Cell membrane {ECO:0000269|PubMed:23341447}; Multi-pass membrane protein {ECO:0000269|PubMed:23341447}. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via caveolae. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane.
Interaction partners:
- C-C motif chemokine 25
- C-C motif chemokine 21
- C-C motif chemokine 19
- C-C motif chemokine 27
- C-X-C motif chemokine 13
- C-C motif chemokine 8
- C-C motif chemokine 17
- C-C motif chemokine 13
- C-C chemokine receptor type 7
- C-C motif chemokine 1
Sequence:
MALEQNQSTDYYYEENEMNGTYDYSQYELICIKEDVREFAKVFLPVFLTIVFVIGLAGNSMVVAIYAYYKKQRTKTDVYILNLAVADLLLLFTLPFWAVNAVHGWVLGKIMCKITSALYTLNFVSGMQFLACISIDRYVAVTKVPSQSGVGKPCWIICFCVWMAAILLSIPQLVFYTVNDNARCIPIFPRYLGTSMKALIQMLEICIGFVVPFLIMGVCYFITARTLMKMPNIKISRPLKVLLTVVIVFIVTQLPYNIVKFCRAIDIIYSLITSCNMSKRMDIAIQVTESIALFHSCLNPILYVFMGASFKNYVMKVAKKYGSWRRQRQSVEEFPFDSEGPTEPTSTFSI