wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c oxidase subunit 5B, mitochondrial (Cytochrome c oxidase polypeptide VIa) (Cytochrome c oxidase polypeptide Vb) (P00428)
Organism: Bos taurus (Bovine)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Peripheral membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Matrix side {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
Interaction partners:
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 6C
Sequence:
MASRLLRGVGALASQALRARGPNGVSVVRSMASGGGVPTDEEQATGLEREVMLAARKGQDPYNILAPKATSGTKEDPNLVPSITNKRIVGCICEEDNSTVIWFWLHKGEAQRCPSCGTHYKLVPHQLAH
Protein: Angiopoietin-like 3 (F7FHP0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Angiopoietin-like 8
- Lipoprotein lipase
- Angiopoietin-related protein 4
- Glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1
- Apolipoprotein A-V
- Apolipoprotein C-III
- Apolipoprotein B-100
- Endothelial lipase
- Proprotein convertase subtilisin/kexin type 9
Sequence:
MHTIKLLLFVVPLVISSRVDPDLSPFDSVPSEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQCFYDLSLQTNEIKEEEKELRRTTSKLQVKNEEVKNMSLELNSKLESLLEEKMALQHRVRALEEQLTSLVQNPPGAREHPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHIQIKEIENQLRKTGIQEPTENSLYSKPRAPRTTPPLHLKEAKNIEQDDLPADCSAIYNRGEHTSGVYTIRPSSSQVFNVYCDTQSGTPRTLIQHRKDGSQNFNQTWENYEKGFGRLDGEFWLGLEKIYAIVKQSNYILRLELQDWKDSKHYAEYSFHLGNHETNYTLHVAEIAANIPEALPEHRDLMFSTWDHRAKGQLYCPESYSGGWWFSDMCGENNLNGKYNKPRAKSKPERRRGISWRPRGGKLYSIKSSKMMLQPTT
Protein: Minichromosome loss protein 1 (DNA polymerase alpha accessory factor Mcl1) (Q9C107)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in regulating DNA replication complexes. Acts as a regulator of post DNA replication initiation. Associates with chromatin during G1 and S phases of mitosis. Required for the transcriptional repression of the outer repeats of the centromeric region. Acts as a polymerase alpha replication accessory factor and is important for S-phase DNA damage survival. Plays a role in lagging-strand synthesis and Ozaki fragment processing, in addition to DNA repair.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- DNA polymerase alpha catalytic subunit
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm5
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm6
- DNA replication complex GINS protein sld5
- DNA replication complex GINS protein psf2
- F-box/TPR repeat protein pof3
Sequence:
MAGNRLVPRYAHTDGLTRLAYTRDGKFLLTVGSNQVIRKFQVGSDEEPDSIDNHQDPITGIAVAENYFCTCSEDATVCVYPIDSPTEHTLLARTTLPIRDVAYSVDGNWIAIASDETAVKVVSSTDSSQIFSLRPAKASNKHVTYSPNGNFLAVSSCNGILYFYDTQTRELIKFLTNTIASLEAESEICSKAAWHPKNGTFAVASTDHFVSVISPDDWLPLYKLLPKENHSGVTDISWSSNGMYIAASFKKGGILIWDTQSHEVVVELPYSTVVALAWQPFENVLSFTTNQGILYSCPDVIPKSILKEENDPTKPLTSSKSKNRTSKELDDLFGSDDEQSQNVNDLDGNSANEENEFINHDGLDSSLDLDGDSYMVDENDLNLAKKRKQKALIDRTTTIENGSSKRRLLQASIHKPVHTGSTPWQGNRRYLCLNLVGFIWTVQQDAEHNTITVEFHDETTHRKYHFVDDQKFEMACLDHEGALYASPATESSPGVIYYKAHVDWSRKSEWAMALPMENESPVTISLSSSVVLVCTSAGYVRVFSRQGFPISIHRSKHLPFVACSSFQDTIITIANDGLSSDGNSRLVYSIEDISRDEMLQTGDGVALPPQGTLESVFFSDVGDPYIYDSTGVLLVLMHWRIPGQAKWIPVLDTNELERRKSRQESYWPVTVADNQFHCILLKGASRYPYFPRPMFTEFDFRIPCNTNNPDASTSVPVLEELQLRNKLFLTLLEDSIGDGDVTEDEKISIARLEANIDKALLQLIQKACLEERIERVYELTKTLRRTTSIAAAQKIALHHSLTNVAEKIGNLLSNV
Protein: Calpain-9 (EC 3.4.22.-) (Digestive tract-specific calpain) (New calpain 4) (nCL-4) (O35920)
Organism: Rattus norvegicus (Rat)
Function: Calcium-regulated non-lysosomal thiol-protease.
Interaction partners:
Sequence:
MPYLHRSLRPQPQPVPRDARTVHSSGHSFEQLRQSCLQSGTLFEDADFPASNSSLFYSERPQVPFVWKRPGEIVENPEFILGGATRTDICQGELGDCWLLAAIASLTLNQKALARVVPQDQGFGSGYAGIFHFQFWQHSEWLDVVIDDRLPTFRDRLVFLHSADHNEFWSALLEKAYAKLNGSYEALKGGSAIEAMEDFTGGVAENFQIREAPEDFYEILEKALRRGSLLGCSIDTLNASESEARTPLGLIKGHAYTVTGLDQVNFHGQRIKLIRVRNPWGQVEWNGPWSDSSPEWRSMSLEEQKRLGHTALDDGEFWMAFEDFKTHFDKVEICNLTPDALEDNTLHKWEVTIHQGSWVRGSTAGGCRNFLDTFWTNPQIKLSLTERDEGQEGCTFLAALMQKDRRRLKRFGANMLTIGYAIYQCPDKDGHLNRDFFRYHASLARSKTFINLREVSGRFQLPPGDYILIPSTFEPHQEADFCLRIFSEKKAVTQDLDENIDIDLPELPKPTPQEEETEEERQFRALFRRIAGEDMEVSAEELEYVLNAVLQKKTALKFKRLSLLSCRNIISLMDTSGNGKMEFEEFRVFWDKLRYWMDLFLQFDVDKSGTMSSYELRTALKAAGFQLGSHLLQLIVLRYADENLQLDFDDYLNCLVRLENASRVFQCLSVKNKDFIHLNINEFINLTMNI
Protein: Aminopeptidase (EC 3.4.11.-) (Q9VFX0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
- Aminopeptidase
- Aminopeptidase
- Alpha-mannosidase
- RE65433p
- Uncharacterized protein, isoform A
- trypsin
- Zinc carboxypeptidase A 1
- Trypsin zeta
- Trypsin theta
- V-type proton ATPase subunit a
Sequence:
MIVTAKLVAIGLGLALTAFTVSTIVLAVQKANLKSDLRDAQEKLDLLEAGYTSTAAPTTASTANPGSTASPGSTAEPGSTAEPGSTAEPGSTASPGSTVTPGSTASTSEPGTTASPEKIDYRLPGTLKPTHYDLYLFPNIETGEFSGQETITITVEEATDQIVLHSLNLNISSVSIMNTGSDTLEILETTVDAVREFLIFQLNEPLTKGRTVRLHIGFEGSMANKIVGLYSSSYVKEDETRKWIATSKFEPTYARQAFPCFDEPALKAEFTITLVHPSGEDYHALSNMNVDSSVSQGAFQEVTFAKSVPMSTYLACFIVSDFAYKQVSIDTKGIGETFSMSVYATPEQLDKVDLAVTIGKGVIEYYIDYFQIAYPLPKLDMAAIPDFVSGAMEHWGLVTYRETSLLYDEATSSATNKQRIASVIAHEFAHMWFGNLVTMNWWNDLWLNEGFASFVEYLGVDAVYPEWKMRDQFTVSTLHSVLTLDGTLGSHPIIQTVENPDQITEIFDTITYSKGSSLVRMLEDFLGETTFRQAVTNYLNEYKYSTAETGNFFTEIDKLELGYNVTEIMLTWTVQMGLPVVTIEKVSDTEYKLTQKRFLSNPNDYDADHEPSEFNYRWSIPITYFTSSDSVVQRLWFYHDQSEITVTVPAAVEWIKFNADQVGYYRVNYDTDLWNDLADQLVVQPSAFGSVDRAHLLNDAFALADSTQLPYATAFELTRYLDKETDYVPWSVAASRLTSLKRTLYYTSTYAKYKKYATALIEPIYTALTWTVGEDHLDNRLRVTALSAACSLGLESCLTEAGEQFNAWLAKPEDRPKADVRETVYYYGIQSVGSQEDWDAVWELFVNESDASEKSKLMYGLSAIQIPWILQRYIDLAWNEEYVRGQDYFTCLTYISANPVGESLVWDYVRENWQRLVDRFGLNERYLGNLIPSITARFSTQTKLEEMEQFFAKYPEAGAGTAARVRALETVKNNIVWLAENLEGVDAWLDKQPL
Protein: Uncharacterized oxidoreductase YdhV (EC 1.-.-.-) (P76192)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YdhW
- Uncharacterized ferredoxin-like protein YdhY
- Uncharacterized ferredoxin-like protein YdhX
- Putative cytochrome YdhU
Sequence:
MANGWTGNILRVNLTTGNITLEDSSKFKSFVGGMGFGYKIMYDEVPPGTKPFDEANKLVFATGPLTGSGAPCSSRVNITSLSTFTKGNLVVDAHMGGFFAAQMKFAGYDVIIIEGKAKSPVWLKIKDDKVSLEKADFLWGKGTRATTEEICRLTSPETCVAAIGQAGENLVPLSGMLNSRNHSGGAGTGAIMGSKNLKAIAVEGTKGVNIADRQEMKRLNDYMMTELIGANNNHVVPSTPQSWAEYSDPKSRWTARKGLFWGAAEGGPIETGEIPPGNQNTVGFRTYKSVFDLGPAAEKYTVKMSGCHSCPIRCMTQMNIPRVKEFGVPSTGGNTCVANFVHTTIFPNGPKDFEDKDDGRVIGNLVGLNLFDDYGLWCNYGQLHRDFTYCYSKGVFKRVLPAEEYAEIRWDQLEAGDVNFIKDFYYRLAHRVGELSHLADGSYAIAERWNLGEEYWGYAKNKLWSPFGYPVHHANEASAQVGSIVNCMFNRDCMTHTHINFIGSGLPLKLQREVAKELFGSEDAYDETKNYTPINDAKIKYAKWSLLRVCLHNAVTLCNWVWPMTVSPLKSRNYRGDLALEAKFFKAITGEEMTQEKLDLAAERIFTLHRAYTVKLMQTKDMRNEHDLICSWVFDKDPQIPVFTEGTDKMDRDDMHASLTMFYKEMGWDPQLGCPTRETLQRLGLEDIAADLAAHNLLPA
Protein: DNA-directed RNA polymerase I subunit RPA135 (EC 2.7.7.6) (DNA-directed RNA polymerase I 135 kDa polypeptide) (A135) (DNA-directed RNA polymerase I polypeptide 2) (RNA polymerase I subunit 2) (P22138)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. RPA190 and RPA135 both contribute to the polymerase catalytic activity and together form the Pol I active center. In addition, subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA190 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14555487, ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase I subunit RPA43
Sequence:
MSKVIKPPGQARTADFRTLERESRFINPPKDKSAFPLLQEAVQPHIGSFNALTEGPDGGLLNLGVKDIGEKVIFDGKPLNSEDEISNSGYLGNKLSVSVEQVSIAKPMSNDGVSSAVERKVYPSESRQRLTSYRGKLLLKLKWSVNNGEENLFEVRDCGGLPVMLQSNRCHLNKMSPYELVQHKEESDEIGGYFIVNGIEKLIRMLIVQRRNHPMAIIRPSFANRGASYSHYGIQIRSVRPDQTSQTNVLHYLNDGQVTFRFSWRKNEYLVPVVMILKALCHTSDREIFDGIIGNDVKDSFLTDRLELLLRGFKKRYPHLQNRTQVLQYLGDKFRVVFQASPDQSDLEVGQEVLDRIVLVHLGKDGSQDKFRMLLFMIRKLYSLVAGECSPDNPDATQHQEVLLGGFLYGMILKEKIDEYLQNIIAQVRMDINRGMAINFKDKRYMSRVLMRVNENIGSKMQYFLSTGNLVSQSGLDLQQVSGYTVVAEKINFYRFISHFRMVHRGSFFAQLKTTTVRKLLPESWGFLCPVHTPDGSPCGLLNHFAHKCRISTQQSDVSRIPSILYSLGVAPASHTFAAGPSLCCVQIDGKIIGWVSHEQGKIIADTLRYWKVEGKTPGLPIDLEIGYVPPSTRGQYPGLYLFGGHSRMLRPVRYLPLDKEDIVGPFEQVYMNIAVTPQEIQNNVHTHVEFTPTNILSILANLTPFSDFNQSPRNMYQCQMGKQTMGTPGVALCHRSDNKLYRLQTGQTPIVKANLYDDYGMDNFPNGFNAVVAVISYTGYDMDDAMIINKSADERGFGYGTMYKTEKVDLALNRNRGDPITQHFGFGNDEWPKEWLEKLDEDGLPYIGTYVEEGDPICAYFDDTLNKTKIKTYHSSEPAYIEEVNLIGDESNKFQELQTVSIKYRIRRTPQIGDKFSSRHGQKGVCSRKWPTIDMPFSETGIQPDIIINPHAFPSRMTIGMFVESLAGKAGALHGIAQDSTPWIFNEDDTPADYFGEQLAKAGYNYHGNEPMYSGATGEELRADIYVGVVYYQRLRHMVNDKFQVRSTGPVNSLTMQPVKGRKRHGGIRVGEMERDALIGHGTSFLLQDRLLNSSDYTQASVCRECGSILTTQQSVPRIGSISTVCCRRCSMRFEDAKKLLTKSEDGEKIFIDDSQIWEDGQGNKFVGGNETTTVAIPFVLKYLDSELSAMGIRLRYNVEPK
Protein: Transcription initiation factor TFIID subunit 13 (Q9VIP1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 7
- TBP-associated factor 3
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 5
Sequence:
MASNSMPEENFEGGDFNFDDDAEDDQFVATNSGRKRLFSKELRCMMFGFGDDKNPYTETVDLLEDLVIEYIAETTHRAMEIGRTGRVQVEDIIFLVRKDPRKYARVKDLLTMNEELKKARKAFDEIKYVGTEGKLK
Protein: Intermembrane transport protein PqiB (Paraquat-inducible protein B) (P43671)
Organism: Escherichia coli (strain K12)
Function: Component of a transport pathway that contributes to membrane integrity. May directly span the intermembrane space, facilitating the transport of substrates across the periplasm (Probable).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:27795327}; Single-pass membrane protein {ECO:0000255}; Periplasmic side {ECO:0000269|PubMed:27795327}.
Interaction partners:
- Intermembrane transport protein PqiA
- Intermembrane transport lipoprotein PqiC
- Lipophilic envelope-spanning tunnel protein A
- Intermembrane phospholipid transport system binding protein MlaD
- Intermembrane phospholipid transport system binding protein MlaC
Sequence:
MESNNGEAKIQKVKNWSPVWIFPIVTALIGAWVLFYHYSHQGPEVTLITANAEGIEGGKTTIKSRSVDVGVVESATLADDLTHVEIKARLNSGMEKLLHKDTVFWVVKPQIGREGISGLGTLLSGVYIELQPGAKGSKMDKYDLLDSPPLAPPDAKGIRVILDSKKAGQLSPGDPVLFRGYRVGSVETSTFDTQKRNISYQLFINAPYDRLVTNNVRFWKDSGIAVDLTSAGMRVEMGSLTTLLSGGVSFDVPEGLDLGQPVAPKTAFVLYDDQKSIQDSLYTDHIDYLMFFKDSVRGLQPGAPVEFRGIRLGTVSKVPFFAPNMRQTFNDDYRIPVLIRIEPERLKMQLGENADVVEHLGELLKRGLRGSLKTGNLVTGALYVDLDFYPNTPAITGIREFNGYQIIPTVSGGLAQIQQRLMEALDKINKLPLNPMIEQATSTLSESQRTMKNLQTTLDSMNKILASQSMQQLPTDMQSTLRELNRSMQGFQPGSAAYNKMVADMQRLDQVLRELQPVLKTLNEKSNALVFEAKDKKDPEPKRAKQ
Protein: Juvenile hormone-inducible protein 26 (Q9GZ72)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEKIEAERQWLRYTVLPSILRNGRLVDNYSESKVTTFHVGDIDIDVIGHSEAFMLTLCYRTTINFEYDGQKFQRKMVVKKTPAMPPEMYESIQFGPLFTNEINFYTEILPEFQKFTDGKFAAPKYYYGELNQHSAVAILENFAEQGWRVTKDRVGLSLQHAMIAVSYLGRFHGFAYAMKHKNPEKFAQLTDNLKESRYANDNIHPEWKLTMKTSIDRAAKAVATYQPQIDEEFVKKFCFMISDYSQYGRQRVAPREPLATLCHGDYVRNNVAYRYDDKEEPQEIMMFDYQTLRVSSPMVDLNVFLAVSIFAEVRDPNFEDIFCEYTLALHNSYREHAKEEVPDFLSRGELLKEYVRFLPYSLSISASFLMSLVDPLDISPEEMFALQLSDEEIIERTMNRGGEVVDREVAHQVKEMLELSQATGVSIDDGIDLDKLPKE
Protein: Ubiquitin thioesterase trabid (dTrbd) (EC 3.4.19.12) (Q9VH90)
Organism: Drosophila melanogaster (Fruit fly)
Function: Positive regulator of the Wnt signaling pathway. Specifically cleaves 'Lys-63'-linked ubiquitin chains. May act by deubiquitinating APC protein, a negative regulator of Wnt-mediated transcription (By similarity). Required for an efficient wg response, but not for other signaling responses, in the eye.
Interaction partners:
- GH01161p
- Mitogen-activated protein kinase kinase kinase
- Ubiquitin-ribosomal protein eS31 fusion protein
- Nuclear protein localization protein 4 homolog
- Ubiquitin-ribosomal protein eL40 fusion protein
- ubiquitinyl hydrolase 1
- Mitogen-activated protein kinase kinase kinase 7
- APC-like, isoform A
- Adenomatous polyposis coli 2
- GH17761p
Sequence:
MCDTKDDAQKWKCETCTYENYPSSLKCTMCQASKPLLNEDIFRLSPAQESCTVAEEAAAVEVAVMSPTPSSTCYSLQPQSQARQSNVADSEKWPCKVCTYLNWPRSLRCVQCCTKRGGEAIERGKKDMDNEADGDRAGEALQALRISGSEENLANKPVQLIGATASHRLSLSRGIDDATHLNNLANASHNQSQSQHRQPVLQQQMQLQLQPQQQRESSSSAAVPPQQQKQCYVSKWACNSCTYENWPRSIKCSMCGKTREREISGSQNDLHASSSLNSQEENQQQLQQPNVDTVSVNNSFNKKHIYQLGSSETINNCDTLQERQERRQRQIRRQVDWQWLNACLGVVENNYSAVEAYLSCGGNPARSLTSTEIAALNRNSAFDVGHTLIHLAIRFHREEMLPMLLDQISGSGPGIKRVPSYVAPDLAADIRRHFANTLRLRKSGLPCHYVQKHATFALPAEIEELPIPIQEQLYDELLDRDAQKQLETPPPALNWSLEITARLSSRMFVLWNRSAGDCLLDSAMQATWGVFDRDNILRRALADTLHQCGHVFFTRWKEYEMLQASMLHFTLEDSQFEEDWSTLLSLAGQPGSSLEQLHIFALAHILRRPIIVYGVKYVKSFRGEDIGYARFEGVYLPLFWDQNFCTKSPIALGYTRGHFSALVPMEPFTRIDGRRDDVEDVTYLPLMDCELKLLPIHFLTQSEVGNEESMMRQWLDVCVTDGGLLVAQQKLSKRPLLVAQMLEEWLNHYRRIAQVITAPFIRRPQITHYSSDGDSDEE
Protein: Voltage-gated purine nucleotide uniporter SLC17A9 (Solute carrier family 17 member 9) (Vesicular nucleotide transporter) (VNUT) (Q8VCL5)
Organism: Mus musculus (Mouse)
Function: Involved in vesicular storage and exocytosis of ATP. May accumulate ATP and other nucleotides in secretory vesicles such as adrenal chromaffin granules and synaptic vesicles (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000269|PubMed:18375752}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:18375752}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:23876310, ECO:0000269|PubMed:24962569}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to mucin granules and vesicles. {ECO:0000250|UniProtKB:Q9BYT1}.
Interaction partners:
Sequence:
MPSQRSSLMQPIPEETRKTPSAAAEDTRWSRPECQAWTGILLLGTCLLYCARVTMPVCTVAMSQDFGWNKKEAGIVLSSFFWGYCLTQVVGGHLGDRIGGEKVILLSASAWGFITVTTPLLAHLGSGHLAFLTFSRILTGLLQGVYFPALTSLLSQKVQESERAFTYSTVGAGSQVGTLVTGGVGSVLLDQCGWQSVFYFSGGLTLLWAYYVYRYLLNEKDLVLALGFLAQGLPVTKPSKVPWRQLFRKASVWAAICSQLCSACSFFILLSWLPTFFKETFPNSKGWVFNVVPWMLAIPASLFSGFISDRLISQGYRVITVRKFMQVMGLGLSSIFALCLGHTTSFLKAMIFASASIGFQTFNHSGISVNIQDLAPSCAGFLFGVANTAGALAGVVGVCLSGYLIETTGSWTCVFHLVAIISNLGLGTFLVFGKAQRVDLVPTHEDL
Protein: V-type proton ATPase subunit H (A0A8I6ACJ2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTKMDIRGAVDAAVPTNIIAAKAAEVRANKVNWQSYLQGQMISAEDCEFIQRFEMKRCSEEKQEMLQTEGSQCAKTFINLMTHISKEQTVQYILTMVDDMLQENHQRVSIFFDYAKRSKSTAWPYFLPMLNRQDPFTVHMAARIIAKLAAWGKELMEGSDLNYYFNWIKTQLSSQSSQYVQCVAGCLQLMLRVNEYRFAWVEADGVNCIMGVLSNKCGFQLQYQMIFSIWLLAFSPQMCEHLRRYNIIPVLSDILQESVKEKVTRIILAAFRNFLEKSTERETRQEYALAMIQCKVLKQLENLEQQKYDDEDISEDIKFLLEKLGESVQDLSSFDEYSSELKSGRLEWSPVHKSEKFWRENAVRLNEKNYELLKILTKLLEVSDDPQVLAVAAHDVGEYVRHYPRGKRVIEQLGGKQLVMNHMHHEDQQVRYNALLAVQKLMVHNWEYLGKQLQSEQPQTAAARS
Protein: Evasin-3 (EVA3) (P0C8E8)
Organism: Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus)
Function: Salivary chemokine-binding protein which shows chemokine neutralizing activity and binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6 and CXCL8. Binds to CXCL8 with 1:1 stoichiometry. Disrupts CXCL8 homodimer formation, disrupts the glycosaminoglycan-binding site of CXCL8 and inhibits the interaction of CXCL8 with CXCR2.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRALLARLLLCVLVVSDSKGLVSTIESRTSGDGADNFDVVSCNKNCTSGQNECPEGCFCGLLGQNKKGHCYKIIGNLSGEPPVVRR
Protein: NADPH oxidase 2 (CGD91-phox) (Cytochrome b(558) subunit beta) (Cytochrome b-245 heavy chain) (Heme-binding membrane glycoprotein gp91phox) (Neutrophil cytochrome b 91 kDa polypeptide) (gp91-1) (gp91-phox) (p22 phagocyte B-cytochrome) (Q9ER28)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MGNWAVNEGLSIFVILVWLGLNVFLFVKYYKVYDDEPKYNYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRIRRQLDRNLTFHKMVAWMIALHTAIHTIAHLFNVEWCVNARVGTSDPYSVALSNIGDKENEEYLNFAREKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTSDSLKEHNLDVCADKIKEWGKIKECPVPKFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFRMEVGQYIFVKRPAVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFKACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPSASILKSVWYKYCDNATSLRLKKIYFYWLCRDTHAFEWFADLLQLLETQMQERNNANFLSYNIYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASQHPNTRIGVFLCGPEALAKTLSKQSISNSESGPRGVHFIFNKENF
Protein: Peroxiredoxin-6 (EC 1.11.1.27) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Glutathione-dependent peroxiredoxin) (Lysophosphatidylcholine acyltransferase 5) (LPC acyltransferase 5) (LPCAT-5) (Lyso-PC acyltransferase 5) (EC 2.3.1.23) (Non-selenium glutathione peroxidase) (NSGPx) (Thiol-specific antioxidant protein) (O35244)
Organism: Rattus norvegicus (Rat)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19700648}. Lysosome {ECO:0000269|PubMed:19700648}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000269|PubMed:19700648}.
Interaction partners:
- Glutathione S-transferase P
- Glutathione synthetase
- Glutathione hydrolase 5 proenzyme
- Glutathione hydrolase 7
- Glutathione hydrolase 6
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Glutathione S-transferase Mu 5
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Thioredoxin
Sequence:
MPGGLLLGDEAPNFEANTTIGHIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHFAWSKDINAYNGAAPTEKLPFPIIDDKDRDLAILLGMLDPAEKDEKGMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTASNPVATPVDWKKGESVMVLPTLPEEEAKQLFPKGVFTKELPSGKKYLRYTPQP
Protein: NAC domain-containing protein 89 (ANAC089) (Protein FRUCTOSE-SENSING QUANTITATIVE TRAIT LOCUS 6) (Q94F58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in plant cell division.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}. Note=Relocalization from the cytoplasm into the nucleus is induced by auxin treatment and in association with PAS1. {ECO:0000269|PubMed:16803883}.
Interaction partners:
- bZIP transcription factor 60
- bZIP transcription factor 28
- Metacaspase-5
- bZIP transcription factor 17
- BAG family molecular chaperone regulator 7
- Bax inhibitor 1
- Serine/threonine-protein kinase/endoribonuclease IRE1b
- Heat shock 70 kDa protein BIP3
- Bax inhibitor-1 family protein
- Endoplasmic reticulum oxidoreductin-1
Sequence:
MDTKAVGVSKDTAASMEASTVFPGFKFSPTDVELISYYLKRKMDGLERSVEVIPDLEIYNFEPWDLPDKSIVKSDSEWFFFCARGKKYPHGSQNRRATKMGYWKATGKERDVKSGSEVIGTKRTLVFHIGRAPKGERTDWIMHEYCVKGVSLDDAMVVCRVRRNKEYNSGTSQKAPKPNSSAEKHAKVQNGATSSGSPSDWDNLVDFYLAGESGEKLLAEMAESSENLQVDNDEDFFADILRDEIINLDEAVMTGNTPNEVPTLESASMEIRVLPLPNMIDKQMSSLLEERPSQKKKGKDATESLSSCFVGLYSIKSVNKARWDVIIGVVALIAMLFYLE
Protein: D(2) dopamine receptor (Dopamine D2 receptor) (P14416)
Organism: Homo sapiens (Human)
Function: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21645528, ECO:0000269|PubMed:26535572}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:26535572}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium-dependent dopamine transporter
- Guanine nucleotide-binding protein G
- Beta-arrestin-2
- Adenosine receptor A2a
- Guanine nucleotide-binding protein G
- Cannabinoid receptor 1
- Guanine nucleotide-binding protein G
- Neuronal calcium sensor 1
- Guanine nucleotide-binding protein G
- Beta-arrestin-1
Sequence:
MDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYNYYATLLTLLIAVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISIVWVLSFTISCPLLFGLNNADQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRAHLRAPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHPKIAKIFEIQTMPNGKTRTSLKTMSRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFLKILHC