wanglab/gogpt-training-data huggingface dataset:
Protein: Probable metal homeostasis protein bsd1 (Q9P3T9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for homeostasis of heavy metal ions such as cadmium, cobalt and copper.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P38356}. Vacuole {ECO:0000250|UniProtKB:P38356}. Membrane {ECO:0000250|UniProtKB:P38356}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P38356}.
Interaction partners:
- Inactive zinc metalloprotease C354.09c
- SPRY domain-containing protein C285.10c
- Uracil permease
- GYF domain-containing protein mpd2
Sequence:
MSTNSNQNSIHTPIPEFPENRSTNRSELAAAFEPPDDDVEYSETAPLYSSARASIEGEEAFYQHLSTPDPGNDSGHVRSSNDRIPSTSSNHADGHHVDSVFSNLSAKPTVESNTEELEEEPPSYEQAAADTAPPYWDTTMVIPDYGSNEIYIDGMSVGTGFSFVWSACVAILFPFVGFLVTYVLSTTHLGRYGAQIGLSLTLFQRGYIMISESGMENNDDQYNYDELPHQKLIGSILIIIGWCLVLVDTFGFIRIRRMKNAISRTDSPGETSPEEVV
Protein: Diamine acetyltransferase 1 (EC 2.3.1.57) (Polyamine N-acetyltransferase 1) (Putrescine acetyltransferase) (Spermidine/spermine N(1)-acetyltransferase 1) (Q7T174)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Spermidine synthase
- ornithine decarboxylase
- Agmatine ureohydrolase
- Amine oxidase [flavin-containing]
- Amine oxidase.
- Amine oxidase
- Acyl-CoA thioesterase 9, tandem duplicate 1
- Spermine synthase.
Sequence:
MANFNLRKAEPKDVPDILRLIKELAKYEEMEDQVLITEKDLLEDGFGEHPFYHCVVADVSAEHQKVEGYSVIGFAMYYFTYDPWIGKLLYLEDFYVMKEYRGFGIGSEILKHLSDTAVKNRCSSMHFIVAESNKTSIDFYKRRGASDLSLQEGWRLFRIDKENLLKMSAEE
Protein: Probable caffeoyl-CoA O-methyltransferase At4g26220 (EC 2.1.1.104) (Trans-caffeoyl-CoA 3-O-methyltransferase) (CCoAMT) (CCoAOMT) (Q9C5D7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers (By similarity).
Interaction partners:
- Shikimate O-hydroxycinnamoyltransferase
- Cinnamoyl-CoA reductase 2
- Cinnamoyl-CoA reductase 1
- Chalcone synthase
- AT5g57840/MTI20_9
- Spermidine hydroxycinnamoyl transferase
- 4-coumarate--CoA ligase 1
- 4-coumarate--CoA ligase 2
- 4-coumarate--CoA ligase 4
- 4-coumarate--CoA ligase 3
Sequence:
MAKDEAKGLLKSEELYKYILETSVYPREPEVLRELRNITHNHPQAGMATAPDAGQLMGMLLNLVNARKTIEVGVFTGYSLLLTALTLPEDGKVIAIDMNRDSYEIGLPVIKKAGVEHKIDFKESEALPALDELLNNKVNEGGFDFAFVDADKLNYWNYHERLIRLIKVGGIIVYDNTLWGGSVAEPDSSTPEWRIEVKKATLELNKKLSADQRVQISQAALGDGITICRRLY
Protein: Hepatoma-derived growth factor-related protein 2 (HDGF-related protein 2) (HRP-2) (Hepatoma-derived growth factor 2) (HDGF-2) (Q7Z4V5)
Organism: Homo sapiens (Human)
Function: Acts as an epigenetic regulator of myogenesis in cooperation with DPF3a (isoform 2 of DPF3/BAF45C). Associates with the BAF complex via its interaction with DPF3a and HDGFL2-DPF3a activate myogenic genes by increasing chromatin accessibility through recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic gene promoters. Promotes the repair of DNA double-strand breaks (DSBs) through the homologous recombination pathway by facilitating the recruitment of the DNA endonuclease RBBP8 to the DSBs. Preferentially binds to chromatin regions marked by H3K9me3, H3K27me3 and H3K36me2. Involved in cellular growth control, through the regulation of cyclin D1 expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:26721387}. Cytoplasm {ECO:0000250|UniProtKB:Q925G1}.
Interaction partners:
- Histone H3.3
- Histone H3.1
- Histone H3.2
- Histone H3.1t
- Pogo transposable element with ZNF domain
Sequence:
MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNNPHASYSAPPPVSSSDSEAPEANPADGSDADEDDEDRGVMAVTAVTATAASDRMESDSDSDKSSDNSGLKRKTPALKMSVSKRARKASSDLDQASVSPSEEENSESSSESEKTSDQDFTPEKKAAVRAPRRGPLGGRKKKKAPSASDSDSKADSDGAKPEPVAMARSASSSSSSSSSSDSDVSVKKPPRGRKPAEKPLPKPRGRKPKPERPPSSSSSDSDSDEVDRISEWKRRDEARRRELEARRRREQEEELRRLREQEKEEKERRRERADRGEAERGSGGSSGDELREDDEPVKKRGRKGRGRGPPSSSDSEPEAELEREAKKSAKKPQSSSTEPARKPGQKEKRVRPEEKQQAKPVKVERTRKRSEGFSMDRKVEKKKEPSVEEKLQKLHSEIKFALKVDSPDVKRCLNALEELGTLQVTSQILQKNTDVVATLKKIRRYKANKDVMEKAAEVYTRLKSRVLGPKIEAVQKVNKAGMEKEKAEEKLAGEELAGEEAPQEKAEDKPSTDLSAPVNGEATSQKGESAEDKEHEEGRDSEEGPRCGSSEDLHDSVREGPDLDRPGSDRQERERARGDSEALDEES
Protein: 40S ribosomal protein S24 (Q8I3R6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 60S ribosomal protein L27
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S5, putative
- Small ribosomal subunit protein eS30
- 60S ribosomal protein L29
- 40S ribosomal protein S28e, putative
- 40S ribosomal protein S11, putative
- 60S ribosomal protein L3
- 40S ribosomal protein S15
- Small ribosomal subunit protein eS12
Sequence:
MTDQFTIRVKKYMSNPLLRRKQFALEILHPNKGSVAKKEVKERLAKMYKLNNVNTIVLFGFKTLFGGGRTKGFGLIYKNVDAVKKFEKKYRLVREGLIDKETKAGRRASKELKNRRKKVRGTEKTKVSGAKKK
Protein: Matrix metalloproteinase-24 (MMP-24) (EC 3.4.24.-) (Matrix metalloproteinase-21) (MMP-21) (Membrane-type matrix metalloproteinase 5) (MT-MMP 5) (MTMMP5) (Membrane-type-5 matrix metalloproteinase) (MT5-MMP) (MT5MMP) [Cleaved into: Processed matrix metalloproteinase-24] (Q9R0S2)
Organism: Mus musculus (Mouse)
Function: Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin.
Subcellular location: [Matrix metalloproteinase-24]: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3. {ECO:0000269|PubMed:14990567}.; SUBCELLULAR LOCATION: [Processed matrix metalloproteinase-24]: Secreted, extracellular space, extracellular matrix. Note=Also shed from cell surface as soluble proteinase, by a proteolytic cleavage. {ECO:0000269|PubMed:11470782}.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 1
- Lens fiber membrane intrinsic protein
- Metalloproteinase inhibitor 3
Sequence:
MPRSRGGRAAPGQASRWSGWRAPGRLLPLLPALCCLAAAAGAGKPAGADAPFAGQNWLKSYGYLLPYESRASALHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWMKKPRCGVPDHPHLSRRRRNKRYALTGQKWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEIKSDRKEADIMIFFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQGIQKIYGPPAEPLEPTRPLPTLPVRRIHSPSERKHERHPRPPRPPLGDRPSTPGAKPNICDGNFNTVALFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLPARIDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPKPITVWKGIPQAPQGAFISKEGYYTYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGCKQKEVERRKERRLPQDDVDIMVTIDDVPGSVNAVAVVVPCTLSLCLLVLLYTIFQFKNKAGPQPVTYYKRPVQEWV
Protein: Non-homologous end-joining factor 1 (Protein cernunnos) (XRCC4-like factor) (Q9H9Q4)
Organism: Homo sapiens (Human)
Function: DNA repair protein involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair and V(D)J recombination. Plays a key role in NHEJ by promoting the ligation of various mismatched and non-cohesive ends. Together with PAXX, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends. May act in concert with XRCC5-XRCC6 (Ku) to stimulate XRCC4-mediated joining of blunt ends and several types of mismatched ends that are non-complementary or partially complementary. Associates with XRCC4 to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired. The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other. The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors. Binds DNA in a length-dependent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:16439204, ECO:0000269|PubMed:16439205, ECO:0000269|PubMed:20558749}. Chromosome {ECO:0000269|PubMed:18064046, ECO:0000269|PubMed:18644470, ECO:0000269|PubMed:27437582}. Note=Localizes to site of double-strand breaks; recruitment is dependent on XRCC5-XRCC6 (Ku) heterodimer. {ECO:0000269|PubMed:18064046, ECO:0000269|PubMed:18644470, ECO:0000269|PubMed:27437582}.
Interaction partners:
- DNA-dependent protein kinase catalytic subunit
- X-ray repair cross-complementing protein 6
- X-ray repair cross-complementing protein 5
- DNA repair protein XRCC4
- DNA ligase 4
- Protein PAXX
- Protein artemis
- Serine-protein kinase ATM
- DNA excision repair protein ERCC-1
- UV excision repair protein RAD23 homolog B
Sequence:
MEELEQGLLMQPWAWLQLAENSLLAKVFITKQGYALLVSDLQQVWHEQVDTSVVSQRAKELNKRLTAPPAAFLCHLDNLLRPLLKDAAHPSEATFSCDCVADALILRVRSELSGLPFYWNFHCMLASPSLVSQHLIRPLMGMSLALQCQVRELATLLHMKDLEIQDYQESGATLIRDRLKTEPFEENSFLEQFMIEKLPEACSIGDGKPFVMNLQDLYMAVTTQEVQVGQKHQGAGDPHTSNSASLQGIDSQCVNQPEQLVSSAPTLSAPEKESTGTSGPLQRPQLSKVKRKKPRGLFS
Protein: Somatostatin receptor type 4 (SS-4-R) (SS4-R) (SS4R) (SST4) (P31391)
Organism: Homo sapiens (Human)
Function: Receptor for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. It is functionally coupled not only to inhibition of adenylate cyclase, but also to activation of both arachidonate release and mitogen-activated protein (MAP) kinase cascade. Mediates antiproliferative action of somatostatin in tumor cells.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Somatostatin
- Cortistatin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Glycogen phosphorylase, brain form
- Urotensin-2
Sequence:
MSAPSTLPPGGEEGLGTAWPSAANASSAPAEAEEAVAGPGDARAAGMVAIQCIYALVCLVGLVGNALVIFVILRYAKMKTATNIYLLNLAVADELFMLSVPFVASSAALRHWPFGSVLCRAVLSVDGLNMFTSVFCLTVLSVDRYVAVVHPLRAATYRRPSVAKLINLGVWLASLLVTLPIAIFADTRPARGGQAVACNLQWPHPAWSAVFVVYTFLLGFLLPVLAIGLCYLLIVGKMRAVALRAGWQQRRRSEKKITRLVLMVVVVFVLCWMPFYVVQLLNLFVTSLDATVNHVSLILSYANSCANPILYGFLSDNFRRFFQRVLCLRCCLLEGAGGAEEEPLDYYATALKSKGGAGCMCPPLPCQQEALQPEPGRKRIPLTRTTTF
Protein: Uncharacterized protein (Q57XF3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTDPFYRLRRRCLFLFDRGAIGEALSKPDMLKRVDAILQQARQSNGVETESTSTAACGAVGTFDELCVCISRWQRRRQFADWEECLEWLLFLQERVQTPEAERDAYRWALREMITLFSEEEREYKDALSEEGVKYWRKTIISMQPYFHFTNSAQAMDVEGREGHHQVSWSIGGELSPLVRQVFLPF
Protein: PHO85 cyclin-10 (P53124)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL8, negatively controls glycogen accumulation under favorable growth conditions. The PCL10-PHO85 cyclin-CDK holoenzyme has glycogen synthase kinase activity and phosphorylates and negatively regulates glycogen synthase GSY2. Also has minor GLC8 kinase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cyclin-dependent protein kinase PHO85
- Glycogen [starch] synthase isoform 2
- PHO85 cyclin-9
- PHO85 cyclin PHO80
- PHO85 cyclin-5
- PHO85 cyclin CLG1
Sequence:
MDMTKNHTTDTEEFDDGDIRPVSLGIVDDYNASFELPLKPKFLQSENFSDLTSEWDQSRSNTPGLAEGKTEKAQPCGTTDSSKNRIHVEQLLESANEMNNYLAQNIENINNFQVGLLNGGKGLYSSMGDDSSACINGTNFSSTSNFELSDDELEDTTGCTSSIFDKDLFHQQNGLSIPRRRSPLFKSPTASFEIGDATDVEEQDIDDSIFSECSSITSFDMGGLHISLPHDEEEDQEKTKSESENPLLHGIPVDVEVPHISVDEALANFKETIELLLKLSGNRKCTGFNTRVEKKEYSNFYMKSKPTLSSADFLKRIQDKCEYQPTVYLVATFLIDTLFLTRDGNNILQLKLNLQEKEVHRMIIAAVRLSTKLLEDFVHSHEYFSKVCGISKRLLTKLEVSLLICVCNTKLMVSNRKLAASKLLLNELRSFCV
Protein: Erythroblast membrane-associated protein (Erythroid membrane-associated protein) (A0A1C9HIH9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEMASSAGSWLSGCLIPLVFLRLSVHVSGHAGDAGKFHVALLGGTAELLCPLSLWPGTVPKEVRWLRSPFPQRSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDAQEGSVTLQILDVRLEDQGSYRCLIQVGNLSKEDTVILQVAAPSVGSLSPSAVALAVILPVLVLLIMVCLCLIWKQRRAKEKLLYEHVTEVDNLLSDHAKEKGKLHKAVKKLRSELKLKRAAANSGWRRARLHFVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEPCLHDGGKNTAPLVICSELHKSEESIVPRPEGKGHANGDVSLKVNSSLLPPKAPELKDIILSLPPDLGPALQELKAPSF
Protein: Two component signal transduction system response regulator (Q8EEF6)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Sensory/regulatory protein RpfC
- histidine kinase
- histidine kinase
- histidine kinase
- Sensory/regulatory protein RpfC
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
Sequence:
MSRILLVDDDPLFRVWLTDVLKAQGHEVKCAVNGVEGLTCIRSFAPDIVMLDLVMPQMDGFELLQARECMTPIMMLSARDNEEDRIRSYELGADDFLTKPFSIKELLVRLQAIERRLVQRPKPPMAVEQVATIQSVRFDETAYKITIGKHAVELTQTEFRLFKYLFERKGQVITKQELQKSVLQKDLGRFDRNLDMHISNTRRKLANTRLPRTLINTVRGQGYSFSA
Protein: Alanine--tRNA ligase (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Q57984)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala) (By similarity). Also functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala), and maybe also from Gly-tRNA(Ala).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Leucine--tRNA ligase
- Isoleucine--tRNA ligase
- Tryptophan--tRNA ligase
- Valine--tRNA ligase
- Protease HtpX homolog
- Glycine--tRNA ligase
- Methionine--tRNA ligase
- Histidine--tRNA ligase
- Threonine--tRNA ligase
- Uncharacterized aminotransferase MJ0959
Sequence:
MKHNYKVKLFDELGFVRKKCKKCGQWFWTLDEERETCGDAPCDIYSFIGKPITKKPYTYKEMVKEFINFFKEHGHEPIKRAPVTARRWRDDILLTIASIAVFQPWITKGIVKPKANPLVIAQPCIRLNDIDNVGRTGRHLTCFTMGGHHAFNREDDFKYWQDETVELCFNFFKKLGIDEKSITFIESWWEGGGNAGPCYEVITHGVELATLVFMQYEKVGDNYKEIPLKIVDTGYGIERFVWASTGEPTIYDAIFKNIVNKLKEDAGVKDIDKEILAKITEVAGLMDVKDVGDLRKLREEVANKVNIPVEELDKLISPYEDIYAIVDHTRALAFMLGDGIVPSNVKDGYLVRMLIRKTLRHMDRLNLSTPITEIVAMQLNELKDLYPELLDMEDYIMEILEIETNKYRQTIERGKGIVERLLKSKKEIDLENLIELYDSHGLPPEIVKDVAKSLGKDVKIPDNFYTIVAERHENKKEVKEKIKLPEVNVDKTELLFYEYPKMKEFEAKILRIVDDYVILDRTAFYPEGGGQKADTGYIIKGDKKFRVVDVQKENNIVYHKIENLNDELKEGDIVKGVIDWKRRLSLMRNHTATHIINAAAQKVLGRHVWQAGSDVDVDKARLDITHYKRISREELKDIERVANEIVLNNYNIKSIFMDRNEAEEKFGFRIYQGGVVPGNVLRIVIIEDENGNIVDVQACGGTHCQNTGEVGFIKIIKTERVQDGVERLIYSSGLSALKAVQEMEDILEESAEILRCPTEELPKVIKRFFEEWKEQRKKIEELEKKIGELKKFELINKFETIGNYKVLVEKVEANPKEMLNIADNLATENAIVVLLNDKGNILCKRGENVDIKMNELIRYIAKGGGREHLAQGKYEGDVEEIKKKVIEFIKNK
Protein: Capsid polyprotein VP90 [Cleaved into: Capsid polyprotein VP70; Core protein VP34; Spike protein VP27; Spike protein VP25] (Q9IFX1)
Organism: Human astrovirus-8 (HAstV-8)
Function: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the VP70 virions. This immature virion is composed of 180 VP70 subunits with 90 dimeric spikes and displays a T=3 icosahedral symmetry. The mature virion is obtained by further cleavages resulting in three structural proteins VP25, VP27 and VP34. This forms contains only 30 spikes located on the icosahedral 2-fold axes. Plays a role in the attachment to target host cell. This attachment induces virion internalization through clathrin-dependent endocytosis.
Subcellular location: [Capsid polyprotein VP90]: Virion {ECO:0000269|PubMed:27466429}. Note=Immature capsid. {ECO:0000269|PubMed:27466429}.; SUBCELLULAR LOCATION: [Capsid polyprotein VP70]: Virion {ECO:0000269|PubMed:22743104}. Note=Immature capsid after cleavage by host caspases. {ECO:0000269|PubMed:22743104}.; SUBCELLULAR LOCATION: [Core protein VP34]: Virion {ECO:0000250|UniProtKB:O12792}. Note=Capsid. {ECO:0000250|UniProtKB:O12792}.; SUBCELLULAR LOCATION: [Spike protein VP27]: Virion {ECO:0000250|UniProtKB:O12792}. Note=Capsid. {ECO:0000250|UniProtKB:O12792}.; SUBCELLULAR LOCATION: [Spike protein VP25]: Host extracellular space {ECO:0000250|UniProtKB:O12792}. Virion {ECO:0000250|UniProtKB:O12792}. Note=Capsid (By similarity). Spike protein VP25 that lacks the core attachment region may need to dimerize with spike protein VP27 to remain stably bound to the viral particle (Probable). {ECO:0000250|UniProtKB:O12792, ECO:0000305}.
Interaction partners:
Sequence:
MASKSDKQVTVEVNNNGRSRSKSRARSQSRGRGRSVKITVNSHNKGRRQNGRNKYQSNQRVRKIVNKQLRKQGVTGPKPAICQTATATLGTIGSNTTGATEIEACILLNPVLVKDATGSTQFGPVQALGAQYSMWKLKYLNVRLTSMVGASAVNGTVVRISLNPTSTPSSTSWSGLGARKHLDVTVGKNAVFKLKPSDLGGPRDGWWLTNTNDNASDTLGPSIEIHTLGQTMSSYQNTQFTGGLFLVELSSAWCFTGYAANPNLVNLVKSTDKSVNVTFEGSAGTPLIMNVPEHSHFARTAVEHSSLSTSLSRAGGESSSDTVWQVLNTAVSAAELVTPPPFNWLVKGGWWFVKLIAGRARTGARRFYVYLSYQDALSNKPALCTGGVPASARQSNPVRTTLQFTQMNQPSLGHGATPMTFGRSIPEPGEQFRVLLTVGPPMAPNTANSQNWVNKTIVPPENQYTVKIGIDLEHYTTMQGFTPVESVSWYTADFQPSDEPSPIPGLYARVNNTKKADVYGVQQFKSSHTNNRHQITSVFLVRVTTSFQVINYTSYFIRGAESGSNVSNLKIRDQTYHTPLQFTQGKWYLLTSTVMHDGPTSSGWVWMNQELTNNIAYRVDPGMMYLITPPPAASQLYFELHTVLPQARSEEPETYVDAPLPEEPPIEEEETDSDFESTEDENDEVDRFDLHPSSESDDDDVENDRATLLSTLLNQGISVERATRITNGAFPTRAARVRRSVYNDLLVSGLSPGAAWSHACEQARRAGDNHDLQLSGSRDHAE
Protein: Cytohesin-3 (ARF nucleotide-binding site opener 3) (Protein ARNO3) (General receptor of phosphoinositides 1) (Grp1) (PH, SEC7 and coiled-coil domain-containing protein 3) (CLM3) (SEC7 homolog C) (mSec7-3) (O08967)
Organism: Mus musculus (Mouse)
Function: Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays a role in the epithelial polarization.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18042453}; Peripheral membrane protein {ECO:0000269|PubMed:18042453}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Note=Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate.
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor 1
- ADP-ribosylation factor 2
- FERM domain-containing protein 4B
- General receptor for phosphoinositides 1-associated scaffold protein
Sequence:
MDEGGGGEGGSVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
Protein: Nicotinamide riboside transporter 1 (Thiamine transport protein 71) (Q08485)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High-affinity pH-dependent nicotinamide riboside transporter which also transports thiamine with low affinity. Involved in 5-fluorocytosine sensitivity.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- High-affinity nicotinic acid transporter
Sequence:
MSFSSIVSKFLRYLEIPAKNRTAVNFLRNPDLQPIKSANQTWGFWSNLAYWGAVSFTAGTWMSGSAALSVGLSYPETIVSFLLGNVLTIIFTMANSYPGYDWKIGFTLAQRFVFGIYGSAFGIIIRILMSIVNYGSNAWLGGLSINMILDSWSHHYLHLPNTLSPSVAMTTKQLVGFIIFHVLTALCYFMKPYHMNYLLIWSCVATCFAMLGIVIYLTKNAHGVGELFTSTKSTVTGSKRAWAWVYMISYWFGSISPGSTNQSDYSRFGSSNLAIWTGSVCALLIPATLVPIFGVISASTCDKLYGKQFWMPMDIFDYWLTNNYSAGARAGAFFCGLCFTMSQMSSTISNCGFATGMDMAGLLPKYVDIKRGALFCACISWACLPWNFYNSSSTFLTVMSSFGVVMTPIIAVMICDNFLIRKRQYSITNAFILKGEYYFTKGVNWRAIVAWVCGMAPGLPGIAWEVNNNYFHDSGIVKFFYGDSFFSFLISFFVYWGLCVFFPFKITVRHDDKDYYGAFTDEEARKKGMIPYSEISEEEIRAYTLGECYTTGHEYKPESSDNESPELIKTSSENTNVFEIVHQKDDEKHSFSTTQQVV
Protein: Selenoprotein M (SelM) (Q8VHC3)
Organism: Mus musculus (Mouse)
Function: May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839807}. Endoplasmic reticulum {ECO:0000305|PubMed:11839807}. Golgi apparatus {ECO:0000305|PubMed:11839807}. Note=Localized to perinuclear structures corresponding to Golgi and endoplasmic reticulum.
Interaction partners:
- Thioredoxin reductase-like selenoprotein T
- Selenoprotein K
- Selenoprotein N
- Selenoprotein S
- Selenoprotein F
- Protein adenylyltransferase SelO, mitochondrial
- Ethanolaminephosphotransferase 1
- Selenoprotein V
- Selenoprotein H
- Selenide, water dikinase 2
Sequence:
MSILLSPPSLLLLLAALVAPATSTTNYRPDWNRLRGLARGRVETCGGUQLNRLKEVKAFVTEDIQLYHNLVMKHLPGADPELVLLSRNYQELERIPLSQMTRDEINALVQELGFYRKSAPEAQVPPEYLWAPAKPPEEASEHDDL
Protein: DNAation factor-related protein 2, isoform B (A8DY77)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DNAation factor-related protein 1, isoform B
- DNAation factor-related protein 3, isoform A
- DNAation factor-related protein 4
Sequence:
MWSNALCTLGVTKPLCNCLSIRQVAAAAAAAAQATQGVAASAAAAGGAGVGGGAITTGPSSSVTNGGLSAMESRGKRPLKIWDSWRNVRKGVVVGTFEELLVRGKDKLGVPASEPVRVVLECDGTQIEDGEYFRTLANNTVLLLLRQGERWYPTGVDVIKAAISAIPKIVCETIHALELHDETPSWKIMDNKGRVTVVLHWDQRQGGGSGGGGGGGGAGGGVGSMCSGLGSSNGLLSSDKYSPSKKGLSAQSSLDNKSVSSQSSQPRYASPQITVISDDGPASIYHPGGVVLPPGVVIPGGSRRLSKQGSSFDSTVGVGVGAVHVHTPECAHHAHTPSRAGSPSTTECDFHCCALHEEGRKIAVHKSVATSPIQDGSSSPQPQSAPSVMDPMLGGSGGGGSGSMQRRSSGAKGHVRFLDIAPERDSSESETENTVMEDDKTTTEKFLLLIDQLSVDQKRHLSIKDIGIILERLNSKILDVERLDRESESDDCYNWTIKATIRGDALRELGVIYNGNYYAISEHPGYKEELEENGEEVEEEEEEDEEDRI
Protein: Tunen (Q9NGZ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSTLRPVSVCDTTPLQRFESQSSSGEEPSSPTASSIIAAASGPNHNNNNNVKLDLQLPTFVDSTRSQGSLYAVASNKKPPLRGPRQIFGRILTDLCLLSCVGLPMLGFSLWGEAVKRGFFCDDSSLRHPYRDSTMPSWILYLMCGALPLTVMLVVEFFRGQDKRLHSPFPKSTMCSGYHLCHLELPTWLVECYHRMGIFIFGLGVEQLSTNIAKYSIGRLRPHFYTLCQPVMKDGTTCSDPINAARYIEDFTCAAVDITSKQLKDMRLSFPSGHASFACYSMLYLVIYLHRRMQWKQLRMLCHLLQFLLLMFAWYTALTRVSDYKHHWSDVLAGSGIGLTYAVVVTSTMW
Protein: Signal peptidase complex-like protein DTM1 (Protein DEFECTIVE TAPETUM AND MEIOCYTES 1) (Q7XI45)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions in tapetum development during early meiosis. May play a role in the endoplasmic reticulum (ER) membrane in the early stages of tapetum development in anthers. Seems to function after MSP1 and before UDT1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22111585}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGRDEMLRRSLVALAAAVVVTGVVTASVRKAAATYGFGILAIAGVLLPDWEFFDRDYSQWLTPMPASRRTAAEAAADREHDVWKFKPYPLRMAMLTTIYGFGLYKWWMYVSS