lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MANRTDPLAKSIHGTNPQNLVEKIVRSKIYQSTYWKEQCFGLTAETLVDKAMELDHTGGTYGGNRKPTPFLCLALKMLQIQPDKDIVVEFIKNEDYKYVRVLGAFYLRLTGTIADVYQYLEPLYNDYRKIRHKLSDGQFTLTHVDEFIDELLTKDYSCDTALPRIQKRWVLEASGTLEPRRSALEDDFEEEEEDKEEQPMEIDEPNGHENDNHRGRSPARERDRDRDRDRDRKPERHHRDRDYDRDRDYDRDYGRGRERDRDRDRERDRNRDRDRDRHRLRDDDYNRDRDRDRERDGRERERRDRDRGRHRSRSRSRDRRDRDREDGEYRRRRGRGSASPRGRGEDGGPREEPKRKKEKKEKKGEGNAPDPNDPEIIEMNKLRASLGLKPLK
The following text describes a protein:
Function:
Has a dual function as a transcriptional activator and a repressor of the hedgehog (Hh) pathway. The full-length ci form (ciFL), acts as an activator (ciA) while ciR, its C-terminally truncated form, acts as a repressor. Involved in segment polarity. Required for the normal development of the posterior half of each embryonic segment. Engrailed protein directly represses ci expression in posterior compartment cells. Essential component of a hh-signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection.
Subcellular Localization:
Nucleus.
Sequence:
MDAYALPTYFPLAYSELQFLASRRAAAVAAAATVLPGSPCINQHHPTDVSSSVTVPSIIPTGGTSDSIKTSIQPQICNENTLLGNAGHQHNHQPQHVHNINVTGQPHDFHPAYRIPGYMEQLYSLQRTNSASSFHDPYVNCASAFHLAGLGLGSADFLGSRGLSSLGELHNAAVAAAAAGSLASTDFHFSVDGNRRLGSPRPPGGSIRASISRKRALSSSPYSDSFDINSMIRFSPNSLATIMNGSRGSSAASGSYGHISATALNPMSHVHSTRLQQIQAHLLRASAGLLNPMTPQQVAASGFSIGHMPTSASLRVNDVHPNLSDSHIQITTSPTVTKDVSQVPAAAFSLKNLDDAREKKGPFKDVVPEQPSSTSGGVAQVEADSASSQLSDRCYNNVVNNITGIPGDVKVNSRLDEYINCGSISIPSNEYDCANADTTDIKDEPGDFIETNCHWRSCRIEFITQDELVKHINNDHIQTNKKAFVCRWEDCTRGEKPFKAQYMLVVHMRRHTGEKPHKCTFEGCFKAYSRLENLKTHLRSHTGEKPYTCEYPGCSKAFSNASDRAKHQNRTHSNEKPYICKAPGCTKRYTDPSSLRKHVKTVHGAEFYANKKHKGLPLNDANSRLQQNNSRHNLQEHNIDSSPCSEDSHLGKMLGTSSPSIKSESDISSSNHHLVNGVRASDSLLTYSPDDLAENLNLDDGWNCDDDVDVADLPIVLRAMVNIGNGNASASTIGGSVLARQRFRGRLQTKGINSSTIMLCNIPESNRTFGISELNQRITELKMEPGTDAEIKIPKLPNTTIGGYTEDPLQNQTSFRNTVSNKQGTVSGSIQGQFRRDSQNSTASTYYGSMQSRRSSQSSQVSSIPTMRPNPSCNSTASFYDPISPGCSRRSSQMSNGANCNSFTSTSGLPVLNKESNKSLNACINKPNIGVQGVGIYNSSLPPPPSSHLIATNLKRLQRKDSEYHNFTSGRFSVPSYMHSLHIKNNKPVGENEFDKAIASNARRQTDPVPNINLDPLTNISRFSTTPHSFDINVGKTNNIASSINKDNLRKDLFTVSIKADMAMTSDQHPNERINLDEVEELILPDEMLQYLNLVKDDTNHLEKEHQAVPVGSNVSETIASNHYREQSNIYYTNKQILTPPSNVDIQPNTTKFTVQDKFAMTAVGGSFSQRELSTLAVPNEHGHAKCESFHHQSQKYMNTDIGSKQQSALPSAHQRQTEKSNYNQIIDSSMTSLPELNVDSIYPRNETENIFKVHGDHDNEIQCGIISQSQMSPSTNLNNDGQFSTVNMQPITTSKLFPPEPQKIVCDTQASNTSVMHLDTYQRTLEYVQSCQNWMETNNTSTNQIQSLPGMPVNNTLFPDVSSSTHPYHGTNMVINDMTTSLTSLLEENRYLQMMQ
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC).
Subcellular Localization:
Nucleus, nuclear pore complex.
Sequence:
MPEYTNFESKFDDIDMLEIPEDDDGENSIDNSISSETEGISDSSDSSKSSYDQWSPVAIFKSDKEYIDLSDWLNTQKSLEFKFDVQKYRKGIEKSRPFDEKYILYVNNMFKIIQKLTEDDITRFDLEEDDSPIGLVMDSMGSKAKQVRKFKKIDEALREIIDYLQDLVNSIPKEEQESYDSQCLQHVLYILECFEANNFYFDIQQKPELIIKWVNTFDPKPDPELLNDVIVNTPQPYLHPRFWNTCISQLLTRGLFTQIHEVIEHSQYQELKEKCPELYAVIGDMDTLLSNYTSYSSKGQFTAWKLLACEFRDSLSSVRNESITETKHKLIIDQIYDLACIFTGLPKTISSYCDTWYEVYLALSLYQVRDSNEVYIDYFKTAVSEKPPSDIFDDENENLDGLTEACFLNILENNFLKVLETLHELDPPTTAYLAELMELRFLLRGYYFDVTVTSSASFEDLLNRRIVSEYFLTRHAYDCLNIHELVPVGIGLLLNNVVCTSNNAVSANRKVIATFLPNYICNTNDDLEWALTICANLNLVSTARQLYYQAGLKSLEEGYMYEALNNFVNCYDPTLLSGENHSEGMKKVHYIVWDLIFANCLVHNRPIKDELINNIVDKKVDLNFKIHPVIQQCLAPYAVLKEFYETLPQRDIKLSNKLSKLIHLLKFNYLPKKFVPLLLAQFIPFLSEPNTTFQLPDLVIIIELLDNYESDRNEKELKEGADLYLYSINNIESDADENDWRKLVGKDNLPKDIDSFTRLLRNLIAAKVGKVFI
The following text describes a protein:
Function:
May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Subcellular Localization:
Lipid droplet. Membrane; Multi-pass membrane protein.
Sequence:
MADHHRGATGGGGGYGDLQRGGGMHGEAQQQQKQGAMMTALKAATAATFGGSMLVLSGLILAGTVIALTVATPVLVIFSPVLVPAAIALALMAAGFVTSGGLGVAALSVFSWMYKYLTGKHPPGADQLDHAKARLASKARDIKDAAQHRIDQAQGS
The following text describes a protein:
Function:
Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGNASNDSQSEDCETRQWLPPGESPAISSVMFSAGVLGNLIALALLARRWRGDVGCSAGRRSSLSLFHVLVTELVFTDLLGTCLISPVVLASYARNQTLVALAPESRACTYFAFAMTFFSLATMLMLFAMALERYLSIGHPYFYQRRVSRSGGLAVLPVIYAVSLLFCSLPLLDYGQYVQYCPGTWCFIRHGRTAYLQLYATLLLLLIVSVLACNFSVILNLIRMHRRSRRSRCGPSLGSGRGGPGARRRGERVSMAEETDHLILLAIMTITFAVCSLPFTIFAYMNETSSRKEKWDLQALRFLSINSIIDPWVFAILRPPVLRLMRSVLCCRISLRTQDATQTSCSTQSDASKQADL
The following text describes a protein:
Function:
Endoplasmic reticulum-anchored protein that mediates the formation of contact sites between the endoplasmic (ER) and endosomes, mitochondria or Golgi through interaction with conventional- and phosphorylated-FFAT-containing organelle-bound proteins. In addition, forms endoplasmic reticulum (ER)-lipid droplets (LDs) contacts through a direct protein-membrane interaction and participates in LDs homeostasis. The attachment mechanism involves an amphipathic helix that has an affinity for lipid packing defects present at the surface of LDs. Promotes migration of primary monocytes and neutrophils, in response to various chemokines.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Note=Localization to contact sites involving the endoplasmic reticulum and several organelles is regulated by interaction with proteins containing FFAT motif. Dynamically distributes between specific subdomains of the endoplasmic reticulum (ER): ER membranes in contact with lipid droplets (LDs) and the remainder of the ER.
Domain:
The MSP domain is required for binding to the FFAT motif of target proteins; The CRAL-TRIO domain is necessary for the recruitment to lipid droplets (LDs) and mediates the formation of ER-LDs contacts through an amphipathic helix; The transmembrane domain is necessary for binding to LDs.
Sequence:
MAENNAQNKAKLISETRRRFEAEYVTEKSEKYDSRDVERLQQDDNWVESYLYWRHNVVDETLKMLDESFQWRKEFSVNDLSESSIPRWLLELGGIYLHGYDKEGNKLFWIRVKYHIKDQKTIMDKKKLIAFWLERYAKRENGKPITVMFDMSETGLNSIDMDFVRFIINCFKVYYPKYLSKIVIFDMPWIMNAAFKIVKSWLGPEAVSLLKFTSKNEIQEYVSVEYLPPHMGGTDPFKYSYPPLVDDDFQTPLCENGPIASEDETSSKEDIEGDGKETLETISNEEPPALSEKSNPTESVSKKDENEKVDSKTKTFKKPLSVFKGPLLHISPAEELYFGSIESGEKKTLIVLTNVTKNIVAFKVRTTAPEKYRVKPSNSSCDPGASIDIIVSPHGGLTVSAQDRFLIMAAEMEQSSGTGPAELSQFWKEVPRNKVMEHRLRCHTVESSKPNSLMLKDSISTMSDKTSEDLYLQLNRLLESNRKLEDQLQRSIWFQQLLLALTMVLLDFVVSFFYSLYN
The following text describes a protein:
Function:
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
Miscellaneous:
MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Sequence:
MNKIQHISFITKKNPLVSYERVGALQNRFVQHYLNYKANKVEQPPKPTIITSQVCPVYTLGRRESSINFTKGFPKAKVVKALRGGQTTFHGPGQILAYPIIDLKSFGLSPREYVSRLEQAIIATCKSFGIEKAHTTKNTGVWVTENDKIAAIGIHLRRNITSHGLALNVSTDLKYFNYIVGCGLYGKNTTSFKDQGVFTDLKSVEKVLVNNLDSFLMSK
The following text describes a protein:
Function:
GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium.
Miscellaneous:
MISCELLANEOUS: Platelet activation apparently involves disruption of the macromolecular complex of GP-Ib with the platelet glycoprotein IX (GP-IX) and dissociation of GP-Ib from the actin-binding protein.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MALLILLFLLPSPLHSQHTCSISKVTSLLEVNCENKKLTALPADLPADTGILHLGENQLGTFSTASLVHFTHLTYLYLDRCELTSLQTNGKLIKLENLDLSHNNLKSLPSLGWALPALTTLDVSFNKLGSLSPGVLDGLSQLQELYLQNNDLKSLPPGLLLPTTKLKKLNLANNKLRELPSGLLDGLEDLDTLYLQRNWLRTIPKGFFGTLLLPFVFLHANSWYCDCEILYFRHWLQENANNVYLWKQGVDVKDTTPNVASVRCANLDNAPVYSYPGKGCPTSSGDTDYDDYDDIPDVPATRTEVKFSTNTKVHTTHWSLLAAAPSTSQDSQMISLPPTHKPTKKQSTFIHTQSPGFTTLPETMESNPTFYSLKLNTVLIPSPTTLEPTSTQATPEPNIQPMLTTSTLTTPEHSTTPVPTTTILTTPEHSTIPVPTTAILTTPKPSTIPVPTTATLTTLEPSTTPVPTTATLTTPEPSTTLVPTTATLTTPEHSTTPVPTTATLTTPEHSTTPVPTTATLTTPEPSTTLTNLVSTISPVLTTTLTTPESTPIETILEQFFTTELTLLPTLESTTTIIPEQNSFLNLPEVALVSSDTSESSPFLNSDFCCFLPLGFYVLGLLWLLFASVVLILLLTWTWHVTPHSLDMEQSAALATSTHTTSLEVQRARQVTMPRAWLLFLQGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGRGQDLLGTVGIRYSGHSL
The following text describes a protein:
Function:
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs) (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MKNKILFSFSNPMNSNSSNNIENNNNSNNNNNNFKNNFKNFSRKRTNDIEIEDNITFSELLLQKEVLKGLEDGGYQRPSPIQLKAIPLGISGVDLIAQAKSGTGKTIVFGVIALECVLRESKLLRQKQELNKTQLTNQTNKQLLEMDDDTYVETMVGIIRKPLVLIIAPTREIAVQIKDVIKSISKYCKRIKCEVFIGGLNSNNNKDENNNNILNNEDVNRLNGTQIIVGTPGKIKSLIENLHLRTDTLKMVIMDEADKLLDASFSKTINWIYSAIGNGNSNKNNSSSGSGIQMLAFSATYPSYLINLLKLYMNNENLVEIRLCSDTPSLEGIKQYYQIFRNDFTENNYKTFQNKCKSLVLVLEQVSFYQAIIFCNHKIRGEELTRQLNREGWPTAFIAGGQNQKDRLSTMSALKSFNIRILVSTDLISRGIDVERVNLVINLDLPKDHETYFHRIGRTGRFGTYGVSITFINMKSIQQQQQQQQQQQQQIENENENENNNNNEGFQEIDFINQLIQEYSVDITERVDNDIIPEELYSYQLSNPNDQQSLANLKLKQQQTILLNKQLEELKINENENENQYQNEDEEEEQEEDDYHYENQHQNEDEEEEQEEDDYHYENQHQNEEEEQEQQEEDDDNYNYENDNDSEEYEFIDDSIIEQTEYYYLNSNNNNNNNKNKYGNTINNNHYRNSSFNGPKNSINNNKFKNKNINNNDQRNSQSNGIKKKVNTNNNNFYPHYYNNPYPQNYYYDYQYFSDNSYYNNNYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNYYQQHGNNPYGYNIPNSIQYSSNQFYYCTCPNCPTMNYHQYI
The following text describes a protein:
Function:
Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways.
Subcellular Localization:
Nucleus.
Sequence:
MPRIDRRLWHPITSCKKVKGKRPGDEKNLEHVRRIRVMYNDPDATDSSSSDDEGMYIAEGGMFKQNKQVIKEIVIPVNSHKSSGEGCSRANNGSQKYISISKKFGCAASARQEKNNVPPTPSEYRGVRRRPWGKYAAEIRDPIRKVRVWLGTFNTAEEAALAYQRKKLEFDALSVPGKNNTTCQHLTGPAFLVPSPSSVLDVPSSSSSGNRHEVSALEQRGKDKVQIFGNARSEPHLDDDSCIQEFLLEPVPSMSITEEFYCAEEFYCGGLDKNLLLQDESDDVLQDGIAGTDENLGEGEFGEGEFGEDKMHDLANIEINLDKEELAWIDEALNFPSL
The following text describes a protein:
Function:
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Sequence:
MSSREEVVNFAAGPAAMITSVVEEFGKDFVNFQGLGMGVAEISHRSKQGSGIVTSAESNFRKLYNIPENFHILFMQGGGTEQFAACLYNVYAHHALKNGNAKSLVANYIITGAWSKKAYAEAERLGFPCHVAVDMKELAGKYGSLPEDKDLKFTPDGETSLVYYCDNETVHGVEFNEPPTNIPKGAIRVCDVSSNFISRKIDFTKHDIIFAGAQKNAGPAGITVVFVRDSVLARPTPAELHKLNIPVSPTVSDYKIMADNHSLYNTLPVATLHAINLGLEYMLEHGGLVALEASSIEKSKLLYDTLDKHDLYISVVEPAARSRMNVTFRIEPQELESEFLAEAEKHHLVQLKGYRSVGGIRASLYNAISVEQTRRLIDLLESFAKAHSN
The following text describes a protein:
Function:
Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Subcellular Localization:
Cytoplasm.
Sequence:
MERPQLPQGLPADIERKKAEAKAWFESLRDTICADFEAIEDDLAGPLSDRPAGRFVAKDWLRDEGNGGGGRMSMMEGRVFEKVGVHTSTVFGEFSPEFRDQIPGASEDPRFWASGISLIAHPVNPNVPAVHMNTRMVVTTSNWFGGGADLTPVLDRRRIPTDADTVLFHRAMEIACNRHKVADYPKFKQWCDEYFYLKHRNEPRGTGGIFYDWLRSDEEIGGWEADFAFTRDVGKAFAIVYPRIVRTNFNMPWTEQDRSEQLVRRGRYVEFNLLYDRGTIFGLKTGGNVESILSSLPPLVRWP
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that methylates elongation factor 1-alpha.
Subcellular Localization:
Cytoplasm.
Sequence:
MVSSELHKLSYWEEIYINEKKNYEESNIELEEWFEENCDKIMNWIDNKFSQNEEKKNITILDIGCGNGLFLYKLYEKGFMNLYGFDFSSTAIELAKTIFENSPIYVEVMDICLIDKEIQNSKLNKNYNLINDKGTFDVFFMNNKTNEYFKQISYFLQTNTFFCITSCNACKDELLQIINEFNKNNLKSELVLIDEIFYETITYAGIKGQLITTLIFKCK
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MLASLFSLSLCAANIRNTKVERQYKITDGFVAVSLDITFTNFGDKATSEYVLSFDPREAAHMNTVIAVMNRKHIRNTQKSLVIKDQNGQKVVTLLSPLEPGASQTIYVGYTIGQYILFTTNGVTLKNLRVDCYFNTTIGFVSPYQTEEVSLEISGISKNSVTSMTKNLDITQKSNTISMQSIKTVPKNNELYVEYFIYKALPYVSAVNTSTHISHWGISKQESFMEVHNDGPEFVGEFNRIDFRESSNCYFQTVPVRPPADSYHFWANDESGQLQREINLEDKDLSIPLRGPVLPSWKVTYTTGWTVKTSNFVRTEGNTYIFSAPLFPKPYADRGVSVSHIRSEYVFPEGAEIKKITYPQAINGRHHFGQEVCNLDFKGRSVVVIEADRLSSIDETTVQIEYTIEGKYALYKIAYLSAGFGAIFLAIVVLRKIDLSIPSFEKKN
The following text describes a protein:
Function:
May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein.
Sequence:
MVCKVLIALCIFTAGLRVQGSPTVPLPVSLMTKSSAPVATWTTSAPHTARATTPVASATHNASVLRTTAASLTSQLPTDHREEAVTSPPLKRDVNSTDSSPAGFPSTSSDGHLAPTPEEHSLGSPEATVPATGSQSPMLLSSQAPTSATTSPATSLSESLSASVTSSHNSTVANIQPTEAPMAPASPTEEHSSSHTPTSHVTAEPVPKEKSPQDTEPGKVICESETTTPFLIMQEVENALSSGSIAAITVTVIAVVLLVFGGAAYLKIRHSSYGRLLDDHDYGSWGNYNNPLYDDS
The following text describes a protein:
Function:
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Sequence:
MSQEKISEIIKDISALKTSCEKLNSQLDELITQKVENEMLLEEVKVLEDDSVLHKLVGLVLVKEEKSKCYDTISRRLQYITGEIENRKKVITNSEEKLRKLFSDLEAHAGQRKIPVPQA
The following text describes a protein:
Function:
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MDCHISILLFLICSARSCFGELILQPTNEVNLLDSKAIQGELGWISYPAHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEVREVGPVSRKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEEPPRMYCSTEGEWLVPIGKCLCNAGHEERGYVCQACRPGFYKASAGNLKCSKCPPHSSTQEDGAVDCRCENNYFRADKDPPSMACTRPPSAPRNVISNINETSVILDWSWPLDTGGRKDVTFNIICKKCGGSVRQCEPCSSNVHFLPRQFGLSNTTVTVIDLLAHTNYTFEIDAVNGVSDMSSSPRQFAAVTITTNQAAPSPVTIIRKDRTSRNSVSLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISGLKPDTTYVFQIRARTAAGYGTNSRKFEFETSPDSFSISSENSQVVMIAISAAVAIILLTVVVYVLIGRFCGYNKSKHGTEEKRLHFGNGHLKLPGLRTYVDPHTYEDPNQAVHEFAKELDATSISIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTDKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTSPEAIAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPPPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPSSLKIITNAAARPSNLLLDQSSVDIPGFRTPGDWLNGIRTGQCKDIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETHTKNGPVPV
The following text describes a protein:
Function:
Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), and autophagy of large cargos including mitophagy, pexophagy and glycophagy.
Subcellular Localization:
Cytoplasm. Membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Note=Endosome and other perivacuolar punctate structures.
Domain:
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Sequence:
MAVIDQDNFSNISWHSEQNAESAASTAQVHHESNSSPEYARSGPDDGRPGDNAAGMEHDELDHSGGEILDCTVSDPHKENDGTKDAYVSYLITTNTTFPSFQKPKTTVRRRFTDFVFLYKVLCRDYQACAVPPLPDKQRMEYVRGDRFGTDFTARRAYSLQRFLARLALHPILRKADILHAFLESPDWNATMRSRSVRGSLASPGGIGDSTLGGSAAAGGGGGVFDTFADSFMNAFTKVHKPDRRFIEIKEKSDKLDEDLNHIEKVVARVARREADIESDLKDLAEQFQKLITLEPGVETAVRAFAASVEDTASGLKKLKDHTDQDYLGSLRDMVAYSGTLKNLLKAREQKQLDYEQLTEYLNKSRTDRDMLASGQSYGAGSALMSGAGGFIRSKIEDVRGVDHEQARRDRQRKLELRIEELTREVEVARNESESFAEQVSREVESFDWIKRVEFKRQFSGLADAHIEFYGDVMSVWEQYVMEMEKEGVVLPA
The following text describes a protein:
Function:
Has a role in the control of cell polarity and cytokinesis. Involved in bipolar growth, via modulation of cdc42-shk1-orb6 signaling, and septum formation. Stimulates guanine nucleotide exchange of cdc42.
Subcellular Localization:
Cytoplasm.
Sequence:
METLKADLSDMSDSPEYFETLANRDLPRLPGTSKLHRAACIKRKSINLSLPSNSYSLSYRQSDDTDGDVSESQSEYRLSSGRRSRASFARALQDPQTPNTPPVSSQHRRFFSEGSFNLPNSNMSHSLNGDSTASNSSTLTPNRIYGDRNRQDYAQSSRYTLPSLPSSPSYNCPTTLRKIHTNTSSNGTSRRVSGLGSFMAQNSSETSSNRTSAYLPGSSTDEQEKRSSVTLASMPSSHSSTASLLSPLDTTSFSTKLDSTILALETDESLSRTISYATTSLPSTPGKRLSKESLAMSEASSINPEYKRIKKRANLIKELVTTEAAYLNDLIAIQQSYGLRVKECSALNPVDAQTVFGDIESLLTFTVEFHSRLYQAGEGSWRVNLDTQLIDPLPCNLGLIFLESLSEIGQIYTGYCNRQDSVFKIITKWREKPATASWIMEGDKIVQKYTNAWDLGSLIIKPLQRLLKYPLLLQKIIDVTPESSSERPDLVLSYQLLQELISGINQKQKPSHKRGSLSASHKRDAAWSLLYKATSNKSRPTTTSTELKTDARLNFQRQVLQDFRQRFAILKALHATLETWYVTVHRGFSVFEKVLAELEGLSALEPEDKPVDTWRKYHLLAHMMTANLPSQIQTSLNSSILNPITNILRVIQKVIQFIISAEFVIPAQKLEAISTLVEKEFHSVVYHFIGIQRSLYENYAQGFLFLIPQDMRDSILEETQDYAELVRAFEPMHYDDEVLLEELMKSVSLAARV
The following text describes a protein:
Function:
Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion.
Subcellular Localization:
Secreted.
Sequence:
YAEGTFISDYSIAMDKIRQQDFVNWLLAQKGKKSDWKHNITQ
The following text describes a protein:
Function:
Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Replication factor C (RFC) complex has an essential but redundant activity in sister chromatid cohesion establishment. Acts as a PCNA loader, loading PCNA onto primed templates. An RFC-like complex (ctf18-RFC) is formed where ctf18 replaces rfc1 in the RFC complex along with the association of dcc1 and ctf8. This complex is required for efficient establishment of chromosome cohesion during S-phase.
Subcellular Localization:
Nucleus.
Sequence:
MDSIPNEDDLEKLLVAEQNVPYGKNYESFEDEENYLLELRNANALENLEHRSIPNDLFHSSQPVGSPTRNGDDIPSTLDLYSSDNAAIDTDISEDETINQRHAPQTDYRYPNTSANPKMGLEESMDIDMPSIDLDISNAAAFPRDSNLLFRNYNSHTKTSEKGSPVNFEKENQDSNVLFSTGRTSVLHIDAEQSQTNNTVTPLKDDALSLFSFENDVNGAVNDNSLDQKLSASKNSQRVSLPFFSKIELDEGSSFSGPKISARTSSGKIIYFPKKKNRHSDGLLLQPKRLADEISQVNEIGKDFNQDLLNSVRIWSENFLIVSKEKSVALKTEKLDSLQITNCTTKPQSQKLWVDTYRPQLFRDLLGDERVHRAAMHWIKAWDPCVFGKSRLQPSKSMRFNPRFTNITSDSDRPDKRIMMLTGLAGAGKTTLAHVIAHQAGYKVLEINASDDRTAHTVHEKVSSAISNHSALSSQPTCVIVDEIDGGDPAFVRALLSLLESDEKATEYSQAGNSKKKKKFKKLCRPIICICNDLYTPALRPLRPYAQIIYFRPPPQASLVGRLRTICRNENIAVDSRSLTLLTDIYNSDIRSCINSLQLLSLNNKRIDSETIKLLQPKSNSFSTSSLIQSLFLQLDNKQIRAIEASQPTYSHLDALLARIDGANDSESVLMNCFHTYLDLPFTDSLLSKPALTSEWLYFFDQLHSQCYKGNYELWRYIPYSIIHFHYLYATPEKCRLPHPPRSDLEALKLYRTRKEILDSFISTLNAYENQMHGERSILLELIRTILITINPTLKQKEDSMPRSALPSKIEHAINILNHYNLRFQQLPVGDGNYVYRLEPPLDELVWDAPTSSYSVRQMLSQELLKKRLADIKKQTLTDNPTSSNSSRKRKDFNSGKAIKRDFFGRIISEPKSEAVTSNNAALNTGDHPVSIKHAINIKFHDGFSNAVRKPISLNEILNF
The following text describes a protein:
Function:
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Miscellaneous:
MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.
Subcellular Localization:
Cytoplasm.
Sequence:
MAELPQSRINERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGMTPDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGNFGSMDGDGAAAMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSVLPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAELMEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQRIVVTEIPFQVNKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDVRKDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQKTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAMESLQQRFKLSEKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELEAILADEEVLLQLVRDELTEIRDRFGDDRRTEIQLGGFEDLEDEDLIPEEQIVITLSHNNYIKRLPVSTYRAQNRGGRGVQGMNTLEEDFVSQLVTLSTHDHVLFFTNKGRVYKLKGYEVPELSRQSKGIPVVNAIELENDEVISTMIAVKDLESEDNFLVFATKRGVVKRSALSNFSRINRNGKIAISFREDDELIAVRLTSGQEDILIGTSHASLIRFPESTLRPLGRTATGVKGITLREGDEVVGLDVAHANSVDEVLVVTENGYGKRTPVNDYRLSNRGGKGIKTATITERNGNVVCITTVTGEEDLMIVTNAGVIIRLDVADISQNGRAAQGVRLIRLGDDQFVSTVAKVKEDAEDETNEDEQSTSTVSEDGTEQQREAVVNDETPGNAIHTEVIDSEENDEDGRIEVRQDFMDRVEEDIQQSSDEE