lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Muscle-derived dendritic guidance cue, which is required for the formation of somatosensory dendritic arbors which extend from PVD and FLP sensory neurons during development. Ligand of a multi-protein dma-1 receptor-ligand complex, which is activated upon binding of lect-2, mnr-1 and sax-7 ligands to control the growth of dendrites that extend anteriorly from the PVD neuronal cell body. Enhances the binding of the mnr-1 and sax-7 ligands to the dma-1 receptor-ligand complex. Restricts the growth of secondary PVD dendritic branches and any irregularly positioned ectopic tertiary dendritic branches that originate from secondary branches, and promotes the formation of stable higher order dendritic branches. In particular, it is required for the formation of quaternary PVD dendritic branches and promotes their innervation of body wall muscles. Promotes self-avoidance of tertiary dendritic branches of PVD sensory neurons. Not required for the growth of dendrites that extend from AIY and PVQ interneurons, DVB GABergic neurons, PLM and ALM mechanosensory neurons, AFD sensory neurons and DD/VD and DA/DB motor neurons.
Subcellular Localization:
Secreted. Cell junction. Secreted, extracellular space, extracellular matrix, basement membrane. Cell projection, dendrite. Perikaryon. Cell surface. Note=Secreted by body wall muscles and taken up by coelomocytes. Localizes to the basement membrane of hypodermal tissues, body wall muscles and along fibrous organelles in larvae and adults. Co-localizes with sax-7 at dendrites. Dendritic localization is dependent on sax-7, but not mnr-1 or dma-1.
Sequence:
MHLRTLHFLILIGIFIGGQTLGCMKKVCGNNAKNDFRRCPDTDGSCGNYHTERTSGEIIDGVDVRCHLGEPIYAPIEGEMYFWRPYGGKREKSCADQGVRIEGTGQWQGYAVHISSVKLSFFGGHVEAGDEIGEALNRYCFNDRGQNDVEPHVEIRLYKEGRLIDPTHHLQNCMCTGQICESNTRNVLLGDPFKTDKRYNGVRGWDVECQMIDDDDEDSPRAPMIYSPIAGEIVGRIRLFTDSNGAYTGCDNDGIFIVGIDDWLGFEARLYNVKARADIGFGRKRIIQGEPIATRLACENSPDSVFVEIRFEGRVVNITDIITAANCKTPNFPVF
The following text describes a protein:
Function:
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing, maturation and degradation events. In vitro, is a processive phosphorolytic exonuclease and requires a single-stranded poly(A) tail on the substrate RNA for its activity (By similarity). Plays an important role in seed germination and early seedling growth by mediating specific cytoplasmic mRNA decay of transcripts coding for the abscisic acid (ABA) biosynthetic enzymes NCED5 and NCED6, and the ABA signaling transcription factors ABI3 and ABI4.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAAKPGAATPTYSPKIVGRSRLPIFKDSDLDWSRPDGRGFHQCRPALLQTGAVSSASGSAYAEFGNTKVIVSVFGPRESKKAMVYSDVGRLNCNVSYTNFASPTLGQGTDHKEYSSMLHKALEGVIMMETFPKTTVDVFALVLESGGSDLSVLISCASLALADAGIMMYDLITAVSVSCIGKSLMIDPVTEEEGCEDGSFMMTCMPSRYEITQLTITGEWTTPNINEAMQLCLDASSKLGEIMRDCLKQSASASDE
The following text describes a protein:
Function:
Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis. Plays a role in ergosterol synthesis. Binds and transports sterol. May be involved in ergosterol transport from the plasma membrane (PM) to the ER.
Miscellaneous:
MISCELLANEOUS: Present with 1690 molecules/cell in log phase SD medium.
Subcellular Localization:
Vacuole membrane. Bud neck.
Domain:
The OSBP-related domain (ORD) mediates binding of sterols and phospholipids. It displays an incomplete beta-barrel containing a central hydrophobic tunnel that can accommodate a single lipid molecule with a flexible lid covering the tunnel entrance. The ORD can bind two membranes simultaneously. It has at least two membrane-binding surfaces; one near the mouth of the lipid-binding pocket and a distal site that can bind a second membrane. These structural features correlate with the phosphatidylinositol 4-phosphate (PI(4)P)-coupled lipid transport optimized in closely apposed membranes, such as organelle contact sites. The lipid transfer cycle starts from the association of the LTP with a donor membrane, which accompanies conformational changes that uncover the ligand-binding pocket. The tunnel opening is generally mediated by displacement of the lid covering the binding pocket allowing uptake or release of a lipid molecule. The LTPs extract the lipid from the membrane by providing a hydrophobic environment as well as specific interaction. Dissociation from the donor membrane shifts the conformation to a closed form. Then, the LTPs loaded with a cargo lipid diffuse through the aqueous phase. Lid opening may be induced by the interaction of a hydrophobic side of the lid with the target membranes.
Sequence:
MSQHASSSSWTSFLKSISSFNGDLSSLSAPPFILSPTSLTEFSQYWAEHPALFLEPSLIDGENYKDHCPFDPNVESKEVAQMLAVVRWFISTLRSQYCSRSESMGSEKKPLNPFLGEVFVGKWKNDEHPEFGETVLLSEQVSHHPPMTAFSIFNEKNDVSVQGYNQIKTGFTKTLTLTVKPYGHVILKIKDETYLITTPPLHIEGILVASPFVELGGRSFIQSSNGMLCVIEFSGRGYFTGKKNSFKARIYRSPQEHSHKENALYLISGQWSGVSTIIKKDSQVSHQFYDSSETPTEHLLVKPIEEQHPLESRRAWKDVAEAIRQGNISMIKKTKEELENKQRALREQERVKGVEWQRRWFKQVDYMNENTSNDVEKASEDDAFRKLASKLQLSVKNVPSGTLIGGKDDKKDVSTALHWRFDKNLWMRENEITI
The following text describes a protein:
Function:
Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Required for progression of S phase. The complex CDC7-DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53' and then is involved in regulating the initiation of DNA replication during cell cycle.
Subcellular Localization:
Nucleus.
Sequence:
MNSGAMRIHSKGHFQGGIQVKNEKNRPSLKSLKTDNRPEKSKCKPLWGKVFYLDLPSVTISEKLQKDIKDLGGRVEEFLSKDISYLISNKKEAKFAQTLGRISPVPSPESAYTAETTSPHPSHDGSSFKSPDTVCLSRGKLLVEKAIKDHDFIPSNSILSNALSWGVKILHIDDIRYYIEQKKKELYLLKKSSTSVRDGGKRVGSGAQKTRTGRLKKPFVKVEDMSQLYRPFYLQLTNMPFINYSIQKPCSPFDVDKPSSMQKQTQVKLRIQTDGDKYGGTSIQLQLKEKKKKGYCECCLQKYEDLETHLLSEQHRNFAQSNQYQVVDDIVSKLVFDFVEYEKDTPKKKRIKYSVGSLSPVSASVLKKTEQKEKVELQHISQKDCQEDDTTVKEQNFLYKETQETEKKLLFISEPIPHPSNELRGLNEKMSNKCSMLSTAEDDIRQNFTQLPLHKNKQECILDISEHTLSENDLEELRVDHYKCNIQASVHVSDFSTDNSGSQPKQKSDTVLFPAKDLKEKDLHSIFTHDSGLITINSSQEHLTVQAKAPFHTPPEEPNECDFKNMDSLPSGKIHRKVKIILGRNRKENLEPNAEFDKRTEFITQEENRICSSPVQSLLDLFQTSEEKSEFLGFTSYTEKSGICNVLDIWEEENSDNLLTAFFSSPSTSTFTGF
The following text describes a protein:
Function:
Sugar proton-coupled antiporter which contributes to vacuolar sugar import (e.g. monosaccharides including glucose, sucrose and fructose), particularly during stress responses (e.g. in response to cold). Required for cytosolic glucose homeostasis.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MKGATLVALAATIGNFLQGWDNATIAGAMVYINKDLNLPTSVQGLVVAMSLIGATVITTCSGPISDWLGRRPMLILSSVMYFVCGLIMLWSPNVYVLCFARLLNGFGAGLAVTLVPVYISETAPPEIRGQLNTLPQFLGSGGMFLSYCMVFTMSLSDSPSWRAMLGVLSIPSLLYLFLTVFYLPESPRWLVSKGRMDEAKRVLQQLCGREDVTDEMALLVEGLDIGGEKTMEDLLVTLEDHEGDDTLETVDEDGQMRLYGTHENQSYLARPVPEQNSSLGLRSRHGSLANQSMILKDPLVNLFGSLHEKMPEAGGNTRSGIFPHFGSMFSTTADAPHGKPAHWEKDIESHYNKDNDDYATDDGAGDDDDSDNDLRSPLMSRQTTSMDKDMIPHPTSGSTLSMRRHSTLMQGNGESSMGIGGGWHMGYRYENDEYKRYYLKEDGAESRRGSIISIPGGPDGGGSYIHASALVSRSVLGPKSVHGSAMVPPEKIAASGPLWSALLEPGVKRALVVGVGIQILQQFSGINGVLYYTPQILERAGVDILLSSLGLSSISASFLISGLTTLLMLPAIVVAMRLMDVSGRRSLLLWTIPVLIVSLVVLVISELIHISKVVNAALSTGCVVLYFCFFVMGYGPIPNILCSEIFPTRVRGLCIAICAMVFWIGDIIVTYSLPVLLSSIGLVGVFSIYAAVCVISWIFVYMKVPETKGMPLEVITDYFAFGAQAQASAPSKDI
The following text describes a protein:
Function:
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit is less well bound than the others.
Subcellular Localization:
Cytoplasm.
Sequence:
MMDLAERGPQNRRALTLAEVKALVFDRWSSSVESLTLDQRRLLIYLSKFTKVSDPKRAREAVEELMNRFKLKEEHAVMIVNILPEDEEELRAYLFKDYPLLSQQDYKEMLNLLKSLRE
The following text describes a protein:
Function:
Activates the atg1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, atg13 is also required for glycogen storage during stationary phase (By similarity).
Subcellular Localization:
Cytoplasm. Preautophagosomal structure.
Sequence:
MHQHPRSPAPAAPTSSTRSNRSTDHRELDTDPSSPSSDVRMHNGRGLGIEPETEPSEQVQRNTQPAKEAMAKLNQIITFNVEIEDTDILREQLRIWRTCDAIENRPPPLIIETYLETKGLTNNQSLVILDENGKRWDVLEALTASGQASPVRPPHSNSDDVILERWRVELGSASSKPPSDLGSILPTVYKKSIVLFRSLFTYSKFLPAWKFAKRNGRLRSNPALQIRYRILDGRTASDRRQVDHLTVPLYEGNTKVVETYSFGVTDSPAGPFSVEVTYRTNCDFRVDDSEALLSSRFMGADDEIFRPSFPSRDANRRASNAEPGSAPLEKRTVEEPDPGRAYGSLSTFHHVGPATGASPISALRAARESVTSSPSPPSSASRRPLSAARAAPTGRAAALAAEASPSPLRRPSISFQPFKAPPLSASPSLIDPPLGASPRSRPIVSAPSSEPKHMPPPSVAASGRKTGQAASENAIASSNSASPRPAPIARYSSAFSHRRGRPSSGGINKIEDDASSGKASATSSGAQPGSGLLAEVTGTSADSLHADDENISEFLKMLDLRKDLLSPSNLSNLDAVARRTTVTSAALTRFQRMRDSNAALSESMSSSLLLQRSSNASSKQLSGVPPMVAGASVSTASSPGKPISPHTPHTPAIPSRLSSNSIVDYNDHGHSDGRLLHGGPTSLPEDTTGEETALVHRPPTVTAIDIPTSPRLFPPTYRRSSSAAQNRRSVVADEEEIFPFNMRSVSLGAEERTNVSLSTLHRRHEYHNAATNPEQQQESQRASSSSDQGPTALPSPAKRETRSQGDATVSGQTPELSSSANHNLYQPRLGQFRSRGSFGGAHSLSSGSSSLARGGGIPTYLTERDNDRDGNASGSNSGNSTTEERRGFGRRVSAGRNYPPHPSQVEEDEPLLFAMSDFGASRRSFEEGRQGNHGADFGGSRRGSGRRGAGVPGFHVWS
The following text describes a protein:
Function:
May play a critical role in development of the progeny of eagle-positive neuroblasts.
Subcellular Localization:
Nucleus.
Sequence:
MNQLCKVCGEPAAGFHFGAFTCEGCKSFFGRTYNNIAAIAGCKHNGDCVINKKNRTACKACRLRKCLLVGMSKSGSRYGRRSNWFKIHCLLQEQQTTSGLGGGSSVGSGSGGGVSSASLEQLARLQQASNQARQTYQDKTNPCIKSATATTSPRIEGAAVGTGIGGGASPSFLQAAKLHHQRQLKLDSRLSNTPSDSGASSAGDPNEDGVTSVLGGQIATPSSTNATSLPKLDLRHPNFPATSEPDADMQRQRHQELLEIFRSHSEPLYSSFAPFSHLPPVLLAAGVPQLPIFKDQFKAELLFPTTSSPELEEPIDLSFRSRADPASPMAHNSNSPSLSEPAAASHCLGESTNFVRKSTPLDLTLVRSQTLTG
The following text describes a protein:
Function:
Component of the NF-Y/HAP transcription factor complex.
Subcellular Localization:
Nucleus.
Sequence:
MPDSDNESGGPSNAGEYASAREQDRFLPIANVSRIMKRALPANAKISKDAKETVQECVSEFISFITGEASDKCQREKRKTINGDDLLWAMTTLGFEDYIDPLKLYLHKFRELEGEKAIGAAGSGGGGAASSGGSGSGSGSHHHQDASRNNGGYGMYGGGGGMIMMMGQPMYGSPPASSAGYAQPPPPHHHHHQMVMGGKGAYGHGGGGGGGPSPSSGYGRQDRL
The following text describes a protein:
Function:
Potentially involved in chemo- or phototactic signal transduction.
Subcellular Localization:
Cytoplasm.
Sequence:
MSKNKHELGSPFTVPLLLNTLDVPAFAVDADGAVVAWDDQIAALLETAPEDAIGVTDIGERLNDDGSRALANKVADTPIDAHHEYDGVGLADESYALLTGDYVYEDTTVAGNTDLWFIATPVYHTGEFRGVIEIVQDRSSSARYQSELQALFGELVDTLDAYDAGRFDATVDIAAEDTLLDDEYIQIGRNLTEFGDTLAAHITEVHNDVERLEAASQAVSESSAEIDELSTAQSTNVSTVATEVETLSATVQEIASTADEVVDTSATAERLADDGSAAASDAADMMADVATAADSVTSDVEALQNRIEDIDEVVDVITGIAEQTNMLALNASIEAARAGEEGEGFAVVAEEVKALAEDAQSNAGHIESLVSEIQRDTADTVTDLVTTTDRIEDAVAQVEDAMASFEEIVTAVEATAEGIEQVSDATNEQAASAEEIAAMVDETADLADDITTAVADIVSQTEAQSAMLHDLDESVSELHDQ
The following text describes a protein:
Function:
Component of a multiprotein complex equivalent of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MEATDPSAEIELYTIPAQSSWFLWDDIHEIERREFAEFFTESSITRTPKVYKEYRDFIINKFREDTCRRLTFTSVRKFLVGDVNLLQKVFLFLEKWGLINFSSSLKKNDHLLSVDNAKIEQGTPAGIRVTATPNSLRPITAPPLVEERVETGIKVPPLTSYSDVFSDLKKPDHVLVCAHCGERCDSPFYQHNKGIVNICEKCFKNGNYGENNTADDFKLIGNSAAAVWTEEEILLLLESVLKHGDDWELISQSVSTKSRLDCISKLIELPFGEFLMGSASGRLNPSILTEDENTEQVQTDGQEHEETETREEKEDRVNEDEPPAKRKRVALISEGDSSLMKQVAAMASKVGPSVATAAAKAALAALCDEASCPKEIFDTDDYSNFTVDRANGEKDTDMEEQQEEKDGPQGLPVALRIRASVATALGAAAAQAKILADQEEREMEQLAATVIEQQLKKLQSKLKFLDDLESIMDEEEKVIEGVKETIIQERVSVLQCAFRSGITKRWDHTYVK
The following text describes a protein:
Function:
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence:
MAPVSRRPCFRFAFDSALFSDKTLRLEVVSADPDLPVSRKRPRARDDVTSPDTVKKRQEAYERRDESSLEESDEPVGYTSKGPAGVIVIGNTNPVKPNNIEANDTDDDRLADFSRHARKAYVRLQEEGKIDNAGKGLDNVQKTPVPQVQHIRVSAMLLASESQFFHKLFTNGMKESNQNVIELQVSEAELEPVLEIIKFIYNGEFSKLDPKSLLATLLAADKYEVTTAISECGELLLNSEMTLGTARMYLDFTTTNSVLSEALGPLKSAAGDFVALKFKDVVQHENELLQMPLSVIRCVFLSSELIVPSEYHVYNFLLKWASENYPDPSHSRDVFCNELIHLVRFMHVSLDGLRQFFECPLMADDRKRVMTIIMNALLFKDDNTCSRVCNWNYDPRVYLTKPVKVSILHPYAEAIAYMDLTLDDCYRISKPGNTSRINSEVFTFYGHTFFMRVVCRMDPASSAPMALGLFLGTNHLRQTPVNLNVNFAVRQRPSGDFFNKLRFNRGFTNGNTYGMADLFSCPWAQLVGDGSMYVIDGRIHIRVKVKTGAG
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with ctu1/atpbd3 that ligates sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSEELPSCGINDNDINNTIPINTRKVQIIPNGNTQCVKCLYNVANNVKDKKLSKKEKKEQKLKEEENNNNNNEEPITQQQKPIGKPIINFRSEQLCWECYRELILKKFKLNIVKVRESKRDAEKLLVALSGGTCSSMLLELLKQCTEGSGKAKMFLDIKCVHIDESSITPYQNHNDTIEFLKEFNNVKLGFPNLEIIPLEDILGTVTPLGERTNQLKLQFAQLSSETSKEDLLLYYRNQLLIQVAHKLNCKKVILGTSSNRLAVQLVASTSKGRGFSVPNETSVIIEQPSNDIKFYQPMRDFLLKEIFIYYRHLNILPVPVMFSILNLKPKHSINTLCEDFLHCLQDISNQTVHTLLRSVDKLISPSIDSNYNCSICSSPLTSAEIKSLEKVILDNNNNINKENKNNNNNNNNNNNNNGCCSTTKTEDSSCCNKTEDNSSNNNNNNTGCCSSSSSTSTSSITVNKETLCYSCKILYRDFKSTPNIAPYIKENSKQLLTTSQLKNEIKDFLLNSDDDDDDEDN
The following text describes a protein:
Function:
Involved in the restart of stalled replication forks, which reloads the replicative helicase (DnaB) on sites other than the origin of replication. Recognizes abandoned replication forks and remodels DNA single-stranded binding protein (SSB) on ssDNA to uncover a loading site for DnaB. There are several restart pathways, the PriA-PriC pathway is a minor restart pathway. Also part of the minor PriC-Rep pathway for restart of stalled replication forks, which has a different substrate specificity than PriA. priB and priC have redundant roles in the cell. Stimulates the 3'-5' helicase activity of Rep helicase in vitro. In vitro can load the DnaB replicative helicase from a DnaB-DnaC complex on an SSB-coated stalled replication fork with no leading- or lagging-strand (or with a gap between the leading strand and fork junction) in the absence of other primosome proteins (PriA, PriB or DnaT). Also part of the major restart pathway with PriA, PriB, DnaB, DnaT and DnaG primase. PriC may contribute to the stability of the preprimosome complex (Probable). Preferentially binds approximately 7-9 nucleotides of single-stranded (ss)DNA, also binds double-stranded (ds)DNA. PriB is probably more important in the cell than PriC.
Domain:
The N-terminus weakly binds single-stranded (ss)DNA. The C-terminus (residues 96-175) binds ssDNA as well as full-length protein.
Sequence:
MKTALLLEKLEGQLATLRQRCAPVSQFATLSARFDRHLFQTRATTLQACLDEAGDNLAALRHAVEQQQLPQVAWLAEHLAAQLEAIAREASAWSLREWDSAPPKIARWQRKRIQHQDFERRLREMVAERRARLARVTDLVEQQTLHREVEAYEARLARCRHALEKIENRLARLTR
The following text describes a protein:
Function:
Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction.
Miscellaneous:
MISCELLANEOUS: Considerably less active in nick joining than LigA.
Sequence:
MKVWMAILIGILCWQSSVWAVCPAWSPARAQEEISRLQQQIKQWDDDYWKEGKSEVEDGVYDQLSARLTQWQRCFGSEPRDVMMPPLNGAVMHPVAHTGVRKMVDKNALSLWMRERSDLWVQPKVDGVAVTLVYRDGKLNKAISRGNGLKGEDWTQKVSLISAVPQTVSGPLANSTLQGEIFLQREGHIQQQMGGINARAKVAGLMMRQDDSDTLNSLGVFVWAWPDGPQLMSDRLKELATAGFTLTQTYTRAVKNADEVARVRNEWWKAELPFVTDGVVVRAAKEPESRHWLPGQAEWLVAWKYQPVAQVAEVKAIQFAVGKSGKISVVASLAPVMLDDKKVQRVNIGSVRRWQEWDIAPGDQILVSLAGQGIPRIDDVVWRGAERTKPTPPENRFNSLTCYFASDVCQEQFISRLVWLGAKQVLGLDGIGEAGWRALHQTHRFEHIFSWLLLTPEQLQNTPGIAKSKSAQLWHQFNLARKQPFTRWVMAMGIPLTRAALNASDERSWSQLLFSTEQFWQQLPGTGSGRARQVIEWKENAQIKKLGSWLAAQQITGFEP
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which probably functions outside the N-end rule pathway, since it lacks the residues essential for the degradation of N-end rule substrates. Mediates RPN4 ubiquitination and subsequent degradation.
Miscellaneous:
MISCELLANEOUS: Present with 49 molecules/cell in log phase SD medium; MISCELLANEOUS: Deletion produces no detectable phenotype.
Subcellular Localization:
Cytoplasm.
Domain:
The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.
Sequence:
MEDSDLSITNIRDFLTELPKLAKCEYSETTSYLLWKTLNLRLKHSDNDINWRSLVSILNSEAWENEKYRDILNGRKWRTLEFENDHHSVGNMHIGTACTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYVAKVVMRPEGRICHCGDPFAFNDPSDAFKCKNELNNIPISNDNSNVTDDENVISLLNYVLDFLIDVTVSYKEEAEAHSSERKASSLMHPNQNSITDDIMEKHECEPLVNDENFVFFDNNWSNTRKEAHMEWAIQIEEEECNVHYMDLASTITRILNTPVEYAISITKALEDSHDVVTVLQSENFFEIDQIAKEFQKENIVVHVRKADDIFKRKLTDDLTDWLYSLCFKAATSLQNKYALRISMLDVWYSHFSKMRVSPTNTNPDFSKINLLGGFLISNEDSDESWFKPWSLENIEDERISKILTNYNERLIRAHSPNTVSHFYNFYGSRFQYIIINSINILSKKSKFKMLKIMASLFSLRDESRKFLAAQYIDVYLSVLYDAVASDAKECQVTLMSILGQYTFQDPSIANMTISSGFIERTIRFAFTLMAFNPEDLMSYLPISLYNGFKLPTETIRNRRTIICFKDLCTIMSANTVPEELLSNEAIFNAIIESFSEFSNVLPLKRETKEHVEVENFDFSAFYFFFSSILIMTDGYTRSISLVKDAAFRKQIVLKLLDVAQTREFESLTNSRKAISPDNASTNENDSNKATLSTVRETICNYVAETINFQVGVNTQYFFNPMSYLFKFVIQWSQCGRYEPIPASLTNYINLFEVFQDKQKALYISESALSTLVLIGQINVGFWVRNGTPITHQARMYTKYSMREFTYISDIFNVQFSMAMCNPDELMVTYLSRWGLKHWANGVPMYDYPDTETTVAVVNECILLLIQLLTEVRSLVMKSSKEGFERTFKSEIIHALCFDTCSYAQIVNCIPEHITKHPSFDIYLEKYANYTSPVSLTDNGIFVLKEKYKDEIDPYYIGLSSSRRYDVEKNIRLNMANLKKMKYEDTFVPAKKVKDLLKNTLFSGLYSISSVNTFGLFLKNTLDHIIKYDYDNLLPRVVHLIHLCVVNNLNEFMGILWHEYAIVDTEFCHYHSIGSILYYCLLKDNFSESHGKIREIFRYLMETAPHVNVNSYLREQTTSYTPGILWPTKEDKSHKDKEFERKKHLARLRKKKLMKKLAQQQMKFMENNSVDTSDISTPRTTSPSLSPTRINAENSSNTINSCCDDDCVFCKMPKDDDVFVYFSYQERNICDHGIDFTNPTDVNRINSLFSGKQTKDSAIQENPQDDDGTRLKFTSCEPVLRACGHGSHTKCLSGHMKSIRGIQNQTTKNIPLSYGSGLIYCPVCNSLSNSFLPKTNDIDKRTSSQFFMCIEKRSEAEENLDPMSSICIKAAMILGDLQGKKVTTIEDAYKVVNSVFINTISNTELRLRSHKKEGKIVNMERISSQCILTLHLVCELKSFIYKKFVNSKTFSSEISRKIWNWNEFLIKGNNVNLLLYMSQNFDNIDGGKTPQPPNLCIYEMFKRRFHQLLLLLARDMMRVNFYKDCRNKIKISSNGSEEPSTSFSYLFNTFKKYVDLFKPDDVRFDFTSLEKIKDFICSLLLESLSIFCRRTFLLFNIQYDDDGDGDNNNNRSNNFMDVKQREIELIFRYFKLPNLTHFLKDFFYNELTQNIERYNDGNDNLRIQQVIYDMVQNINTRAYPSPEHIQLIELPLNLSKFSLDNDEISNKCDKYEIAVCLLCGQKCHIQKSIALQGYLQGECTDHMRNGCEITSAYGVFLMTGTNAIYLSYGKRGTFYAAPYLSKYGETNEDYKFGTPVYLNRARYANLANEIVFGNMIPHIVFRLTDGSADLGGWETM
The following text describes a protein:
Function:
Important role in the capacity of milk to transport calcium phosphate.
Subcellular Localization:
Secreted.
Sequence:
MKLLILTCLVAAAFAMPRLHSRNAVSSQTQQQHSSSEEIFKQPKYLNLNQEFVNNMNRQRALLTEQNDEIKVTMDAASEEQAMASAQEDSSISSSSEESEEAIPNITEQKNIANEDMLNQCTLEQLQRQFKYNQLLQKASLAKQASLFQQPSLVQQASLFQQPSLLQQASLFQQPSMAQQASLLQQLLLAQQPSLALQVSPAQQSSLVQQAFLAQQASLAQKHHPRLSQSYYPHMEQPYRMNAYSQVQMRHPMSVVDQALAQFSVQPFPQIFQYDAFPLWAYFPQDMQYLTPKAVLNTFKPIVSKDTEKTNVW
The following text describes a protein:
Function:
Heme transporter that regulates intracellular heme availability through the endosomal or lysosomal compartment. In macrophages, is the heme transporter for heme-iron recycling. Essential for macrophage iron homeostasis, transports heme from the phagolysosome to the cytoplasm during erythrophagocytosis (EP).
Subcellular Localization:
Endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle, phagosome membrane; Multi-pass membrane protein. Note=In macrophages, specifically localizes to the phagolysosomal membranes during erythrophagocytosis.
Sequence:
MGPNRIYISVGYSTFGMLVGFSAFIVWNVVYKQPWTAAMGGLSGVLALWALVTHIMYIQDYWRTWLKGLKFFMFVSSVFSLLAVAAFATFITLSVIEKQSLSDPKSFYLSAVWSFMTLKWAFLLGLYSYRYRQEFADISILSDF
The following text describes a protein:
Function:
ATP-binding RNA helicase involved in ribosome assembly.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MRAENEFILTIEDSEDDIQYDDSEIEAESDMEAEKETKKVQKKQKKKKNKENDFSGSFMFESGINDGVEAGNGTDWDFQSAKNALRNNTTDVDLNSIIQRNRKQPTSEENKEVHQESSADDVSSAEEEEETTAVDSDEESFTGIASDDEDLATDGFGGAVKEQASDSSDEDSDEDDITVPVPDTVPGEVNEIDSDSAVSDDDEEQARIEREKSEAYFAAGAEDAAAVTAQVSFQDMKLSRPILRGLSSLNFEDPTPIQSKTIPVALLGKDIVGAAVTGSGKTAAFVVPILERLVYRPKKIPTSRVLIICPTRELAMQCHNVAKRIAAFTDITLCLCVGGLSLKVQEQELRKRPDIIIATPGRFIDHVRNSQGFSVDNIEIMVIDEADRMLEDGFADELNEIVKLCPKSRQTMLFSATMTEKVDDLVRLSLNRPVRIFVDAKKATAKRLVQEFIRVRPQREQLRPAMLVHICKTFFHRRVIIFFRNKAFAHKMRIIFGLVGLNATEIHGSLSQEQRVRALEDFRDGKVDYLLATDVASRGLDIKGVEFVINYEAPASHEIYLHRVGRTARAGRSGRAISLVGENDRKVIKDVLKSSENQHDNVVSRNLDFPRVEAIGKELEELEDTVKQVMEEEKQERHIKIAERDLKKGENILKHQDEIKARPARTWFQTEKEKKASKTAATGKAVPLSKRKKAMDAEEAAARPYKKTRQDRMKKGKNSKSGKNSKRGKK
The following text describes a protein:
Function:
Nonessential SNARE involved in retrograde transport within the Golgi complex.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type IV membrane protein.
Sequence:
MKSMLLRDSVKKASQFQRSLHSDPNQAKILLEERRKLLEEANSSADENDSHSMATIKSHFERLKRDEQLLNGVLKKYDAKQEVLSPEELRDAQNFLEMQEANSLDNSIRGTNELLERAYATREDFDYQNSVLGNVTNRINGAAMSIPFINQILRKTSIRRRRDSIILALLISVLMLLFLFFH
The following text describes a protein:
Function:
Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSPLINGFIIFSLTVTLLYFVGLLTFVNDHEENKCEMTYMFEYPQFVRISNKIDDKYPRYGLYAYSEGRLTEKTRNMFFDGIPVLFIPGNAGSHRQGRSLASVALRKALNSRTPFHFDYFLIDLNNELSGLNGALLADQLEYVNNSIYTVLDLYQNRKNPAKSVVLVGHSMGGIIAKRLVSNLGENSDLVPIVLGLATPHRRPPLQLDSFSYDFYKNIDTKNSSTTFVSITGGYNDFLVPSFLTNHPDSILNVVSTQIPRSWLPADHVCILWCKQSILAINRALVDSVDPKTKQISSDQTLRYRVFHHHLIHHSGINIRLLDSYSLSPNIKNQGEWIEPFGRQYSVQVPRLSSSPHFYMIRLLNQPQHQTLTVVALNLETVDWAFVCGAHIPRGNSRICEEFTHLTHLSEISPSSNYKRRSLTVDMHELMKNNTVWTHIVLRVLPTDEQVILNVDVYNTGDRKTLVNLPNLLSFKRQTIIEQTHEKAIHYELVLPNLYHLMQSYQLYVESIQCVNQFRHATASLIVPWGHQNQHKFFIDGDNKPMNVRLYSSRPQWASNQSAVIQLRLDPTCRYKISIQSSFIGVLSQLARFYSPLLIVNVAAVILVALNTQLKSLGQENDCCLFFTAVKEGAKPYYILTSVKLISRFLSFKPFVTYLAAPDWLIMSEEGTDFFLLPLLLYICSVGIVWLLGIFLSVSLVVCETTVHKFTLKFLAKTVSFTVSWSDYLMSALHKLPCIVATFLICLCVTTTGSLALCVGMVFYFMRLTQLSQDYIEELVWYYVKKIGKKLKKPNKDKDNNSINSGETPAHNAIFFHATLFLLWSILTVINVPSVLTWAHNFKFSTALKPDPAFYPGLVLSICALPLWQLDVPKIERRGYVELGKLIIVLAVASLIYAPISLFRLNFTLTSAIAFVTLHQLVAPNREIPETSRTEQPISYETIKAKLE
The following text describes a protein:
Function:
G-protein-coupled receptor for histamine, a biogenic amine that functions as an immune modulator and a neurotransmitter. Through the H1 receptor, histamine mediates the contraction of smooth muscles and increases capillary permeability due to contraction of terminal venules. Also mediates neurotransmission in the central nervous system and thereby regulates circadian rhythms, emotional and locomotor activities as well as cognitive functions.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSWNTTIADFATDFLPTTAYDGNGSFGGNVTAVGPVDGGSVWTDVALGIVLGSLCLLTSVGNAMVLHAVRTNRDLQTVSNFFIVSLAVSDLAVGTVVMPLSTVNIVAHQWVLGLPVCQVWLSVDYVASTASIFNLFVLNLDRYWSVTTPLKYMRKRTKRRAMAFIALVWGVSALWIIPIVGWHAFEFGGVRKVPGDVCDTEFNANCTFKVITSLFNFYFPMILMSVIYAQIYNKVRKRHKNLSVHISRGSVPTENDIKMHEGLRRSSTSELQRLRTRRGSCVGDKIRGPSPEQKSPAKSCNGPRGQPVAVLAKMSSPNNTIQSVIDTLPPDDGKYLSVDKTDSGDSRRSSAEMPPIPEDGSALKSERKSSKLSWPGGRLSPRKSIADLQGSPSKQGSTKKRLSLTRGSLLRRMNLKNRSRMHSERKAAKQLGILMGCFVACWLPYSILFVAFCNSGDISEDILIGATWLGYINSTMNPFLYPLCNDNFKRAFRKMLGCGDGSNLQNSTTSRL
The following text describes a protein:
Function:
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Sequence:
MSTPTLPDMVAPSPRVRVKDRCRRMMGDLRLSVIDQCNLRCRYCMPEEHYTWLPRQDLLSVKEISAIVDVFLSVGVSKVRITGGEPLIRPDLPEIVRTLSAKVGEDSGLRDLAITTNGVLLADRVDGLKAAGMKRITVSLDTLQPERFKAISQRNSHDKVIAGIKAVAAAGFTDTKIDTTVMRGANHDELADLIEFARTVNAEVRFIEYMDVGGATHWAWEKVFTKANMLESLEKRYGRIEPLPKHDTAPANRYALPDGTTFGIIASTTEPFCATCDRSRLTADGLWLHCLYAISGINLREPLRAGATHDDLVETVTTGWRRRTDRGAEQRLAQRERGVFLPLSTLKADPHLEMHTRGG