lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi. Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1. Important for neuronal function.
Subcellular Localization:
Golgi apparatus, trans-Golgi network. Perikaryon. Cytoplasm, perinuclear region. Note=Co-localizes with rab-2 to perinuclear puncta in the perikaryon. Co-localizes with the small GTPases rab-6.1 and rab-6.2 at Golgi structures.
Sequence:
MPRTRVNLQKSEANDRSFTISSLEFCLSQLRKADPNLVKKAIASGDGLTESKNDVSTRLSEAHRYSVQQCLDNSEQLAQLHNQLVHCDNVFERLQATLYSFQDNLGSIGQDMKNLQLQSHHIHQELENRQKVRVELSQFVDDIAVSQTMMKTINDTDANDRGFLEALHELHHKITLILQRGNGDAVAVNDTMPILEGLKLKAVVKVREWLLQKMFQFRKPLSNYQVFQHQLLKCRFFYEFLLHHDLISAKELQDEYIDTISKMFFTYFKAYATRLFKLAMKDVATKEDALGSIDFAKPAGLGAIFSSKQHVVRNKATVFSIGQRHQILSDDFLGALIVPHAATQNHQSYQFEALFRSIQLAFVDHYSHEYLFITDFFLVSNDEAIELHNKAMARAMSVVLKSCEEQIALSWDAISLHLCICLCDKFTEVLAEREVPEVSDYWNTVTSFLWTRLNLVMSQHYESVKSVDLKKLMHSGSLDARPHFIVRRYAELTSAHLMIAKASGKEMGAKMEAVLENSEDSIEQLLTRMSAMQQTQKNKHVFLINNYDLILSIIDNEESKHTKIYAIVHELEQKSIDDFVEEMLEPHIGYMIKFVNECESLIVQGHTQLLVRYNDKVGTVVANFNAKWRPAVDSINSECIQLFTNFSLGTTILQTIFTKYVQYINRFTKILSHDVFAKNPVCSQLVNVHQVMLEIKRFKPAY
The following text describes a protein:
Function:
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MLREIRPAIVLLLVLTAITGLAYPLAMTGIAGMLFPAQAQGSLIEKDGKVIGSALIGQEFKDDKYFHGRPSATLAPDPNDSTKTVSAPYNAANSGGSNLGPTSKALADRLKEDVDKLKAENPNAAVPVDLVTTSASGLDPDISPEAAQFQVPRVAKARNMPEEAVKQLVASNVQGRLLGLLGEPRVNVLALNLALDRAAAK
The following text describes a protein:
Function:
Malate transporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MATQEAGKLEWRISVDNGTTERLVPRSGLSKRIFLWLKDLVMKVIMERVAKFMRKAWRIGADDPAKVVHCLKVGLALSLVSIFYYMRPLYDGVGGNAMWAIMTVVVVFESNVGATFCKCVNRVVATILAGSLGIAVHWVATQSGKAEVFVIGCSVFLFAFAATYSRFVPSFKARFDYGAMIFILTFSLVSVGGYRVDKLVELAQQRVSTIAIGTSICIIITVFFCPIWAGSQLHRLIERNLEKLADSLDGCVAEYFKENEVSTNRNEDENTNMKLQGFKCVLNSKGTEEAMPLIRFSGFSFSQANLARWEPAHGSFNFRHPWKLYVKIGAAMRRCAYCLENLSICINYETEAPDQVKNHFGEACMKLSSASSKILRELADMMKNTRKSSKMDFLVFDMNSAVQELQETLKNVPIETNKPEEVPSEEENKVDSEERTTSMSLHEVLPVATLVSLLIENAARIQTAVEAVDELANLADFEQDSKKKTGDNNTKQPPLSS
The following text describes a protein:
Function:
May promote appropriate targeting of ribosome-nascent polypeptide complexes.
Sequence:
MPDEEPSAEEMIRVRQLVDLLNLEMAMQNLDMKPVPCVSQVTIKKTKDTKVVISNPTVFKVLNSDTYVILGNDAQTGNLSSLLQQPMVRKASNDVAESESESDESGSSDDDVDESGSSDDVDESGSSDDVDESGSEEDGENLSWYENLSWSEQEDIKLVTNHTGVSKRKAAKALKEFDGDIVTAIMELNSN
The following text describes a protein:
Function:
Involved in mitotic DNA repair and meiotic recombination. Functions in the recombinational DNA repair pathway. Essential for interhomolog gene conversion (GC), but may have a less important role in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51 enhances the ATPase activity of okr/Rad54.
Sequence:
MASVKETGSFFTHGDSKQYEFVLTLYPQALKLKAKEKKLKKPEDLLKLDAWYQEELPKKIRARGKDAHLTHDELVQCMKWKLTRGQWRPRLQNLVQLNTPHAVEEQSREAFKQMVLKGEKGIESAIHSLAKMKGVGPATASVHPSKSRFRFFSPTCENKRAKRGKFYSQMINLVMINTPKAVATETRKALRKLPNLESALNNLSSLKGVGTTMATAILAAAAPEIAPFMADECLMAIPDIEGLDYTAKEYLKYVQHIRTVVDRLNAENQNSAWSPHRVELALWCHYVTRKLEPSLLDGIPGLEEESKENGTAKSSDVANGSPTAVDGKDSEDSSSGPLALANTEDSSEATNDSLSVVINSEETSREPTTNGNGNDTTNDNTNDNTTNDHDSSLADGVPSNGANVVAPDDNAVVGGRDDNAVIGGDDNAVVDQEELSSEPSASAAQKQPPESNSVYFEMEEPKESPESVIASVVNENETPRVLPNFQINRDIIESVALENQSEELRSLGITVYDQSKFEESILRQVDDALEEQERHKKVINAKKILASKDGDKEKTVADKPLKIRKETEKEKMVRLGQMTPFGTVLGSGGKTTELTSFEKYMLEQEKLQNVKTKISTRKGKTLKSPASVVNLSPGKDIVKRVAPKSPTKTSSKKGFHKNESDSDYVPSDEESPKPQKPGGLQRKKRKQEIEKEWNTDDSNWEYSEDEETPKKRKSKKTSDRIVDDGNINDFRERLAVLPHFETENEDCEEFEGGYRIPLSIWNQLYNYQKVGVRWMYELRLQRCGGILGDEMGLGKTIQVVAFLAGLAHSKLLTRLSSYRGLGPVLLITPATVMHQWVKEFHKWYPPIRVAILHESGSHTGSRDALIKSINSSNGVLITSYTGVPQYSERLLELDWDYVILDEGHKIRNPDAQATLVVKQFRTSHRFILSGSPMQNNLKELWSLFDFVFPGKLGTLPIFLQQFAVPITQGGYSNASQVQVATAYKCATVLRDTINPYLLRRMKADVKDHLQLPDKNEQFNESDPKKQFGCVERSGKLLVVESLLKIWKEQNHRVLLFSQSRQMLDILECFIRQQSYNYLRLDGTTSIGSRQPMIEKYNKSADIFVFLLTTRVGGANRVIIYDPDWNPSTDTQARERAWRIGQQKDVTIYRLLTSGTIEEKIYHRQIFKQYLTNRVLKDPKQRRFFKSNDLYELFTLKDTDNQCTETEAIFAGTGSEVATNPHDGPPSGKMDKPSDDEWMRQWKKEREKRELEWKKSLDKREKQKTKMTETEEEKRRRKKREAKEKKEKKRIKIDGAKVKHVVKMSSHNSVAVDLDDGSTPSTSSNNQDDYVLQRLFAKTGVMSALRHDSIIDAGDPDYALVEGEAERVAKEAVQVLKSSRRNCYRAEAGIPTWTGTSGAVRSACPTDTKKPRFGAKKKSVLPSVGACTSSHHAEMSKESPGAVDAIDLPIPGSSNAVLSSQDLLSRMQARNRLLGLPGNSADDCTAGSSFRSANEEESLILETQSAPLEFATGVDYHTMTDNIRSFVAFRGVTPGQVTTTDILSEFDGKLPLRGAPLFRALLNQLCSFTRDVNNQGIWQLKPEFQ
The following text describes a protein:
Function:
Subunit b, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MDLNVFAPTTLLLVAVTVEPPKRAEPKAVAESLINAFPGESLVAKSSSVLVAASIAAFLISKEIYIVDAETIEMFCLFGAYYVWYSNGKDSALAYFQGRKDSIRNVLTQARLDHKAVVQERISHIGKLSDAVEVTKGLFDISKDIAKLEAEAYELKQKVAFNTEVKGVLDSWVRHEANVREEEQKRLAAHVIGKIKQDLTDPRLQQTILQQSIADIESMFN
The following text describes a protein:
Function:
Required for the transduction of an SCO1-dependent redox signal from the mitochondrion to ATP7A to regulate cellular copper homeostasis. May be required for the assembly of mitochondrial cytochrome c oxidase (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Mitochondrion intermembrane space. Mitochondrion. Note=Partitions between mitochondria and the cytosol in a copper-dependent manner. Enriched in the cytosol when intracellular copper concentrations are elevated.
Sequence:
MSTAMNFGTKSFQPRPPDKGSFPLDHLGECKSFKEKFMKCLHNNNFENALCRKESKEYLECRMERKLMLQEPLEKLGFGDLTSGKSEAKK
The following text describes a protein:
Function:
Thiol-dependent isopeptidase that specifically cleaves UFM1, a ubiquitin-like modifier protein, from conjugated proteins. While it is also able to mediate the processing of UFM1 precursors, a prerequisite for conjugation reactions, ufsp2 mainly acts as a protein deUFMylase that mediates deconjugation of UFM1 from target proteins.
Subcellular Localization:
Endoplasmic reticulum. Cytoplasm. Nucleus.
Sequence:
MGFQSSVEGLTQASACGDILQYIESDDGGNKKSSKKKDKKKSGPIVVNLKLLFEVTDPAGNEAPSLMRMSAQQHSVKMPLPLDCVLSVSADESMTTVFTGLVEALNKQIADMEEVVLRYRKGSSFLVPQPFHFQLPKPAGLTTVIYPAGVPDSQLQAVREDLHRKFELSLDRPYLRRANAFHFPYEAYKDGYLRNPHIHLNPPNIEDAKLYLVQGVYSYHHYMQDRVDDDGWGCAYRSLQTICSWFQQQGYVETAVPTHTQIQQALVDVGDKEPRFVGSRQWIGSIEVQAVLNQLLGVTSKIMFVSQGSELATKGRELANHFHTEGTPVMIGGGVLAHTILGVAWSENTGEIRFLILDPHYTGGEDLQIITDKGWCGWKGPEFWDQNAYYNLCLPQRPKTV
The following text describes a protein:
Function:
Palmitoyltransferase that targets several endosomal SNAREs. Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic end of their transmembrane domain. May have a role in the cellular quality control of transmembrane domain-containing proteins (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The DHHC domain is required for palmitoyltransferase activity.
Sequence:
MWLKIYLLSILAISVFTFVFLFGALPQFEDTAVWKFRKWLSNRPAAIRSWDSKYCGGRLSVVGDFCGSVVAPAAPWSVPILYCAFTTYMFSAYYEDLHPFIAENHWYYAWLAPVAYTILVVSFVLATFSDPGKITKQNHALLLNQFRFDNLMFLEDTECSTCKFTKPARSKHDRFTNKCVAKFDHYCLWINNTVGLYNYRWFLFFLLGNVWTLCWGALLAGLKMIVMVAAEYKDHPKPLPSIFSQWWQVMITNENKRVGIIFLLSVSTGALACAFTAMHFYYIYLGATTNETDKWGDIHAAISEGSVWMFQKPGFKLDRSILLQKDEEGRPNRSLTAEEREYVAQNGLALTLLTDHKPIVNIYDKGFLNNLKAVMFPNSAY
The following text describes a protein:
Function:
Implicated in development of the cochlea.
Sequence:
MAEMEKEGRPPENKRSRKPAHPVKREINEEMKNFAENTMNELLGWYGYDKVELKDGEDIEFRSYTTDGESRQHISVLKENSLPKPKLPEDSVISSYNISTGYSGLATGNGLSDSPAGSKDHGNVPIIVPLIPPPFIKPPAEDDVSNVQIMCAWCQKVGIKRYSLSMGSEVKSFCSEKCFAACRRAYFKRNKARDEDGRAETFPQQHYAKETPRLAFKNNCELLVCDWCKHIRHTKEYLDFGDGERRLQFCSAKCLNQYKMDIFYKETQANLPAGLCSTLHPHMESKAEGTGVQLLTPDSWNIPLTDARRKAPSPVTAAGQSQGPGPSSSTTVSPSDTANCSVTKIPTPVPKSLPISETPSIPPVSVQPPASIGPPLGVPPRSPPMVMTNRGPVPLPIFMEQQIIQQIRPPFIRGPPHHASNPNSPLSNPMLPGIGAPPGGPRNLGPTSSPMHRPMLSPHIHPPSTPTMPGNPPGLLPPPPPGAPLPSLPFPPVSMMPNGPMPVPQMMNFGLPSLAPLVPPPTLLVPYPVIVPLPVPIPIPIPIPHVNDSKPPNGFSSNGESFVPSAPGDSSAAGGKAGGRSLSPRDSKQGSSKSADSPPGSSGQALSLAPAERGRGEVVDLTRRAGSPAGAGGQPGFAGVLHGPQDGVIDLTVGHRARLHNVIHRALHAHVKAEREPGAAERRTCGGCRDGHCSPPAAGDPGPGAPAGPEAAAACNVIVNGTRSAPAEAKGAEPPPEQPPPPAPPKKLLSSEEPVVNELESVKENNCASNCHLDGEATKKLMGEEALAGGDKSDPNLNNPADEDHAYALRMLPKTGCVIQPVPKPAEKAAMTPCVISSPMLSAGPEDLEPPLKRRCLRIRNQNK
The following text describes a protein:
Function:
Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta-oxidation of fatty acids.
Subcellular Localization:
Peroxisome.
Sequence:
MLSNFAVVVRCIESYQNVRSCSGVVIDFERGLVLTSGSLLSCLIDTNAADRQSLATVDQLAKTLKFEIIVKLENNHSKSSSFMALKCQLRSRWYCRQVQEVLDNSMPSHRWSFTIPPEKQWDNMDDGTKAANTNPLAEENHSNQKSDPSVITQFLLLQITDTNKKFLNSDPIEMADRRLLKRGDVVEVISTPFGDSYPLIFYNSSTKGIISNICGKKNQLFLTDARCLAGSEGGAVVCKLAGQSKASLVGVVMSPFCFKDTEWTGFTLVVPIDLILTSLPSKHHPLVHDFMALKLPNSTRSNLTPNSDISFFDKVSSAVVYIQSLSSWGSGVVIDRYKGLIITCSHVVHPCNSNSDDDCNHGESDRKVRVLTTKPIKRWYNAVVLYPKQHCQVLDVAVIKILDFLPSQLSSISLCKSDSAISTGSDILIIGYGMFPPHTYEANEPTVTRGSIASICRINNKPMLIQTSAAIQCGTSGGALISKNTGELLGITVSKVKNVNSGGIYTYISFCIPVTRIYPQIVKYNQSKDISDLKMLSYQNDSAVGQLWLMKATAANYRQLDLRYTMQKILCEYSSRPHKQTLMISSCSRSEVLKGSYKKY
The following text describes a protein:
Function:
Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the third heptose unit (HepIII) to the second heptose unit (HepII) of the phospho-Hep2-Kdo2-lipid A module.
Sequence:
MRYHGDMLLTTPVISTLKQNYPDAKIDMLLYQDTIPILSENPEINALYGISNKGAGTFDKIKNVLSLIKTLRANNYDLVINLTDQWMVALLVRCLPARMKISQLYGHRQHGIWKKSFTHLAPIHGTHIVERNLSVLEPLGITDFYTDTTMSYAEDCWKKMRRELDALGVKDHYVVIQPTARQIFKCWDNDKFSKVIDALQQRGYQVVLTCGPSADDLACVDEIARGCETKPITGLAGKTRFPELGALIDHAVLFIGVDSAPGHIAAAVKTPVISLFGATDHVFWRPWTENIIQFWAGNYQKMPTRHELDRNKKYLSVIPAEDVIAATEKLLPEDAPSADRNAQL
The following text describes a protein:
Function:
Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B.
Sequence:
MAGLLLCAIFIWLASADTPCWCANDQVLGTWKIESTGFKYTITNDRTSCPASIRVKETRMITLLSPNVAVDEDTGASGTWSQVYSQAIQINIGDLKYLYFLAWEDVPDSSTVHSMCYKSQPEMGWAVKQGMMRRYRACIRATNVKPLLTTVDNYYEPSGPGPVNPTLIRRKLDVSVPTGDMYIQMKKNGDVTNIPAGFRQSFSHSLFPTGAAAENSNSSYRGDKLPKNFDWRSVNGKSYVPEPFDQGHCGSCYTAATVWAMTARVMVASEDEDKLGATRRLSVQHALDCNQYAQGCSGGFAEMVVKFAEEFGILTENSYYISYLSGDGVERPCKAGKFLEGDRYFFTAGLPLGGYTGAVTDPEEIKWEVYRHGPLPVSVYAGNDLFKNCSPYGPSSRAAYTDDDDVSANDKAKRHYFAEYLDHLIFIIGWEEDENGVAYWRIQNSWGADWCDGGTSRIALGRNEYGIETAPVPFYWWRNGRVYYDEGLVAVSLAEIIILPVAIVVLAGLIIGLSFVIAIMKKNRRLKYQRLRDEQTTHYEFTSTALDSTVPESTTDPSSYQ
The following text describes a protein:
Function:
May be involved in fructose recognition during germination.
Subcellular Localization:
Cell membrane; Lipid-anchor.
Sequence:
MSKAKTLLMSCFLLLSVTACAPKDQAADMDYDQTKKMVVDILKTDDGKKAIKELLNDDAMNEALVIDQDAIKGTIEKTLTSKKGEEFWKNIFEDTDFAEGFAKTLQTEHEKVIKKLMKDPDYQKMLMSVMQDPGMDKKYSQLAKSQEFRSYLEEVINETLSSPLYKKQFEDELKKAAKDTAKESE
The following text describes a protein:
Function:
Seems to be involved in the correct timing of cell separation after cytokinesis, as separation of mutant daughter cells is delayed. Could either be an enzyme necessary for glucans-degradation of the cell wall at the neck region between mother and daughter cells or a regulatory protein controlling this metabolic step.
Subcellular Localization:
Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Localizes to the septum of dividing cells.
Domain:
The number of the intragenic tandem repeats varies between different S.cerevisiae strains.
Sequence:
MNKLLLHLVRVISILGLANALTQTQPILKDIQITDSYTKTKECTDPDHWFIIEGQLSIPKGSQQNITFQVPDAFSSFPQEPFSIKHNSNSVATISRPDKSTNNFTISIPEKSSEDITTTFNFLAQLTSDAKSKVTEPKSIVYSFYSENTMFNDVIDYVAKNTSAITTDGGIYKTNNTAWFTVDLPMRTFRNPVYLTSQTSSSSDYVFDTSLTKFEVVTAVDSFNEPINAIPYTTVHDYSTEDEIRCLFNSTISGGLYFRVTYFTKKLSTSSISNTVELTYPDEGTSVRLLGKRDTSTTLASELYSESAANIDSTTSDDTTSSDAAITPTYSNSTLSSYTSQSSAIPEVAVTASLSSGILSSTVDGASTSADASMSAVSTVSSSSEQASSSSISLSAPSSSNSTFTTPSSSLSATETYSIISSASISVTQASYIDNSTTTAVTQSTSTIAVSSAEKLSSTLSYTSNVTISVSSATQHTTTPSYVSNSTTLSSSSVLESVISSPYLANTTVSGASSASQSTNPPYVSNSTTSSATQLATIAPFAINITGTSISSSITNTSSVSSTTSSLSSGPFVSNTTVASGSYILTTTTESAQLTEIGSLIPISTITTSTTTSGTDKTGSNKVASSTEIAQSIVNNSSLSVSTINTNAATAAANARNATFTHATHSGSLQPSYHSSSLLSSTIDTKVTTATTSTSRDGSSSLAFTTGLNQSVVTGTDKSDTYSVISSTESAQVTEYDSLLPISTLKPTVVTGTSRNSTFSMVSSTKLTEATATDKGDAYSVISSTQSAQVTEYGSMLPISTLETPTVIMSTDESGYFTLTTCTESGQATEYGSLIPISTLDGSVIYTFTGESVVVGYSTTVGAAQYAQHTSLVPVSTIKGSKTSLSTEESVVAGYSTTVGAAQYAQHTSLVPVSTIKGSKTSLSTEESVVAGYSTTVDSAQYAEHTNLVAIDTLKTSTFQKATATEVCVTCTALSSPHSATLDAGTTISLPTSSSTSLSTIITWYSSSTIKPPSISTYSGAAGQLTIRIGSLLLGLISFLL
The following text describes a protein:
Function:
Ras-related protein which binds GDP/GTP and possesses intrinsic GTPase activity (By similarity). Involved in both yeast and hypha development. In the yeast phase, it is required for normal (polar) bud site selection and is involved in cell morphogenesis; in the yeast-mycelial transition it is involved in germ tube emergence; and in the development of the hyphae it is involved in cell elongation.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
Sequence:
MRDYKVVVLGAGGVGKSSITVQFVQGVYVESYDPTIEDSYRKQIEVDGRACDLEILDTAGVAQFTAMRELYIKSGKGFLLVYSVTDENSLKELLALREQVLRIKDSDNVPMVLVGNKCDLEDDRVLSIEDGVKVSQDWGLVPFYETSAMYKTNVDEAFIDVVRQIMRKEAAISAEKKQQKELQKQQQQQQQEQDAEGQQQQQKSGKSKSSATQKDATADGQTDVNARLKQSINDHPKSSSGSKFCTII
The following text describes a protein:
Function:
Acts in a planar cell polarity (PCP) complex; polarization along the apical/basal axis of epithelial cells. Regulates the polarized assembly of fibronectrin on the surface of the mesoderm during gastrulation. Essential for gastrulation cell movements, cooperating with dvl2/dsh to activate jnk. Acts together with tes to control axial elongation.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MPLEMDQKVNKLTFGCQRSSTSDDDSGCAMEEYTWVPPGLRLEQVQLYFACLPEEKIPYVNSVGEKYRIKQLLYQLPPHDNEVRYCQSLSEEEKKELQMFSAQRKKEALGRGNIKMLSRAVMHATCEKCGEKINGGEVAIFVSRAGPGVCWHPSCFVCSTCNELLVDLIYFYQDGKIHCGRHHAELLKPRCSACDEIIFADECTEAEGRHWHMNHFCCYECETVLGGQRYIMKDGRPFCCGCFESHYAEYCESCGEHIGVDHAQMTYDGQHWHATETCFSCAQCKVSLLGCPFLPKKGRIYCCKACSLGEDVHASDSSDSAFQSARSRESRRSVRMGKSSRSADQCRQSLLLSPAVNYKFPGMFGNADDTLSRKMDDLSMSRQGAGFDNDTWKARDEQETAEDHEEWAEHDDYMTQLLLKFGEKGLFQQPPEDNRSNDHWMSENIKGKNDLQRNNRNQSLASKKYQSDMYWAQSQDGLGDSAYGSHPGPASSRKLQELDMDHGASGYMHEKMPWYKRSLECLSNNLKPQNENICDSMDSLALSNITGASVDAESKSRPSLFSYQNFQELNTRDFDKMSNMGTLNSSMLNRSTESLKSLNSEICQEKPPPEEKPMHTSALKRSKSQTRPQVKFSDDVIDNGDYSSIEIRRPPMSERSRRRVYNSEEQSQRPHHHHHHRRRKSRKSRSENALHLATDSKSSGKERKRSYTAEDYERLFHNKSAHEVQAYIQNADLFGQYSNAASNVGLPSQVVDKFLGLYGEDEDSWCSTCSSSSSDSEEEGYFLGQPIPKPRPQRYQYFSDDLCSPTNALSSSQFSQRTSKSKKKKGHKGKNCIIS
The following text describes a protein:
Function:
Involved in skeletal muscle differentiation. May act as a scaffold protein for AKT1 during muscle differentiation.
Subcellular Localization:
Cytoplasm. Golgi apparatus. Cell membrane. Note=Before differentiation of muscle cells, localized to the Golgi apparatus. During muscle differentiation shuttles to the plasma membrane.
Sequence:
MEALEVDDISPALEVTEEFFSTLDSNLEKAVQQAEVYGIQEVPELVGHEVLSNITDNGAMRNVTSLGKGGMIWDHCKSRLLETKAQNVFPAKEQFMVQRGTTPDNLSWMEQKEASTFNFFNICQRRRDRPRSVNDLLDETSTFKPGHARSRSDITQVDWRVVLKTTPLQQQQQQQPLLQGPHVTRPSFLLPSPNKIEDAQGNTEHKQTFPNILKKGYLEIRKDHDSYWQSCYAELSPYNLYFYSLDSSGNQNLYATYQLSHFQSISVLGNLEARMVDTVLYDNTQLQLKAESPWEALDWGQKLWEVVHAAVPGYMGRQNELTISPGLGHHDDYTQNHSFQKKTSGLLPPSPVLDSSKQYQNILKSGTLYRLTVQNNWKAFTFVLSRAYLMAFQPGKLDEDPLLSYNVDVCLAVQMDNLDGCDSCFQVIFPQDVLRLRAETRQRAQEWMEALKIAANVARSSEQNLQVTLRNKPKDQMGGHELRKNKRQSVTTSFLSILTTLSLERGLTAQSFKCAGCQRSIGLSNGKAKVCNYSGWYYCSSCHVDDSFLIPARIVHNWDTSKYKVSKQAKEFLEYVYEEPLIDIQQENAMLYHHAEPLAAVLRLRQRLKSLRAYLFSCRAAVAEDLRRRIFPREYLLQQIHLYSLADLQQVIEGKLAPFLGKVIKFATSHVYSCSLCSQKGFICEICNNGEILYPFEDISTSRCESCGAVFHSECKEKSVPCPRCVRRELQKKQKSFWQRLNMDESLEEACTMFELSYQNT
The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
METVATASPLLLGSPPKHSLSGPLRPPVSLPAVLNPTTPSTGTSPQRAFALPPIGPSSSSSTPLRVGVLEFRIYNIFAKTSPLTFHLAPPRPTLPLPPPPHPHTHTHTHLFTSLSLSLSLSNSLSLSQTLKLSLSLSNSLSLKLSQTLSNSLKLSQTLSLSNSLKLSQTLSNSLKLSQTLSNSLKLSQTHTRAKTAAGGGRQRFSSRERFEHRRQKNKGGSGQGQGGEGQRGQRRPAAAPTEPSRPHSDKRGSSGSRPAASLDKSGSAGPHAARVNGAAPDKTERAKPAAPSSKSSSQTPSASGPSTHQHQRGKTSMLFGKNDDPTPGAKAPKTVGKRNTREVKVMTALSFEDLNIADRLRETLQTMNLNRLTLPQQHATPLLLQHCDVMLKSPTGTGKTLAYAIPIVQDLQGLQHKVERSDGPLAIVLTPTRELAQQSLEVIQQLLKSFNWIVPGAITGGEKKKAEKARLRKGINILVATPGRMMDHIRTTKALQLKSVRWLILDEADRLLDSGFEQTVKDIVGALNQARAKTNKAMRRTNALVSATLTPKVLRLAKDITTDTYFVDTTSETEAKRVYKLKNLSAPELTEESDDKDKPEDESKTAPKASTAEPKAPASQVSTVAEVDEADVIMGAGDDAEARVYISTKLTQYYTVVPPKLRLVAMLAYLRKTCIKNKALVFVQSRDEAAFYAELFTKLQQPKEGAGFSADRILTGVELYFLHGGMEQKDRTASYRAFCKATHGALICTDVAARGLDIPRVSGVLQTSCAPTVADHVHRVGRTARLEAGGEATLFVLPTELEYLQVLEKEQLSLTALDVMDLLTSLTLHRGDRDVTKQVASRVQMACEENTTQEAMHTRAVAAFTAYVRAYATYPSAMKGIFHVKHLHLGHLAKSFALREAPQGLQGAGGKGASKAAQAKKSKLTAKQKMMQNAKRVTAAASDEFSGGFAGAGARAPKRRRGMGQ
The following text describes a protein:
Function:
Functions as a zinc transporter.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MDFKSRYESSLTLTKFFGSLPLLVAFPLVFLSHSLSTTSFEFAYENTILLNIFLASACLSIVILAHRLNVLPISNATATTSGSNKMSTMYLLSTFYVIYTSASFLPANRVAVLYLGLFLNSWNLYTPLAFVLDCYTNFKEFYGLHIVFTYALVILGYYLLSSKLNSSSLSNLLSSLDKPTVFGTFIFSALALVFYNPSMFNFSMIGVNLATFIVFMISVQEFQMRDSRLSSVFVSLLLELLQYVVLLQQPSFSQIINIGLAAVVTPDKSYHFEQDEEKGTDQGHKITNNSAPILKELMGHSDTRAIFNFLLLNATFMFVQFLYSFRSKSLGLLSDSLHMALDCMSLVLGLIAGVISKHEIDSNGKYPFGLKNFEILAGFTNGTLLVGISGSILFEAIGRLFNPVHLQKTTELIIVSILGLLVNLVGIFAFNHGHSHGHSHGHSHGSSHSHEHSHGHSHEHSHAPNCDSEDEHDHMNDNMKGIFLHIMADALGSVGVVISTILTKYFSWDGFDPIASIIIATLIFVSAVPLIKSTASTLLLSISKTKEDQIRNILHEVQQVKGVRSLTTPRFWPGPRNNVCGYVHIQVYRGENTSYIKRQCEKMFESRNMDVMLQIENDYDDCWCRK
The following text describes a protein:
Function:
Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis.
Subcellular Localization:
Cytoplasm.
Sequence:
MGTETKSNSYTGQISTSGGNPKVMKDSLSLVRQTVNQQTLSLSQSNQVQNQLNSHSNSNSYPNPSGSENKNENEQNSRDIRAKPEDKSRKEAIVPFVPIFVEEADVIQGAKELLKVIRPTWDLSHVEFKIRVVPQIEDRYPAQNAMVMMTLYSFTDGITNKLVGCFHKEISKLNDENGGSYLPIKTQGLSPVQSEDPVIIEKEDDDEFTDDRAADDGSPVQYSDNVVLVRIYGNKTDLLIDRKAETQNFLLLHTYGLAPSLYATFKNGLVYEYVPGTTLNTDSVLCPEIWPLVARRMAEMHRKVRKHGDSSATKPMPMIWKKTQSFLDLVPERFSDAEKHKRVKETFLPIGRLREEFNKLYEYLEALDSPIVFSHNDLLLGNVIYTQSLNTVNFIDYEYADYNFQAFDIGNHFAEMCGVDEVDYSRYPKREFQLQWLRVYLEEYLQRSNIQNDEVELLYVQVNQFALASHIFWTVWSLLQAEHSTIDFDYVGYAFLRYNEYLARKVEFLSLTAAKNNK
The following text describes a protein:
Function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus.
Sequence:
MKSRLKSYRRKKLGLATVIVFCSLCFLFGFYGSTLLSQNVPRVKPRLRMLDMVENGEEEASSMPHGVTGEESIGSIPFQVLSWRPRAIYFPNFATAEQCQAIIERAKVNLKPSALALRKGETAENTKGTRTSSGTFISASEESTGALDFVERKIARATMIPRSHGESFNILRYELGQKYDSHYDVFNPTEYGPQSSQRIASFLLYLSDVEEGGETMFPFENGSNMGIGYDYKQCIGLKVKPRKGDGLLFYSVFPNGTIDQTSLHGSCPVTKGEKWVATKWIRDQDQEE
The following text describes a protein:
Function:
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate (By similarity).
Sequence:
MGIPDGSLLDLIDKVRSWITSDSSDSLFLLSSSKQDFGIMPIVSKMCHDCGTKVEQGYCCLSCGSCWCKSCSDTEESKMKLCRECDAEVRELRVKSYDKVHPRDSPDPPSSLATESESLASSLEIRDCRNMASIRCYPSRGEEEEARYCGKQLLSPSSDNYQDSSDIESGSVSARHELFSCKSSAGSSPHDSPLRNNFSPLGRFVQHAKDLRSPTVCSFDNHQEQLLADNLVKPGQGVLEQEDHEEEEDKLQQPLDFENNGRIWYPPPPEDENDDAESNYFHYDDEDDDIGDSATEFSLSSSFSSHIPTKEKLGENSNEPLRTVVHDHFRALVAELLRGEELSPSDDGSAGEWLDIVTALAWQAANFVKPDTRAGGSMDPGNYVKIKCVASGNQNESILIRGIVCSKNITHKRMISQYKNPRVMLLAGSLEYQRVAGQLASFNTLLQQENEHMKAIIAKIESLRPNVLLVEKSASSYAQQYLLEKEISLVLNVKRSLLDRIARCTGAVLCPSLDSISTARLGHCELFRTERVLEQHEAGNQSNRKPSRTLMYFEGCPRRLGCTVVLRGSCREELKKVKHVIQYAVFAAYHLSLETSFLADEGASLPKIRLKQPGMVRTASQRRIIDEGISLITQSPTETDSQALLETAAHEDEHTAPMPEHEVCESLCEDFDPTQIFPPSSEVETEQSDTLNGDFANNLVTRSYSSNQLNDLHEPTLCLSSEIPETPTQQPSGEEDNGRGEEENQLVNPQDLPQHESFYEDDVSSEYFSAADSHQSILVSFSSRCVLKESVCERSRLLRIKFYGSFDKPLGRYLKDDLFDKTSSCRSCKELVDAHVLCYSHQNGNLTINVRRLPSMKLPGEQDGKIWMWHRCLRCAHVDGVPPATRRVVMSDAAWGLSFGKFLELSFSNHATANRVASCGHSLQRDCLRFYGFGNMVAFFRYSPINILTVLLPPSMLEFNSHPQQEWIRTEAAELVGKMRTMYTEISDMLNRMEEKSSLLEPEQSEACDLHSRIIGLIDQLVKEKDEYDDALQPIFEENLQIQGSLDILELNRLRRALMIGAHAWDHQLYLLNSQLKKASVFKTGDDNAPRNPEMHDPPKIDRRMQEGSDERDEQSHTDSEANGDNKDPENIPSPGTSLSERIDSAWLGSFQNLEKAETIAETEGFSAVNSSLRRLARPIRVQSFDSAIRFQERIQKGLPPSSLYLSTLRSFHASGEYRNMVRDPVSNVMRTYSQMLPLEVQKLDLIVGSAPTYISSASQMADGARMLIPQRGLNDIVVPVYDDDPASVVSYAINSKEYKEWIVNKGLASSSSSSNLNNRESEPSAFSTWRSLSMDVDYIQHAVYGSSQDDRKSPHLTISFSDRASSSSTATEGKVKFSVTCYFATQFDTLRKTCCPSEVDFVRSLSRCQRWSAQGGKSNVYFAKSLDERFIIKQVVKTELDSFEDFAPEYFKYLKESLSSGSPTCLAKILGIYQVSIKHPKGGKETKMDLMVMENLFYNRRISRIYDLKGSARSRYNPNTSGADKVLLDMNLLETLRTEPIFLGSKAKRSLERAIWNDTNFLASVDVMDYSLLVGFDEERKELVLGIIDFMRQYTWDKHLETWVKASGILGGPKNASPTIVSPKQYKRRFRKAMTTYFLTVPEPWTS