lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins.
Subcellular Localization:
Cytoplasm. Nucleus envelope.
Sequence:
MYNNNGFHEETNIDESQFTVEKVETVLKSLYFPQNNDYSALPQIQQWLIQFQKSFSSWSIAPLLLMSNIKEIQYFGASTIENKIKNNWLSLSQDMKKEFLDNLLLFLKTQITKCSTVVITRLCLAVSVIACHSTTDLWANPILDVLQLSFQDINNLDCFNPNLVNLTLELLTIFPEELTNADYITQEKRNKVGLQFNKHNSKVFEILCKIMSLPQNQQTLIFMKSSLKCFKSWILFDCSPREYLIDSDLILKCFEAVSNNPKLVEDFLMVLDEMFTFMGGKIFRSYTSAFSLVLSRILMIFPSFYILALQEENQIFNQIFLLFSHIAENHIKTLLKNPELSNNFFKALIQMALKGDFETCELLSPVITEIAALHELHSTSSTTEATTTTIATTTTPTTTSDCDISGWYQYLGEMVEVFRLKSMYPLDKDISDLYEEDAEKFFAFRVIAGDSVLEVYNILEGKILQQLLNSLWSDIQSFPTTKCWQSIEATIYLLSCLSESITEDTEFVPQLFSILGQLPIQSTPLIKSTMTLAGNYSNLIDKSTIFLEKIVKDFFPAFENPDLKSVASQSFLSISKNSKCASILSNSITQLISLCAPILSNNNKILDDPSNFNILEALLYIISTLPSDSQVLNYSTQLLYPFILFIKNYYTNQLQQQQQQQQQQQTELRLLLSSINLLTKFCKIYDDEQVNEYGTTQQENNNNNNNNNNNNNNNNNNNNNNNNNNIKPVFEIINNIIPIYGELLSLNTLESSIIEAISIFYKKAIMINNNHQNITNIPEINRQLTLAFLKHKPLSLVLSTLSISIVNLPKEQHLDFLADSLSSISSKMIQIWSEKSNQNNKKNNKKINNNIDIDNDNENNNNNNQIQFENNELNEFKNLKISIYPDITKEYFTMITQYIRYNAVSIPQGVISHLFSIILVNITKIHDKVTARACFSFMALIITKSKEMKSQIKWEPLLNEINGWLSIHGELFIKQILYSAGGGIPRSVVQFISEVIASLVSSYPDVFRISALKCLSVDGFPSSNITKEQKEKFLNSLMLYRSKKLPLKIVTDFSLVSLGIATNQ
The following text describes a protein:
Function:
GTPase-activating protein (GAP) for Rho1; functions with the ERM protein Moe to regulate Rho1 and control proliferation in the developing epithelium. Recruited by Moe to the cell cortex where it negatively regulates Rho1 activity. Can also promote cell proliferation independently of its GAP activity, perhaps by acting with Arf6 to positively regulate Rac1.
Subcellular Localization:
Cytoplasm. Cell membrane; Peripheral membrane protein. Cytoplasm, cell cortex. Cell junction. Note=Recruited by Moe to the cell cortex. In the epithelium, predominately expressed at the apical cortex.
Sequence:
MNSNTDLHHSDDQDFSEFLNEYYLQSNSQSIEPEASYEDGEMEAEWLVSAGYPELTKPFEQGLEVSKKDLEPILTTLSKPHAEAIVQLVRTLNKTVRVRTKSRPKRKPDIRDVFREFDEQGTVTRSRSATPDSLDSLQIDEAWTNNSLPTFVNVYEKNTETAIQCVEQSNEIYLKQNLRRTPSAPPKSGTYADIFRGSQVRCDIPLYSADGVELLGYSRIGTIQFPRNRSVSDPFCSIGRSKESRSENDARSQKKKSSEVLSASENECGRLLPMPYNVLSFESICRDSSSLDSCEVLDTCDIPSTLFTDVVLISETDMKRLQTILWLELATIFDRNKVSLDKRKPFKRRRKEEGNLFGVSINALIRRDQQVTGTDSSLVPLFLEKLIGELLRRGSREEGLLRIGGHKQKTELLYNELESTFYQNPDNLDNLFRTATVHELSSLLKRWLRELPQPLLTNELIQLFYQCHTLPSIDQMNALSILCHLLPPENRNTLRSLLSFFNIIINLKDINKMNVHNVATIMAPSMFPPRYIHPSDNNSIAEQVRMAAQCCRLTNILILRGEKLFQVPNNLIVESQKTMMGKKGWHRHRNSNEITAKPSGKASNVGVGHDSTVINKYSTNLKHLHPFVI
The following text describes a protein:
Function:
Part of TspanC8 subgroup, composed of 6 members that interact with the transmembrane metalloprotease ADAM10. This interaction is required for ADAM10 exit from the endoplasmic reticulum and for enzymatic maturation and trafficking to the cell surface as well as substrate specificity. Different TspanC8/ADAM10 complexes have distinct substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRRYFWSKGFPWFRRDPSKNEFSPLLPKSGAAGGDDKEVDLETGTHQTETNNGQDLKSPTWIQTHYSYSWMDYFLKYFLFLCNLAFTVFGLMVLGLGMWGLISKESFAQERIGSIGTDPMLVLVSLGFLLAVLCLTGCVGAIRENSCLLRLFSGILLILITVQVLIAIMAYSMQDQIEVYMRSGMLAAMAGYQDDLDLRFITDEIQTNLQCCGADTYRDWETNIYYNCSSPGVLACGVPATCCVDPLDNGTVWNSQCGLGAQRLDEFTAQSTIFLGGCIGGISRWIELNQGLVGAVAVVVLGVQILAVFITTRLLESINWHKMHA
The following text describes a protein:
Function:
Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]GATT-3'. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Could directly activate some type-A response regulators in response to cytokinins (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MEKSGFSPVGLRVLVVDDDPTWLKILEKMLKKCSYEVTTCGLAREALRLLRERKDGYDIVISDVNMPDMDGFKLLEHVGLELDLPVIMMSVDGETSRVMKGVQHGACDYLLKPIRMKELKIIWQHVLRKKLQEVRDIEGCGYEGGADWITRYDEAHFLGGGEDVSFGKKRKDFDFEKKLLQDESDPSSSSSKKARVVWSFELHHKFVNAVNQIGCDHKAGPKKILDLMNVPWLTRENVASHLQKYRLYLSRLEKGKELKCYSGGVKNADSSPKDVEVNSGYQSPGRSSYVFSGGNSLIQKATEIDPKPLASASLSDLNTDVIMPPKTKKTRIGFDPPISSSAFDSLLPWNDVPEVLESKPVLYENSFLQQQPLPSQSSYVANSAPSLMEEEMKPPYETPAGGSSVNADEFLMPQDKIPTVTLQDLDPSAMKLQEFNTEAILRSLNWELPESHHSVSLDTDLDLTWLQGERFLANTGLQFQDYSSSPSLLSELPAHLNWYGNERLPDPDEYSFMVDQGLFIS
The following text describes a protein:
Function:
Catalyzes the transport of the major hydrophobic bile salts, such as taurine and glycine-conjugated cholic acid across the canalicular membrane of hepatocytes in an ATP-dependent manner, therefore participates in hepatic bile acid homeostasis and consequently to lipid homeostasis through regulation of biliary lipid secretion in a bile salts dependent manner. Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts. Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Recycling endosome membrane.
Sequence:
MPNESVKLRSIKKLGHDNNSYQVTDEEQAGSYMTISNSRGTEKAQEKENQPAIRVGFFQLFRFATCKDVLMMVLGSVCAVLHGSAQPLMLLVFGLLTDTFIDYDIELQELSDDRKECVNNTIQWKRNYTGTLDMTLPLNQSFGSLINSTLEMFTPLSNMSCGILDIEHEMTLFALYYVGIGAGVFLLGYFQISLWVTAAARQIQLIRKLYFTKVMRMEIGWFDCTSVGELNTRLSDDINKINDAIADQVSIFVQRFTTFVCGFCIGFVKGWKLTLVIVAASPLIGIGAGLMALFVAKLTGMELQAYAKAGAVADEVLSSIRTVAAFGGEIKEVERYDRNLVSAQRWGIRKGLIMGFFTGYMWLIIFLCYALAFWYGSTLVVDTAEYTPGTLLQVFFGVLVAAMSLGQASPCLEAFAAGRGAATIIFETIDREPQIDCLSESGYKLERVKGDIEFHNVTFHYPSRPEVKILDQLSVQVKSGETTAFVGPSGAGKSTAIQLIQRFYDPLEGMVTLDGHDIRGLNIQWLRSLIGIVEQEPVLFATTIAENIRYGRPGVSMDDIINAAKEANAYNFIMDLPQKFDTLVGEGGGQMSGGQKQRIAIARALVRNPRILLLDMATSALDNESEAVVQEALDKVRMGRTTISIAHRLSTIKNADVIVGFEHGRAVERGKHNELLERKGVYFTLVTLQSQGDKALNEKAQQMADSEKQEPERLNLSRAGSYRASLRASLHQRSRSQLSNLIPESSINVAGDLGLRTYSVSPSEKYDKATPEEEEEQVEPAPVARILKYNAPEWPYMLFGSLGAAINGGVNPVYSLLFSQILATFSVQDPAAQRREIDGICVFFAMVGVVSFFTQMLQGYAFSKSGELLTRRLRRIGFHAMLGQEIGWFDDHRNSPGALTTRLATDASQVQGATGSQIGMIVNSLTNIGVAVLMSFYFSWKLTLLILCFLPFLALSGGFQAKMLTGFAKQDKQAMETAGRISGEALNNIRTIAGLGKEKNFVEMYEFQLDAPYQAALKKANVYGACYGFAQCVVFMTNSASYRFGGYLVKQEGLHFSLVFRVISAIVTSGTALGRASSYTPDYAKAKISAARFFQLLDRIPTISVYSDKGDKWNNFQGNIEFIDCKFTYPTRPDIQVLNGLTVSVKPGQTLAFVGSSGCGKSTSVQLLERFYDPDHGKVLIDGHDSKHVNVPYLRSKIGIVSQEPILFDCSIAENIKYGDNSREISMDEVILAAKKAQLHDFVTALPEQYNTNVGSQGSQLSRGQKQRIAIARAIIRDPKILLLDEATSALDTESEKTVQEALDKAREGRTCIVIAHRLSTIQNSDIIAVMSRGILIEQGSHDQLMGLKGAYYKLVTTGAPIS
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). Required for development of the body axis, brain, ear, kidney, forelimb and neural crest and for pigmentation. Acts as a coactivator for sox9a and/or sox9b promoting the expression of several neuronal determination genes.
Subcellular Localization:
Nucleus.
Sequence:
MAAFGVLSYEHRPLKRPRLGPPDVYPQDPKQKEDELTALNVKQGFNNQPAVSGDEHGSAKNVNFNSSKISSNFSSIIAEKLRCNTFPDTGKRKPQVNQKDNFWLVTARSQSSINNWFTDLAGTKPLTQLAKKVPIFSKKEEVFGYLAKYSVPVMRSAWMIKMTCAYHAAITENKMKKRHVIDPCIEWTPIITKYLWEQLQKVAEFYRQSPSQGCGSPLPAPPAEVETAMKQWEYNEKLAMFMFQDGMLDRHEFLTWVLECFEKIRPGEDELLRLLLPLLLQYSGEFVQSAYLSRRLAYFCTRRLNLLLSDGSIGPGPGGHQAHGISAQQGNALPPTPTSQPAGGNQPQTPFTDFYICPQHRPVVFGLSCMLQSIVLCCPSALVWHYSLTDSRNKTGSPLDLLPIAPSNLPMPGGNSTFNQQVRAKVREIEEQIKERGQAVEFRWSFDKCQETTAGFTISRVLHTLEVLDNHSFEKSDFSNSLDSLYNRIFGSGQSKDGHEMSPDDDAVVTLLCEWAVSCKRSGPHRAMVVAKLLEKRQTEIEAERCGESEVVDEKGSVSSGSLSAATLPVFQDVLLQFLDTQAPVLTEPGNESERVEFSNLVLLFYELIRHDVFSHNIYMCTLISRGDLASNSHLPRPRSPSDEPSDESERKDQDAGSSVKMEDTGMSESMEIDHNSSANFDEMFSPPMHCESKGSPSPEKQAQEQESKSTAKDKGMDPAFPLVYEQPRHIQYATHFPIPQEESASHECNQRLVVLYGVGKQRDEARHAIKKITKDILKVLNRKSTAETGGEEGQKRKRSKPEAFPTAEDIFSKFQHLSHFDQHQVTSQVSRNVLEQITSFALGMSYHLPLVQHIQFIFDLMEYSLNISGLIDFAIQLLNELSLVEAELLLKSSNLAGSYTTGLCLCIVAVLRRYHSCLILNPDQTAQVFDGLRIVVKSGVNPADCSSAERCILAYLYDLYTSCSHLKSKFGEIFSEFCSKVKNSIYYNIDPSDSNMLWDQMFMIDAITNPTAHNLNHSMLGKITNELNDSPANRYSFVCNVLMDVCVDHRDPERVNDIGILCAELTAYCRSLSAEWLGVLKALCCSSNNGNCGFNDLLCNVDVSDLSFHDSLATFVAILIARQCLLLEDLVRCVAIPSLLNAACSEQDSEPGARLTCRILLHLFRTPQRNPCPQDGTKSDKSIVGIRSSCDRHLLAASQNSIVVGAVFAVLKAVFMLGDAELKGSGFSHPAGLDDIGEDDMGSKKSGGRNVSIETASLVVYAKYVLKSICHQEWVGERCLKSLSEDSSALQDPVLVNIQAQRLLQLICYPHRQLDSEEGDNPQRQRIKRILQNMDQWTMRQSSLELQLMIKQSSNNELYSLLENIAKATIEVFQKSAEMNSSNPSWNGSAVSGSSVSNSNSASKLKPVLSSSERSGVWLVAPLIGKLPTSVQGHVLKAAGEELEKGQHLGPSSRKERDRQKQKSMSLLSQQPFLSLVLTCLKGQDEQREGLLTSLYSQVQQIVTNWREDQYQDDCKAKQMMHEALKLRLNLVGGMFDTVQRSTQQTTEWAVLLLDIISSGTVDMQSNNELFTTVLDMLSVLINGTLAADMSSISQGSMEENKRAYMNLVKKLRKELGDRQSESLEKVRQLLPLPKQTRDVITCEPQGSLIDTKGNKIAGFEKEGLQVSTKQKISPWDVFEGLKHSAPLSWGWFGTIRVDRKVTKFEEQQRLLLYHTHIKPKQRSYYLAPLNLPQEEEEPLTPVPPEPDKKLDTAKVEKSVSNVPTKKKKKKPASTVKQEDYKPHNTVMQYAPGMTPDLPLSMGQTNMSYRMGYQAPMNMYAQNQPLPPGGPGLEPPFRPRVPMNKMPPRPNYTMPNMQTAGMGNLMGMEKQYQMNYKPMPNMAQGQMLRHQLQGHNHLIGQQIRQVTPNPQYSSMQPAQNIPQGYTSYGSHMGMQPHPSQTPGMVPNSYGNQGFQTGHPATNPTMVDSIRQMQQRPGYVHQQAPAAYGHTIQSTQRFPHQSMQQTPMMHGLAQSHLGVQGIHPNMRPNQMMEQQQQQQQQQQQQQQQQQQVHQQQQHIRQGPVFRPQQQQQVQQQVQQQVQQQQVQQQQVQQQVQPQQVQQQQVQQQQQQQVSAAQPPAQALGMQALPPQQPMFQRQGMQQTQQQQQTAALVRQLQQQLSSTQPAQNNSSYY
The following text describes a protein:
Function:
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
Sequence:
MTTYGSFPGARPRRLRTTPVMRRMVAETRLHPADFILPAFVREGVSEPVPIAAMPGVVQHTRDTLKKAAAEAVEAGVSGIMLFGVPEDGKKDAAGTAGTDPDGILQVALRDVRAEVGDELLVMSDLCLDEFTDHGHCGVLDGQGRVDNDATLERYAEMAQVQADAGAHVVGPSGMMDGQIGVIRDALDQIGREDVAILAYTAKYASAFYGPFREAVGSSLKGDRKTYQQDSANARESLRELALDLEEGADMVMVKPAGPYLDILAKVAEASDVPVAAYQISGEYSMIEAAAEKGWIDRDRAILESLTGIKRAGARNILTYWATEVARTLR
The following text describes a protein:
Function:
Protein involved in secretion and cell wall organization. Contributes to cell surface-related functions as a auxiliary component of MCC/eisosome that specifically interacts with the secretory pathway.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Localizes to punctate patches on the plasma membrane that are largely co-localized with the plasma membrane microdomains named MCC (membrane compartment of CAN1).
Sequence:
MKKNSSVVFFLVGLSQFVTMAFLIIGSITAPIFKQIGYSKYDEITYGTFGYCKEGSCSKASYNYHPDELSDSDSNWKLNSNARSILGKIIFITPIAAGLNFLGFLCTIMSVLLINVLSSDRVGSASAIMFFVNLTFSTLGFLSASLICIVVFLLFYPHVTWCSWVLIPGAALSLLVIPLIFSAYSRSSGSRDDDETEELEEKGMLLNDPYLSSKSGRFDIDADSEANLRGDSRTNLLGDNFKNGTNITVVPDIISHNQDPKLSNITTSTTSDISTFDKEAKDMENSNGSGLNEEEDDGMAYDKRRSTSTYSVIESESGLKNGSVSNNYVRNNGSNTSNNINYKVPLGKTEISSSASLASSDYSQREVIPHRNPSRLLNDIMETSFNEPNDSHINSMSSYNDKDSTLTSISQRGVNPEVYNQMPRETAAGPANIRPYAGQPHPAPLVYPQQRLQPQQQQPQQQYHQYNLYQRTTPAGPDPSNVILQSNPYFNVAPNQVPQHRNPVPGVGFAPNPLPNQSPITQGYKPAYKRRMQNKNLPRATTSLNNPYGFR
The following text describes a protein:
Function:
Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the eighth mannose residue in an alpha-1,6 linkage onto Man(7)GlcNAc(2)-PP-dolichol to produce Man(8)GlcNAc(2)-PP-dolichol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus.
Sequence:
MEGERGVPNYMLQVSFSSSTPPPQAIHETGFLQFEENQVMSFLSPSQPLTTSPVSNTTNSTTALRFITHNDQVGTLDPIPKAVHDENCGSNVKDGNNNSWWRSSALEKNKVKVRRKLREPRFCFQTRSDVDVLDDGYKWRKYGQKVVKNSLHPRSYYRCTHNNCRVKKRVERLSEDCRMVITTYEGYDLLLVSIAAFYVLMVPYTKVEESFNIQAMHDILYHRHHLDNYDHLEFPGVVPRTFIGAFLVSIFSSPIVLAVQLLHLPKIYSLIIVRLALGCIILSTLRFLRIQVRNKFGHQVEAFFVIFTAIQFHLLFYCSRALPNILAMGVVNLAYGHWLKGNFYTALNYLVFATTIFRCDVVLLLCPLGLELLLTKSISFWRAFKCCTVTTLLCIGLTVLVDSIMWKRFLWPEFEVFWFNSVLNRSSEWGTHSIHWYFTSALPRSLLTAYPLFMLGVLLDRRLLPLVLPALSFVVLYSKLPHKELRFIISSVPIFNLSAAVAASRIYNNRKKSFWKFVNLVMLGLLLISLGCTIITFMASYENYPSGRALKELHQIGHLANKSNELWVHIDPFSAMNGISLFCENEWPWRYSKEEEITLEEFGQRNFTYLINEHRTIDGYKCLFYVNGFSRLRRQSGFPPIILDKEPKVYIHGNIKNEELMLKPWPGCS
The following text describes a protein:
Function:
Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-4-phosphate or ribose-5-phosphate, respectively. Could act as a stress sensor involved in adaptation process.
Sequence:
MASSSLHLSQAFLARAVYLNPEIRAASLSSTSSLSFPALKSSSSSKPPTSRRRTTPAIRATAVETLDKTTEASLVEKSVNTIRFLAIDAVEKANSGHPGLPMGCAPMGHILYDEVMRYNPKNPSWFNRDRFVLSAGHGCMLQYALLHLAGYDSVQEDDLKQFRQWGSKTPGHPENFETYGIEVTTGPLGQGIANGVGLALAEKHLAARFNKPDSEIVDHYTYVILGDGCQMEGISNEACSLAGHWGLGKLIAFYDDNHISIDGDTEIAFTENVDQRFEALGWHVIWVKNGNTGYDEIRAAIKEAKAVTDKPTLIKVTTTIGFGSPNKANSYSVHGAALGAKEVDATRQNLGWPYEPFHVPEDVKKHWSRHTPEGAALEAEWNAKFAEYEKKYKEEAAELKAIINRELPADWEKALPTYTPETPADATRNLSQQNLNALAKVLPGLIGGSADLASSNMTLLKSFGDFQKATPEERNVRFGVREHAMGAICNGIALHSPGFIPYCATFFVFTDYMRAAIRISALCEAGVIYVMTHDSIGLGEDGPTHQPIEHLASFRAMPNVLMLRPADGNETAGSYRVAVLNQKRPSILALSRQKLPNLPGTSIEGVEKGGYTISDNSSGNKPDVILIGTGSELEIAAAAADDLRKEGKTVRVVSFVSWELFDDQSDEYKESVLPASVTARVSIEAGSTFGWHKIVGSKGKTIGIDRFGASAPAGKIYKEYGITKEAVISAAKEVS
The following text describes a protein:
Function:
Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MEQEVYTALTFVELTTVHYQHDDPFGLFNAYVTLIPIAIAIGVITLILFRRDVRTISIFLGLLFSECTNYVLKKSIKEHRPTMWKELRKQSYGMPSSHSQFMFFFAVLMTLFYLKKRIRFGSKILPIISVTFLFFLAAGVAYSRVHLYYHTAKQVFCGSFIGICLGFIWYGVIEYIFRPYLFPIIINHPIGKYFYLRDSSEIEDLLNFEYTNVMNKVKTINKTKPIKTK
The following text describes a protein:
Function:
Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Subcellular Localization:
Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. Note=Stabilized by CcmD in the membrane.
Sequence:
MNIRRKNRLWIACAVLAGLALTIGLVLYALRSNIDLFYTPGEILYGKRETQQMPEVGQRLRVGGMVMPGSVQRDPNSLKVTFTIYDAEGSVDVSYEGILPDLFREGQGVVVQGELEKGNHILAKEVLAKHDENYTPPEVEKAMEANHRRPASVYKDPAS
The following text describes a protein:
Function:
Multifunctional protein involved in chlorophyll synthesis, plastid-to-nucleus retrograde signaling and abscisic acid (ABA) perception. In chlorophyll synthesis, catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step. In addition to its function in the Mg-chelatase enzyme, is required for the plastid-to-nucleus retrograde signaling. The plastid-to-nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. Has a role in mediating ABA signaling in stomatal guard cells and during seed germination. Binds ABA and is a positive regulator of ABA signaling.
Miscellaneous:
MISCELLANEOUS: Plants silencing CHLH show significant ABA-insensitive phenotypes in seed germination, post-germination growth arrest by ABA and ABA-induced promotion of stomatal closure and inhibition of stomatal opening. In contrast, plants over-expressing ABAR display ABA-hypersensitive phenotypes.
Subcellular Localization:
Plastid, chloroplast stroma. Plastid, chloroplast membrane; Peripheral membrane protein; Stromal side. Plastid, chloroplast membrane; Peripheral membrane protein; Cytoplasmic side. Note=Predominantly associated with the chloroplast envelope. Spans the chloroplast envelope and is its N- and C-termini are exposed to the cytosol.
Sequence:
MASLVYSPFTLSTSKAEHLSSLTNSTKHSFLRKKHRSTKPAKSFFKVKSAVSGNGLFTQTNPEVRRIVPIKRDNVPTVKIVYVVLEAQYQSSLSEAVQSLNKTSRFASYEVVGYLVEELRDKNTYNNFCEDLKDANIFIGSLIFVEELAIKVKDAVEKERDRMDAVLVFPSMPEVMRLNKLGSFSMSQLGQSKSPFFQLFKRKKQGSAGFADSMLKLVRTLPKVLKYLPSDKAQDARLYILSLQFWLGGSPDNLQNFVKMISGSYVPALKGVKIEYSDPVLFLDTGIWHPLAPTMYDDVKEYWNWYDTRRDTNDSLKRKDATVVGLVLQRSHIVTGDDSHYVAVIMELEARGAKVVPIFAGGLDFSGPVEKYFVDPVSKQPIVNSAVSLTGFALVGGPARQDHPRAIEALKKLDVPYLVAVPLVFQTTEEWLNSTLGLHPIQVALQVALPELDGAMEPIVFAGRDPRTGKSHALHKRVEQLCIRAIRWGELKRKTKAEKKLAITVFSFPPDKGNVGTAAYLNVFASIFSVLRDLKRDGYNVEGLPENAETLIEEIIHDKEAQFSSPNLNVAYKMGVREYQDLTPYANALEENWGKPPGNLNSDGENLLVYGKAYGNVFIGVQPTFGYEGDPMRLLFSKSASPHHGFAAYYSYVEKIFKADAVLHFGTHGSLEFMPGKQVGMSDACFPDSLIGNIPNVYYYAANNPSEATIAKRRSYANTISYLTPPAENAGLYKGLKQLSELISSYQSLKDTGRGPQIVSSIISTAKQCNLDKDVDLPDEGLELSPKDRDSVVGKVYSKIMEIESRLLPCGLHVIGEPPSAMEAVATLVNIAALDRPEDEISALPSILAECVGREIEDVYRGSDKGILSDVELLKEITDASRGAVSAFVEKTTNSKGQVVDVSDKLTSLLGFGINEPWVEYLSNTKFYRANRDKLRTVFGFLGECLKLVVMDNELGSLMQALEGKYVEPGPGGDPIRNPKVLPTGKNIHALDPQAIPTTAAMASAKIVVERLVERQKLENEGKYPETIALVLWGTDNIKTYGESLGQVLWMIGVRPIADTFGRVNRVEPVSLEELGRPRIDVVVNCSGVFRDLFINQMNLLDRAIKMVAELDEPVEQNFVRKHALEQAEALGIDIREAATRVFSNASGSYSANISLAVENSSWNDEKQLQDMYLSRKSFAFDSDAPGAGMAEKKQVFEMALSTAEVTFQNLDSSEISLTDVSHYFDSDPTNLVQSLRKDKKKPSSYIADTTTANAQVRTLSETVRLDARTKLLNPKWYEGMMSSGYEGVREIEKRLSNTVGWSATSGQVDNWVYEEANSTFIQDEEMLNRLMNTNPNSFRKMLQTFLEANGRGYWDTSAENIEKLKELYSQVEDKIEGIDR
The following text describes a protein:
Function:
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix, basement membrane.
Sequence:
SHWFAIGMQYRKNEYVLLPFTLHLITVSALASCLAQEPDLAHGCSHGSCYPATGDLLVGREKNLKASSTCGLRRKEPYCIVSHLQDEKKCFHCDSRRPYDPVYNTISHRIENVITTFKPHRKKSWWQSENGKSEVSVQLDLEAEFHFTHLIMTFKTFRPAAMLIERSADFGRTWQVYRYFAYDCASVFPGISHGPQRKVDDVICESRYSDIEPSTEGEVIYRVLDPSIPIKDPYSPNIQNQLKITNLRVNFTKLHTLGDNLLDSRVEIKEKYYYAIYELVVRGNCFCYGHASECAPIDGIRDDIEGMVHGRCVCKHNTKGLNCEQCEDFYNDRPWRPAEGRNTNACEKCNCNGHSSRCHFDMAVYQATGNVSGGVCDDCLHSTMGRNCEMCKPFYYQDPSRDIRDPGVCVACDCDPDGSLNGGICDGHDDSALGMIAGQCRCKDHVEGPRCDKCKPGFFGLSADNAQGCQPCQCDPRGTVSEGAQCDPVSGDCYCKRLVTGHNCNQCLPEHWALSHDLHGCRACDCDVGGATDNHCSMETGQCRCRSHMTGRQCSQVESGFYFMALDHYIYEAEVSHIGQGCSVVERELQPGRPPSWTGTGFVKVPEGSTLEFYISNIPFSMEYDMLIRYEPQLPKEWKEVRVTLVRPGPIPTSSPCGNTIPADDLLSVSLPSASRYVVLPQPICLERGVSYTLRLEFSRYLTREKVPNASILIDSIVLLPRYSSLEMFIAGDPAAISRKESFERYHCHDASKAVVRPQLSDVCAKLLNSMSAIIHDGALPCQCDPQGSVSSECDPRGGQCRCKPNVTGRRCDQCAPGTYGFGPAGCKPCECSQEGSRSRFCEQYSGQCQCRPGAFGPRCDRCQPGYWGFPNCRQCQCNGHAEDCEQRTGRCLACRDNTSGDKCERCINGYYGNPLLGSGGQCRPCPCPDGPTSGRHFAASCYQDNRNRQVVCNCNQGYTGSRCDECAPGYYGNPMQPGGRCQPCQCHNNIDITDPDSCDRRTGECKKCLYNTEGPNCEVCRPGYYGDATRRNCRKCTCNFLGTDRSQCSSRDECTCDRRTGQCQCLPNVIGQSCDHCAVNCWNLASGTGCETCNCDPNNAITPTCNEFTGKCQCRPGFGGKTCQDCQENYWGDPKVQCRACDCDPRGIETSQCNRVTGHCVCQQGVSGVRCDQCARGFSGQFPDCLPCHQCFGDWDRVVQDLAARTRALTERARVIQHTGLTGAYEKNFRELEEKLAQAQAIVNARNATAESIASLMDLIKGLRARIGETTDTLNQLEGELTSVQDSNFAASNQLSALEREARELNLSAGELGHQLDVLKNSNFLGAYDSIRGSFDKSREAERRANRSTTAVPSTVSQSADTRRKTERLMTEKRDDFNRKNAANKRALVDLKAKTQTLDMKKINEKVCGAPGDAPCGESPCGGAGCRDDEGKRHCGGLNCNGAVATADNALERAKHAEKELSKAMGEVEELFKKVAEVKTKAEEAKVRAQAALDKANDTKTKVERSNKDLRDLIKQIRDFLMQEGADPDSIEVVASKVLELSIPASPEQIRYLAEEIKDRVNSLSNVDAILEQTKDDVRKAEQLLQDARRARNRAETVKNTAETVKTALDDASRAQAEAEKAIQRAKTDLGQTENRLAEIQSETALSENNLKDAMDRLGTLGRQIDALKTKRANNSLVASRAEETATMARDKANEAKQILDGELNDKYKTVQDLVNMKGKTVQDAKKRAEMLRDEAKQLLKDAQDKLRRLGELERNYENNQKTLESKAKQLDGLEEKMRSILDAINQQIQIYNTCQ
The following text describes a protein:
Function:
Ring-cleaving dioxygenase involved in oxoquinoline degradation and utilization.
Sequence:
MQSLNVNGTLMTYSESGDPHAPTLFLLSGWCQDHRLFKNLAPLLARDFHVICPDWRGHDAKQTDSGDFDSQTLAQDLLAFIDAKGIRDFQMVSTSHGCWVNIDVCEQLGAARLPKTIVIDWLLQPHPGFWQQLAEGQHPTEYVAGRQSFFDEWAETTDNADVLNHLRNEMPWFHGEMWQRACREIEANYRTWGSPLDRMESLPQKPEICHIYSQPLSQDYRQLQLDFAAGHSWFHPRHIPGRTHFPSLENPVAVAQAIREFLQA
The following text describes a protein:
Function:
Postsynaptic density membrane protein that indirectly regulates glutamatergic synaptic transmission through lysophosphatidic acid (LPA)-mediated signaling pathways. Binds lysophosphatidic acid (LPA) and mediates its internalization into cells. Could act as receptor or a transporter of this lipid at the post-synaptic membrane (By similarity). Modulates lysophosphatidic acid (LPA) activity in neuron axonal outgrowth during development by attenuating phospholipid-induced axon collapse.
Subcellular Localization:
Postsynaptic density membrane; Multi-pass membrane protein.
Sequence:
MQRAGSSGARGECDISGTGRLRLEQAARLGGRAVHTSPTGGLGARQVAGMSAKERPKGKVIKDSVTLLPCFYFVELPILASSVVSLYFLELTDVFKPVHSGFSCYDRSLSMPYIEPTQEAIPFLMLLSLAFAGPAITIMVGEGILYCCLSKRRNGAGLEPNINAGGCNFNSFLRRAVRFVGVHVVGLCSTALITDIIQLATGYQAPYFLTVCKPMYTSLEGSCKENSYIVEEICSGSDLTVINNGKKSFPSQHATLAAFAAVYVSMYFNSTLTDSSKLLKPLLVFTFIICGIICGLTRITQYKNHPVDVYCGFLIGGGIALYLGLYAVGNFLPSEDSMLQHRDALRSLTDLNQDPSRVLSAKNGSSGDGIAHTEGILNRNHRDASSLTNLKRANADVEIITPRSPMGKESMVTFSNTLPRANTPSVEDPVRRNASIHASMDSARSKQLLTQWKSKNESRKMSLQVMDSEPEGQSPPRSIEMRSSSEPSRVGVNGDHHVPGNQYLKIQPGTVPGCNNSMPAGPRVSIQSRPGSSQLVHIPEETQENISTSPKSSSARAKWLKAAEKTVACNRGNNQPRIMQVIAMSKQQGVLQSSPKNAEGSTVTCTGSIRYKTLTDHEPSGIVRVEAHPENNRPIIQIPSSTEGEGSGSWKWKAPEKSSLRQTYELNDLNRDSESCESLKDSFGSGDRKRKHIDSNEHHHHGITTIRVTPVEGSEIGSETLSVSSSRDSTLRRKGNIILIPERSNSPENTRNIFYKGTSPTRPYKD
The following text describes a protein:
Function:
Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
Subcellular Localization:
Nucleus.
Sequence:
MTEKQQNSQQPSQLDSTASISALPPQLQQPAAGITGAPGNAEATTSEPPSTKRPRKAIESSEPLTEVILRRLTTIKEGDTVLLRLPSDLVKSVVVQGDNLVQLGKYGAFPASQLIGLHYDITYEIVSSSGSGASTPQPQSLDFSTEETQSKKGNKKNKNKGKDTAAVSKNNPGWNNILRPLKRQLVVDAVIDDIVETNEFIEDLSETEKTTLSHDEIAELRAQGCTPEEIIQAQIARHEKFGLKTDFSKEKWRRRKEKKFYQTVQPLAPSIPNVLYHYNLRSPQSILHLRDDTLSQLLTMANVRPGGRYLVVDDTGGLITAAVLERMGSEGSILLFNESDSPPAWGILQTMNFSDRELEPIKWLNWLEAEEEYQKPAPPVQAEPPTNPIKAAAKQRKYAAQVAELNNTRNELHLGGWDGLILATTLNPISVVARLTPYLLGSAPIVVYSPYYQVLAELLSWSKKDPNYLNDTLTESWERTYQVLPGRTHPMMTTSATGGYLWNATRVHPSQFQPESHQRFKRRKTGKAPGKEQLSSVAKDEEAVNESLEIDPEELANEGE