ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q46108 | MEVKAKQLDSVNATASVKIPSGMIKSEVENLAKKASKSVKMDGFRPGKVPVSAVLKRYERELTQDAEQNLFKSAVNSALQELKKENKELVGEPYFEKFDRKDGEIIAELILSFKPEIKLEGYEKLIPEYQTPKVSKKEIDEKKDELLKRFATPEAIKTKRALKEGDFAKFDFEGFVDDKAFEGGKAENYVLEIGSKQFIPGFEDGMVGMKIGEEKDIKVTFPKEYGAAHLAGKDAVFKVKLHEIQELKIPELDDEMLKKLLPGEEKASVEVLDEKLKEQIKNEKLFKLVNDELKGKFADALIEKYNFDLPKGIVEQETDMQMRAAFNTFSEKEIEELKASKEKYQEKRDSFKEEAQKSVKLTFIIDELAKLRKIEVNDQELIQAIYFEAYRYGMNPKEHLENYKKQGALPAVKMALIEEKLFNDIFIPKTEKSEKVSKKEKEDK | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50968
Sequence Length: 444
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q3AF97 | MKVTKETLEKSRVELTIEVEAEEVSKAYEKAYKKIAQKVVIPGFRKGKAPRVLVERHVGKEYILEEALDELLPESYVKAVNEAGIEPVDKPEVSLVSYGVNEPLVYKAVVDVKPEVELGQYTGLEVTKMPVEVTDEEVEKELEYLQNRYAKLITVEDGEAKFGDIVVIDFAGKMNGEPLEGGSADNYRLELGSKVFIPGFEEQIVGMKPGETKEINVTFPEDYQKEDLAGKPAVFTVTLKEIKRKELAPLDDEFAKDVSEFSTLAELKEDLKKKIAQTKENISREKMEAEVVEKAVDNANVEIPASMVNHEVEHILHHFEEELKYRRLTLEQYLNYQKKTLDELKEELKPRAERNVKTELVLEAIAKKEGITATDEEIDKELGKIAELYQQPVEEIKKLFAQRMDDLAYSIVRRKTIDFLVENAKAV | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48608
Sequence Length: 427
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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P0CAX0 | MQIVEKSGEGLSRVFGVTVPASELATRLEARIAEVAPQMNVKGFRPGKVPTAHVRRLYGKALMGEVIEQALNETTTKVLEDNKLRPAGQPELNPSSDMDKVIAGGEDLSFDLAVEVMPEFEPIDPTSIELVKPVYKVSDEEVQEALDELAKQARTYEPRTGKSLKAKDGDQLLIDFVGTIDGVEFAGGKAEGAELVLGSGQFIPGFEDQLVGAKPGDDVVVKVKFPEEYQAKDLAGKDAEFATKVQEVRAPVDGKADDELAKRLGLSDLAALTELLKSNLAGRYDNSSRFKLKRALLDVLDTKHDFPLPPRMVDAEFAGIWQQVEADKARGGLPPEDAEKTEDQLKDEYKKIAERRVRLGLVLAEIGRKNDVVVTDQELTDAIMREARQYGAQAQQVFDMYRQRADLQAALRAPIYEDKVVDLIFGKAKIEEKEVSKDELLEEDDLPEGYGG | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49767
Sequence Length: 452
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
P56420 | MNLEVKKIDTANARLSAKLSIENLEKRYDKIAQKIAQKVKIDGFRRGKVPLSLVKTRYQAQIEQDAQEEMIQEVLKNAFKELGIENKDLIGSPNLTKFEKKDTHFEIEADIGLKPTIVLDKIKECVPSVGVEVPNEEKIDERLKQLAKDYAKFVDTNTQRKAQNDDKLTIDFEGFIDNAPFEGGKAENFNLILGSKQMLEDFEKALLGMQAGEEKEFPLTFPSKYHAEHLAGKEAFFKVKLHQIQAREMLEINDELAKIVLANEENATLKLLKERVEGQLFLENKARLYNEELKEKLIENLDEKIVFDLPKTIIEQEMDLLFRNALYSMQAEEVKSLQESQEKAKEKRESFRNDATKSVKITFIIDALAKEEKIGVHDNEVFQTLYYEAMMTGQNPENLIEQYRKNNMLAAVKMAMIEDRVLAYLLDKNLPKEQQEILEKMRPNAQKIQAG | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 51989
Sequence Length: 451
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
A9AUT1 | MKVTTEQLPKRIVALEIEPDAATIEKELNKAAQRIASKVAIPGFRKGKAPRFIVENYYGKAAILEEATDEIINVAFRAALEQENIKPVAQASLEKLEPEPFRFRILVPVEPEVILPDYKAITVDLTEEPVTDATLEVALDQAREKHVVLSAPEGEPEAAEGDQLTATVQTLVDGVPLHKLDEEDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDEGEPTTLIMEERRIVPELYAGLKGIKAGETREISAHLPADHPDARVADKDVVFKVTVSEIQNRQLPAWEELPGLEEFEGDLDAYKADLMERLVKNSGDHHRRNVLNQYLEEVVAATSFDVPDALIAERAHELLHEQVESLARYGINMEQYLQIVGKTHDEAVQELLPRGEESLKSSLVVRKIVEAEGLSVDESEINAEIERILNDFPDAQRGPARRRLEKELRPQVAGSLLDKKLQDRLVELATGNAAA | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 53732
Sequence Length: 481
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Q31GF2 | MQVTVEKPETGLEHKINVTLPAGDLDSKVEQRLAQMRRTVKMDGFRPGKVPMSVVKKRYGGQVRQEMMGETVQQSFYDAVAKESLNIAGYPQFQELDEKDGHIVYSATFEVFPEVELPKFSSLKVETVTSEVTDKDVEKMVTRLREQKMAWKPANGNKKAKEGDQVIIDFVGKKDGEEFEGGKAEEVPLELGSGRMIPGFEDGIIGMKKNEEKTIEVTFPEDYQSDELKGQTVTFDITVHSVQTKVLPEIDEEFVKSFGIEEGTEEALVNEIRSNMEKELKRSVENKNRTAVLDALAEKVEVELPQAMVDQEASALMERQLEQFQQQGLKAEDIGLTAEAFKPEAEKRVKIGLVLGEVIKEYKIEATDEARQAFIQDQASSYEDPQEVIEWYAKNPQAQKEIDAILVEKEITNKILSEAKTKEVSKSFEEIVSPAA | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49093
Sequence Length: 436
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
B2GGB4 | MKSAVEKLNPTEAKITIDIAYTDLKPFVQETYKELANQIQIPGFRKGKVPSKLIDQRVGFDFVVENALNEGLNAFYQQALTENELTPLSQPQVEVLSKPEENDREADTKVEISVAIRPEIELPDYKGLEIQVEAREATAEDEQKALDELRARFGTLKTVDRPAAEGDHVTLDLQALVDGEEVDAANDLSYEVGSGTMLEGIDEAVTGLSAGEDATFETTLAGGEHSGAEATVKVKVTAVKERELPEADDEFAQLASEFDTIAELKEDLKKQAAESAVVEQGIEARDKVLDKLVELIEVPVPEKVIEDQLAQHFDSEQAQASAEPGHDTEEHRAEVRQNAENAFRNEIILDAVAEAEEVGVEQSELIDYIINMSQQYGMDPNQFAQMLDGSGQAGMMVGEVRRRKALAKVLETATVTDSNGETVDLSSFVGTGDDAETDEVETEASATE | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48943
Sequence Length: 448
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Q1IRD7 | MTTEASNPEVNATAEVAVPVNPLLRSVTVEIPSDVVDAERNKHVQQYAKLARVPGFRKGKVPPSVIRTRFAQDINEEIVRTLIPHYFREETGKQNLQPVSQPQVTDLHLHDGEPLKFTAEFEILPEIPTTGYENIKVEHPPVEVTDAEIEDTIKSLQEQRATYDPIEDRAAEDGDFVQISFEGRDKSDPEAKPVEVPSIMVELGGSNTVQEFTENLRGTKAGDEKTFDVVYPADYGDQRLAGKSVEYHVSVKSLKKKIFPELDEAFISELGADVKTPDELRAKIREGAEHEKKHHAEHEGKDKLVDALVKLNDFPVPESMVNSQIEIRLERGLRALAQQGMRTEDMKKMDFGKLREGQREAATREVKASLLLEKIADAEKIEVSDEELDRQIAGLARQSQQSPEQVRARLTQDGSLDRIRTQIRNEKTLDLLYSRSA | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 49200
Sequence Length: 437
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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C5CGV0 | MEKNVVKAEKNVEIVEFTFGPDEIAEAENEIVRYVNKNYTIPGFRKGKAPKRIIETFFGENFRDMVLEELSRKIEDTLKDEELFIPAVIADRKIEGDVAVFVVELHREPKVELKDYTGLELSVPKQEEVLANYVDNKLEELRNEAAIVEPKDGPAEIGDVINIEYTIEKDGKIIADHKTQEILIVEDDDRPIVTNVIGKKKGDIVEFDRTFENSNNKYHYKIEIKEVLKRTLMELNDEFAKSVASEVNTLEELKKKLEEEGLEAFESWKKDFLRQQVQDKLAELVELEISEKTLDYFVNRAIENAKKENTYDSYLKQAGSEEKLYEEFKTGILNELKKNTAIEKIAEKEQIEVTDEEVMKTAEELSTYWGISPERAKEIVKTREDIRNDIVENIRRTKVQDLIVEKATIKEISADEPVEEQKEEEEKEEAGSENSENKE | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 50877
Sequence Length: 439
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q88KJ1 | MQVSVENTSALERRMTIAVPAERVENEVNKRLQQTAKRAKIAGFRPGKVPMTVIRQRFEADARQEAFGDLVQASFYEAIVEQKLNPAGAPAVEPKSFEKGKDLEFVAIFEVFPEFTVAGLESIKVERLSAEVADSDLDNMLEVLRKQNTRFEAVERAAQNDDQVNIDFVGKVDGEAFAGGSAKGTLLVLGSGRMIPGFEEGLVGAKAGEERVVNVTFPEDYQNLDLAGKAAEFTITVNSVSAPVLPELNEEFFAQFGIKESTLEGFRAEVRKNMERELRQAIKTKVKNQVMDGLLAANPIEVPKALLENEVNRLRVQAVQQFGGNIKPEQLPVELFEEQAKRRVVLGLIVAEVVKQFELKPDDAKVREMIEEMASAYQEPEQVIAWYYKNDQQLNEVRSVVLEEQVVDTVLQKATVTDKSVSYEEAVKPAEAPAAAE | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48517
Sequence Length: 437
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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A9WUW4 | MKSAVENLSPTRVKLDVEVPFEELQPSIAEAYKTIAEQVQIPGFRKGKFPNRLIDQRVGRGYVLETAINEGLNGWYQNAVAETGLRPLSRPEVEITEVPDPAATDGELKFKVEVDVRPEVELPDYAGITVEVAPAEQSDEDRQKALDDLRGRFGTLKPADRPAAKDDFITIDINAKIADEDVDSATGLSYQVGAGTMLEGLDEAVEGLSTDEEAIFDTKLVGGEHAGEAAQVTVKLTAVKVRELPEADDDFAQLASEFDTIAELREDLVKQVNQSKTVEQGVEARDKVMEKLVELIEVPIPESVIEEQLEQHFDPANAHGEEDHDTEEHRVEVRENTERAFKNEIILDAVADKEEISVSQAELIDYIVNSASQYGMDPNQFAQMLDQSGQVPMVVSEVRRRKALAHVLGLATVTDTEGAAVDLSDFVKPAVDPELEAALNEAAGVTGEDDDTEAEEERVTVSADDPGAARF | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 51532
Sequence Length: 471
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Subcellular Location: Cytoplasm
EC: 5.2.1.8
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Q6F880 | MRSALPTFDEIWQRKFRHRLLIQAQQFPADTVFLIGCSGGMDSMLLLHLMSELFPHKVRAIYIDHQLQSSSRAWGVFVQNFAQQSHIPFTIQPVIVDTGNLENQAREARYAAFESHLKSNEVLVLAHHQQDQTETVLLRLLSGSGVKGLGAMKEIEQKKNICCWRPMLSVSRQQIEHWVEHLKIPYIQDLTNFDTTYDRAWCRETVWPVLQKRFPKMQEAISRTSILMQDADEILHEVLQQDLNQCGDLNHLDLSRLQQLSLARQRQLLSFWMKGKAIYRPAFEMVERVQQEVICAKADAKAALHWNHHYYVRYQNILYRVEKNKYLQKDLVSNVVSTIELQMDASLQLASGVFQIQPMQMGLSPQLFEQPLQLLPRQGGEKIHLYGRVGHWPLKKAIQEAQILPWLRHTIQILALDNVMLGVFTPKGFWLAQSSYCEAGGWQPNLISDVNYLRVEQNS | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 53230
Sequence Length: 459
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q8U9L7 | MPVDARTPNEKTVAPLAAASAFVESLRKPTHILVAISGGSDSTGLLLALQEAKAADDDGLRLSAVTVDHALRPESADEARKVAMLCAELGIPHTTRRWDGPKPASGLSEASRLARYRLIADVAREIGADLVVSGHTIGDQRETVAMRAARSGGSDNLGLSGMADAVLYDAHLWIMRPFLACERQVIRDYVSSRSRHWLDDPSNENIRYERVRVRQTLPHSPIALDDSTAVRRQMLSERTAVFLRERAQVFHAALARLADDDVNPDLPEFRHGLAALIAALGGRSYFPAASSMERVLRFLKTGETGRMTVGRVLLDRRRDGLYIFREQRNLPELQIESSGQAVWDDRFLVKNGSDFPINVAAGRVGTAAQAAALFPSAPSGVVKPAMAGLPQIAAAAEGWVSTPEVAITPRLAPFDLFLPRFDLELANAIANLFGRPAYPQPPV | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 48126
Sequence Length: 443
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q5WAE0 | MEARVEQFIENNRLFGMETNVLVAVSGGPDSMALLAIMANLREKWKLNLFGVHVNHRLRGEESNKDAELVQSFSARLGVPCNVKDVDVAAFKAEHHVGTQQAARALRYQVFQGEMERVHATVLLTAHHGDDEVETAFMKLTRGTTPLTKLGIAATRPFANGVLARPLLEETKRSIVAYCHEKAIPYRIDQSNFSDAYTRNRFRMNMAPYLVEENPHIHKHIGRFDRWQEEDNHYLMEQAKAHLDQILTKKSEKSIELEIQALCLAPFPLQRRMIHLILNYLHLNVYGVNDMRVFPDAIEQIQAFLQTSAPSAQLDLPGRVQVKRSYGTCLFTTAPFIETKAYCHLLSIPGKVDTPLGVIRADTREELLELEHTDAVSFQVSQVAFPLYIRNRKPGDKLSPSGMSGSKKVNRLFIDRKVDRAKRDAWPLLVDANDSILWVPSLQTSRILTRSANVQGELLHVTFSQHKWP | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 53274
Sequence Length: 469
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q0A7K1 | MAPTPELSPETLARHLAVLGPASGYCVAYSGGLDSTVLLHLMAALSAARELPLRAVHIHHGLQPQADAWAEHCRQQAAALGVDCLVLPVEVRRDSGEGLEAAARQARYAALASHLQSGEALLTAHHADDQAETVLLHLLRGSGPRGLAGMRAQRPLGRGRLLRPLLPWPRERLRAYGDTHALCWVEDPSNAHVAHDRNWLRHTLWPVLTQRWPDASRRVGRAAGEQAEAEALLRELAGEDLARHPPGPGLAVSVLARLSPARARNLVRHWLLMSGLRPPPRARLEQGLADLIRAGRDRQPVLTWPEGELRRYRDRIHRLPAGGPPPWPGPDREWDLRVPLVVPGVGVLRLVRADEGIAPSLIGAEGLSVGRRRRGERCQLAHDPGHRPLSKRFQEAGIPPWERDRVPILRRGEEVVAIANLGTAKRFTARPGYRLICEEHGPDGG | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 48871
Sequence Length: 445
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q5P9R1 | MSGVRIPLFPRFIPHGTVKLESAALKKLNSLELSGGYAVAVSGGVDSITLLNLVAALHKTQATSRPVVLTGNHGFRAEADHETRFVQKRAVALGLDCEILRWNRHRTSSKSQETAREIRYSLLHQWCTEHSVKFLLTAHNKSDQAETVLMHLERGSGIDGLSGMHERSVFGDITIYRPLLGFTRQEILEYATQKQLSWVEDPSNQDPKYRRTFFRNLIAESKNPGVVVDRLCRTTSHMHRALACILHYVRSSLDYCLEFSPLGFITVKSQELRSVPEEIASRLLLLSLMAMGGKDHKPRYSAFWPILTKILQGQDFTPRTLHGCKVRKEPDGNFSIVRELARIETKIGVKTIAETIQWDRRFAIKIMCTHNASAAETTSCSAKHAPNPSEETQNLYITPLGNGSLPEHLVHVNRDVACSLPVLAHGDKVLAYPWQNHNIGVSPTISVEEVLVRRGVINLICHQLYR | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 52344
Sequence Length: 466
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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O67728 | MNPESRVIRKVLALQNDEKIFSGERRVLIAFSGGVDSVVLTDVLLKLKNYFSLKEVALAHFNHMLRESAERDEEFCKEFAKERNMKIFVGKEDVRAFAKENRMSLEEAGRFLRYKFLKEILESEGFDCIATAHHLNDLLETSLLFFTRGTGLDGLIGFLPKEEVIRRPLYYVKRSEIEEYAKFKGLRWVEDETNYEVSIPRNRIRHRVIPELKRINENLEDTFLKMVKVLRAEREFLEEEAQKLYKEVKKGNCLDVKKLKEKPLALQRRVIRKFIGEKDYEKVELVRSLLEKGGEVNLGKGKVLKRKERWLCFSPEV | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 37320
Sequence Length: 317
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q5P2I9 | MLVAAAVAPRQRLCVAFSGGADSTTLLHLLARLRPRFGFDLCAAHVHHALSPNADAWLDFCARQCAALDVAFHPFREQVARDHPAGLEAAAREVRHAALSRVTCDWLVFGHHQDDQAETLLFRLLRGAGVRGAAAMAAIEPGFPGRLRPLLGVRRADIRAFAQAASLEWIEDESNADPRHARNFLRHHVFPLFGEAFPGAVPALARASGHFREADGLLGDLAALDYAACGGSPWLRDRLLMLSDERVRNLLRWRIRQMGCEAPARARLVEAVRQLRATHAPLYLPLGTAACCTYRDRLWLEPQRDGAPEQPLPWRQEPALCWGAGVVRFEPVTGAGIGRGALQRAMDVALVPRWPGLMLRQDSGRPLRSFKNLCQEAGIPAWLRPRLPVLRVDGEAAWIGEIGVAAEFRCGPGEAGLLLVWQR | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 46557
Sequence Length: 423
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
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Q2NIN4 | MENIKLACSLETNQTYIIAVSGGVDSMALLHYLVAQKIKLQVVHFNHLTNSNTWKNKELVKNYCLQNSLGFHYFELNCPQKNFQAQARLLRQQKLMQIAAKHRTPFILTAHHLDDLAETILQKISRSSTLLGYSGMQIQTSWTDFIFLKPFLYIPKAKIISYAAFYKIPFLEDYTNQKLTYQRNQIRHQVIPYLKTQTSFLQNIQKYQQTLLQAYNFIRKQTLLFLTKHTNHSCNQPNSIALAPFLNLDLVIQKDIILLLLEQKNITQSFIFIQNIIKGINNPYKPNLSWHLNSDWHLIKDYKHIKLMNPALPLPFALTKPLLCVSTCNLCLVCVCPLIETLNYNSQKVSFPLKVRLRQPKDTLKFSFGTKKLKKFLIEKKVPLTQRNNLWLVVDNLDNILFIPQLYTNLTLGNQFRIYLAFKNFFTSSNCFSQTN | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 50858
Sequence Length: 436
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
Q81VX7 | MKDTFVEKVDDFVRQHDVLKERSTIVVGVSGGPDSLALLYYLLEKRAAKQFEIVVAHVDHMFRGDESHEDLQFVQDLCKGLGVICETIRINVSQYQKQYGMNAQVAARECRYAFLERIMKKYDARYVALGHHGDDQVETILMRLVRGSTPKGYAGIAVKRPFHNGYLIRPLLGVTKEEIVNYCNELKIIPRIDPSNKKEVYTRNRLRKYVLPHLKEENPQVHEKFQKFSMQMQEDEAYLQELAFEKMNKVITKKSDKQISLSIPTFESMSMPLQRRGIQLILNYLYEYKIPSSLSSIHIDKVIEFFKRTQPSGSLDFPGDLKIVRAYEECSFGFKQEIVSPFLQDLSVPGTITLSNGDKLVTEVSEDIPSDMNETVFVAKYNDISYPIRIRSRENGDRMSIQGMNGTKKIKAIFIEAKVPREKREEWPVVCDASGNIIWLPLLKRSAFAISKETAKKDKYMIIHYKSKESSGRIMK | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 54891
Sequence Length: 476
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
B3CUJ5 | MNIEVDFCHNMECFGAFEKNPKLAIAVSGGSDSLALMLLVKHWNEKVKGEITILTIDHHLRSESTSEADYVSSICQNIKLQHVTLHWIHKGITGNIQAQARKARYQLLTNYCQEHDILHLITGHHADDIVENFFIRLLRGAGLAGLSSHNLFFVNNVRIIRPLFNITKQDLKKYLEQQNIKWINDPSNSSNKYLRTQVRDLLKSMLISFQHNFTVELLKKRIMLSQMHLTQALESVNNEIIHYVVHVVKIYSAGFAVIDRKLFKKASPEARYAILSYLLMIVGANTKPPRFSSLQRISLHDIQEYNTYKTLHGCIVEYSIEYIIIYREFGRCYPISQVVSNSVVWDYRFKVVDNRKNNHMNLTIDYLKKSDYHLIKSYVESNQRNAYFNYSKKILFTFPVIKHLEKVVAIPHIKYYSDKTIQESVSFVFEPKLISRWFHYC | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 51539
Sequence Length: 441
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
Q7UA26 | MGEQRPLALAWSPWHDRLHRRLHQHPQLLPQRQPLLLAVSGGQDSMALLVLLQELQRLHHWPLNIWHGDHGWHSGSAVIAADLRSWCQQRDLPIQVDQAPQGSTASEASARHWRYSQLQQRAEELGADVVTGHTASDRAETLLLQLARGTDLAGLGALRPVRPLFNDSPDGAQLRRPLLGFSRADTAAVCRDLQVPIWHDPSNQSPAFARNRIRAEVLPVLEQLHPGCSQRMANLAERTSQLRDTQQELSQLALQPLRTSTGLDRRRLGALQPSTRRQLLVIWLAQQGVTALNAALLEQLTDRLALSAAGGSCDLPGGWRLQWQGDNLSLQPPAAGH | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 37383
Sequence Length: 337
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
Q6MDI6 | MSCICLKNEKLNVINQVKRFIKKYCKSTQPLLLALSGGADSLSLFYCLLACRLEGILSFHVAHVDHGWREESAKEATILKNLAEQHQVPYHQLKIDLSQLAGNLEDACRKQRQKFFKEICLQNNLQAVCLGHQENDQVETVLKRILEGSHWSHFDGLKERMWHDQVQFLRPLLGIQKDEILAFLKGNQLKAFEDGTNCDERFMRARMRRTIIPDLNRSFGKKIDNSLVYIASEMSELKNFFLGRVSPLLGQIVKGPFGVYLNLANHPSIDLVEIKYLLRLISEQELFFLSRQILQRASEAIEKLEPQLSFEMGTKKIVIDRGHFFILSKKTACKNPNLQISGSSLQYYGKWMIKTNESFYHQNLQASTWLDGWRGYLKTYLPLDKYVLGQASKHAKLLRHHSTINKWWSSHHVPPFLRSFFPVIWQHNEIAHEFLTGLERQNLQEGEKCLQIELSYLT | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 53186
Sequence Length: 458
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
Q6D8C5 | MDRTEPDDELLQTIVTQTAGCGSILLAYSGGLDSSVLLHLLVTVRQRSGQTIRAAYIHHGLNPLADSWAEHCRQQCERWQVPFSSLAVTVEAQNGGIEAAARTARYQALQVHLKEGETLLTAQHLDDQSETFLLALKRGSGPAGLSAMAANSFLGHHRLVRPLLGFSRLQLEAYAQRHQLRWIEDDSNQDERFDRNFLRRQILPRLTQRWPHFPSAVARSAELCAEQEQLLDELLEESLRTLRQPDGALSIDGLVPLSPVRRFALLRRWLAQQGATMPARDQLQRLWDEVAASRRDAEPILQLNQMQIRRFRQHLYLLPLMPSLKDRVLPWQPTSCPLSLPDNLGTLLLADSGVAVRAPKNGETVSIRFSTSGTVHIVGRAHGRQIKKLWQELGVPPWWRDRTPLLFYNEQLIAAVGRFVTREGQVREHQPLWHIVWERN | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 50029
Sequence Length: 440
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
C0QU23 | MVEKKFLEAVKKYSLISEGDRILVAFSGGIDSTVLTYLLIKFRDHLKISDIYLAHLNHSLRKESDEDQRFCEDFAKKYGLEIFTKKVDIKSLAEKEKKSIEQKAREERYSFFRKVMEERSINRLATGHHLSDLVETMIMWFIQGNRKGIKGFRPKERDIIRPLYLINKDQIENYAREKGIEYRIDITNFETDFLRNRIRHNIIPHIKGINPSLEGSLLTLSYFLSLDDQYLEEESEKISQKFLNGKIELEELLVYDKALVYRAIQNWIYRKTGVYPSYRQIMDIMEIIEKKEGTKSIRLSPEYNLIRRYSTLYIEKVKEKTEPYQYRIKPGEKIFVKEANLYIKSYIETDYTLDKLKDERKKVCFQIESMEDAEFVVRNRRKGDRFIPFGRKKEKKLKDVMIDLKIPSDMRENIPLVVYGNKILWIAGYKRSAYFPVTEKGKKLICFELEEV | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 53867
Sequence Length: 452
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
A9BJK2 | MILQDFEKKIFKFIRDYKIFNKYDKILLGVSGGKDSMSLLHVMSKLSKTMGFEISVAHLNHCMREEADNDEAFVRQACWKLKIPFFSKKVDVFTYSKKNKVGVEVAGRKLRYEFFYETLRRLSYNKIATAHHMDDLFETMIYRILRGTGIYGLGGLIPIEEEITKPMLCVDLEEIKNYVTINNIEYVEDKYNYSLDYARNKIRYEITPLFKKINPRYKESFFRLAKIIWSYREEVKRKFEERSEISKDSLKLRLENDFFDGEIIRIAFLKFGKYPPNMEETEKIIKMRKGGVRKINGLSITKKSDSLLVKI | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 36881
Sequence Length: 311
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
Q7N8N0 | MANIDERLFVTLAKQLGEYKKILVGFSGGLDSSVLLHLLVNWRNQHNQKIQLRAIHIHHGLNLKADQWIEHCQLICDDWQVEFHSARVTIDARQKGIEAAARDARYQVFKSELQKDEVLVTAQHLDDQAETFLLALKRGSGPAGLASMPSIAVFADTLLLRPLLDYSRNELEKYASKHRLNWIEDDSNQDDRYDRNFLRLHIMPLLNQRWSHFPKAAARSASLCGEQEQLLDELLNESLKELITQDGALGIVSLAVCSEAKRNALLRRWFGYHGMKMPSREQLNRLWYEVALARTDAEPRLQFGKYDVRRYKQKLWLVPQWQSLRETILEWDICNTLVLPDRLGELNIADRGIQVRVPADNERVTIRFGVQGMISIVGRQHSRHSKKLWQELGVAPWLRERIPLLYYNEQLIAALGVFVTKESEAAEGRKMLTMNWHKTLLK | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 51163
Sequence Length: 442
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
A1VRB1 | MAAPVASLNPALAGIDSLFSAFPSSSSLPLGVAYSGGADSTALLLAAAERWPGQVQAFHIHHGLQAAADDFVRVCESVCAKAGLPLHIVQVDARHASGESPEDAARRARYAALATAATARGMQGVLLGQHADDQVETMLLALSRGAGLPGLSAMPASFGRGGMVFYRPLLHIPSAVLREWLVEQPIEFVDDPTNTDERYTRNRIRARLLPALAQAFPQFHATFARSARHAAQAQAVLVEVAAQDLAVVGNPPAIKALQALSPPRQANVLRHWLLLQYATPSAAQLEQLLHQVAACTTRGHRIHLKVASGHVTRLGGSLCYSDAAARAC | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 34690
Sequence Length: 328
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
B2RMB4 | MKISLTNRVRTTIRERKLFREGNRLVLVALSGGADSVALLCVLRELGYETVAAHCNFHLRGVESDEDAAFVEGLCRDLDVPLHRIDFDTVRYARERSISIEMAARELRYEWFGLLRKELAIEYVAVAHHADDNAETMVLNLCRGTGISGLCGMPYKRNDGIVRPLLDATRDEIEAYLLDQKITYRTDSSNEDTRFRRNLVRHRIMPLLKELNPSLQEALLRTRENLEGVAAFFSKATEDFHNTLRATASISIREVKETPAPFTLLYDLLHPYGFNRDQIREVVTSLDNPPGASFFSSSHRLLRERDRLTVLPLSPKMEVPELFGLKIGDSFLDLPDGKQLSWQRGTPADLDLEGLRLPNTKLLLPLAFVESLQEELGVRRPQRGDHIHPYGMKGCKTVSRFFIDRHVPRRRREEAWLLCQGTEVVWIMGYAADRRFAIDELSDTEEYLLFSFEL | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 52089
Sequence Length: 454
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
P51383 | MFLDSFLHKKFFSTIEKKSLLPSKSSLLVAFSGGQDSLTLVKLLYDLNPFYRWRITLIHFDHRWRWDSMLASKQVFSFARYYNFPLYYFECPDYLNTEEASRKWRYTTLIDLAVKNNFTKILLAHTATDSSETLLSNLFRGTSLDGLASIGWSCQLAQSVYIVRPLLNFYRFETSWFCRKYYLPIWVDRSNYDYIMFRNRLRQELVPYIKSYFQPNLEERCYSLSSLVKYDTDFLEQEALRIYFILIHQDLIAINHTALRLLHLSVQSRIFKIFFIANLNFNPNSRQIEDVIIFIKQNILSQINMNNYILVMDDIWFYVGVKIIKFS | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 39154
Sequence Length: 327
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Plastid
EC: 6.3.4.19
|
Q7V9L9 | MTNSTKVEKPWTKWHERLHKSLKSKSNLLPYGSSLLISVSGGQDSMALLKLILDLQRIYEWKVHVWHGDHGWHNQSRQIAEELEEWCKCQKLSFFCNRTNKQKVSTEEDARNWRYKSLIQQAKTLSKESPSLPCERVLTGHTANDRTETFIMNLARGAHLKGLSSLREDRTLETKIQLIRPILRFSRQETIQICDEMDLPIWIDPSNSNIAYSRNKIRAEIIPVLESLHPQSTIRISNLAERLTSLQKDQHQLAHLALGALLTSTGLSRSKMTKLSKTVRAIILAQWLEDNKAPLLSSKQLEELSQKIGKNKGPGNMDISNHLKIRWNKNSIELIN | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 38635
Sequence Length: 336
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
B4F252 | MELKNCPLINEIKRQIGSHTHILVGFSGGVDSTVLLHGLVCLRDKYQLPLELTAIYVHHGLNSKADDWLTHCEHFCHNWQVSFISERVQVNGKEGGIEQGAREARYQAYRQYLQPNQVLVTAQHQDDQAETFLLALKRGSGPAGLSSMPAKMPFEQGYLLRPLLNITREQIEAYAHEHGLLWIEDDSNQDDRYDRNFLRLHVMPLLTQRWPHFSQAVTRSAALCGEQEALLDELLDVELQQLIDEHQSLDINLLSRCSEIKRNALLRRWFAKCNKSMPSRSQLSRLWQEVALAKADAEPRLRFFQDEVRRYQQRLYLVPVMEELTDRVIEWSLSQPLILPNQLGILAVSRDSGKTICRAPLADEKVTVRFGLTASSLRIVGRDLARSSKKIWQELNIAPWQRTRIPLIYYNDTLIAAVNTFVTLEGNATTEQSITIEWQAS | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 50613
Sequence Length: 441
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
Q7V987 | MASSSSTQLPWSAWHARLHHKLLANPDLLPAKASLLIAVSGGQDSMALLGLLIDLQRKHGWSLEVWHGDHNWHKQSATIATELKNWCESHNLSFCSDQAKPGQTNNEATARHWRYEQLTLHAERLSSNNPNHPCRYVLTGHTSSDRAETLLLNLARGTDLAGLSSMRQCRPISKDHPHKNVQLIRPLLGFSREDTALICSELGLPIWLDPANSNPDFSRNRVRQEVLPVLESLHPGCSLRMAALAERLNHHHADQQAIAMLALNNLSKQNGLCRKDLAQLPITARTTLLAYWLKRSGAPSLPAVQLEQISQSIAPGKPPGSLHLAQGWKVQWQRNSVQLEHHD | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 38259
Sequence Length: 343
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
Q7UZL1 | MSDKNSSQKNWTSWHHLLHKEILGNKTLIPDGANLLIAVSGGQDSMALLNLINDMKTQHNWFVNVWHGDHQWHKKSAKYALELKSYCNKKNISFFFDQANKNNISSEEKARDWRYKKLSERANQLLIENQKEIDIYLLTGHTNTDNAETFLLNLARGSNYAGLSNINKKRLLKHHIFLIRPLLIFSREDTKKFCQLQNIPIWEDPTNCDLTIKRNIVRKEIIPILETMYPGCSKRINSFAEKMSNYKNEQNDLSKLASLYCEDAIGVKRELLNSLCIEARCTILNTFLKKDCTKQLSSKNLTHLASSILVKDRGKIDLPDGFEIVWNKDYINLEKN | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 38969
Sequence Length: 336
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
Q46ID9 | MRLHKRLKQNKSLLPSNSTILLAISGGQDSMALLKLIIDLKRLHQWQVEVWHGNHQWHAKSEETEDELKLWCLKNQISFHSNKADKKEVANEEKARDWRYKNLIMKAKFLSSKNIHFPCTRILTGHTATDRAETVIMNLARGTDLTGLTTLKEQRTIENNIDLTRPLLIFNRNETLEICKDFNLPIWIDPSNENINLTRNKIRKEILPILNSIYKGADSRIASVANRLESYNEDQKLFAKIAIQFCQGEKINSLSRIKLFGLTNSIRQIILSNWLKTMGVKRVTALQIEEINTKVSQRKPPGSIHLHGDFLIRWNKEAIYISNKTN | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
Sequence Mass (Da): 37752
Sequence Length: 326
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Subcellular Location: Cytoplasm
EC: 6.3.4.19
|
Q6FPU1 | MDGTGISDGSSVTGDAAAGFPAGATQAPGSKQGMDLYFDNALQYMGEHPVLAGVGGFLALYVGAGVYKGVQTRLNGGKAATQFLKGGFDPKMNAKEALQILNLKENNLTTKKLKEVHRKIMLANHPDKGGSPYLATKINEAKDFLEKKGIVRK | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16156
Sequence Length: 153
Domain: The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Subcellular Location: Mitochondrion inner membrane
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Q6PBT7 | MASTMVAVGLTLAAAGFTGRYAVRAMKHMEPQVKQALEASKSAFGSGYYRGGFDPKMNRREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAKINEAKDLLDGQAKK | Function: Mitochondrial co-chaperone which forms a complex with prohibitins to regulate cardiolipin remodeling (By similarity). May be a component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12433
Sequence Length: 115
Subcellular Location: Mitochondrion inner membrane
|
Q6BH37 | MAPFNMDIPTLAIPGDRNQSQAIELSQQAQQPQQPQQSQQAYTGHLQRKQADEGSAEYYFDKGCEWMGNHPWMTGMGVLGVAYFASGFVKSKQPGINGKAFVKGPFGQKMTPKEALQILNLKETNLSQAKLKEQHRKLMMANHPDKGGSSYLATKVNEAKDILEKRGGLKKK | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19094
Sequence Length: 172
Domain: The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Subcellular Location: Mitochondrion inner membrane
|
Q54QN1 | MATPIIVGATIAGIAYSSRFLIRVIQRAKSKQLFEMVSTPGFTVETIEDGFENKMTPAEAANILGLKEESTKEEIKIRHKLLMIKNHPDKGGSSYLATKINEARNVLSSKNSN | Function: Mitochondrial co-chaperone which forms a complex with prohibitins to regulate cardiolipin remodeling (By similarity). May be a component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12436
Sequence Length: 113
Subcellular Location: Mitochondrion inner membrane
|
Q9VTJ8 | MASSVILAGLSVAAVGFAGKHLMRRMPQMTTKFNEALKNLPKYDAESMAASKYYKGGFDPKMNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAKINEAKDFLDKAK | Function: Probable component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12868
Sequence Length: 118
Subcellular Location: Mitochondrion inner membrane
|
Q5B4H1 | MASALTLGLGVATAAFLGRAGLVAYRRSKGGVNALGKAFYKGGFEPRMNRREAALILELPERTLNKEKVRKKHRQLMLLNHPDRGGSPYLATKINEAKEFLDKHT | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1/sscA) (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11605
Sequence Length: 105
Domain: The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Subcellular Location: Mitochondrion inner membrane
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Q4I7T5 | MASVMAWGAGAAVAAFLGRAGLVAWRRSRGGVGAMGKAFYKGGFEAKMTKKEATLILSLNERAITKDKVRKAHRTLMLLNHPDRGGSPYLATKVNEAKEFLDKNG | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11293
Sequence Length: 105
Domain: The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Subcellular Location: Mitochondrion inner membrane
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Q96DA6 | MASTVVAVGLTIAAAGFAGRYVLQAMKHMEPQVKQVFQSLPKSAFSGGYYRGGFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLLEGQAKK | Function: Mitochondrial co-chaperone which forms a complex with prohibitins to regulate cardiolipin remodeling (By similarity). May be a component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12499
Sequence Length: 116
Subcellular Location: Mitochondrion inner membrane
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Q9CQV7 | MASTVVAVGLTIAAAGFAGRYVLQAMKHVEPQVKQVFQSLPKSAFGGGYYRGGFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLLEGQAKK | Function: Mitochondrial co-chaperone which forms a complex with prohibitins to regulate cardiolipin remodeling . May be a component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. May act as a co-chaperone that stimulate the ATP-dependent activity (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12437
Sequence Length: 116
Subcellular Location: Mitochondrion inner membrane
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Q7RX75 | MSSAVAIGAGVAVAAFLGRAGLVAWRRSRGGVGALGKAFYKGGFEPRMNKKEASLILSLNERTITKDKIRKAHRTLMLLNHPDRGGSPYLATKVNEAKEFLEKSV | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (hsp70-5) (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 11312
Sequence Length: 105
Domain: The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Subcellular Location: Mitochondrion inner membrane
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Q9UT37 | MSSAILLGVGIAATAAAGKIGVDAFRKYRNLNGGVKAFLKGGFESKMSRAEAIQILSLNNRTLTRQKIKEAHRRLMLANHPDRGGSPYVASKVNEAKSLLDADRSIRKFSSWALPVSKQRSMPSVLEAVKWLEYSSIPKA | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (ssc1) (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15271
Sequence Length: 140
Domain: The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Subcellular Location: Mitochondrion inner membrane
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Q6CEU0 | MSTTPVQPLQSEPLMDSETGVAPQIEAPQVPEGPKKGIDEQIFDYFAEHPVQATAATLVGLYALGAVFKRPAAGARGQFFKGGFENKMGPSEALQILSLRDAGLTMNKLKGQHRKIMLLNHPDRGGSPYVATKINEAKSVLEKRGGLK | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1) (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15927
Sequence Length: 148
Domain: The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Subcellular Location: Mitochondrion inner membrane
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Q07914 | MSSQSNTGNSIEAPQLPIPGQTNGSANVTVDGAGVNVGIQNGSQGQKTGMDLYFDQALNYMGEHPVITGFGAFLTLYFTAGAYKSISKGLNGGKSTTAFLKGGFDPKMNSKEALQILNLTENTLTKKKLKEVHRKIMLANHPDKGGSPFLATKINEAKDFLEKRGISK | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17910
Sequence Length: 168
Domain: The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.
Subcellular Location: Mitochondrion inner membrane
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O62250 | MPWRTALKVALAAGEAVAKALTRAVRDEIKQTQQAAARHAASTGQSASETRENANSNAKLGISLEESLQILNVKTPLNREEVEKHYEHLFNINDKSKGGTLYLQSKVFRAKERIDEEFGRIELKEEKKKEENAKTE | Function: Regulates ATP-dependent protein translocation into the mitochondrial matrix.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 15276
Sequence Length: 136
Domain: The J-like region, although related to the J domain does not have co-chaperone activity.
Subcellular Location: Mitochondrion inner membrane
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Q59ZW9 | MAHRLLVNVIFTGASVFGRAFTEAYRQAAKASAAGAAGRPAKASSAGGIPVEEAMKILDLEKSELSLDKVEEKYEYLFNVNSKEQGNSFYLQSKVYYAMDTLKKELEYLEKLQNEKGAASN | Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13306
Sequence Length: 121
Domain: The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function (By similarity).
Subcellular Location: Mitochondrion inner membrane
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P20614 | MAPLAALASSMLLLLWLVAPSRACTCVPPHPQTAFCNSDLVIRAKFVGAPEVNHTTLYQRYEIKTTKMFKGFDALGHATDIRFVYTPAMESVCGYSHKSQNRSEEFLIAGQLRNGLLHITTCSFVVPWNSLSFSQRSGFTKTYAAGCDMCTVFACASIPCHLESDTHCLWTDQLLLGSDKGFQSRHLACLPQEPGLCAWQSLRPRKD | Function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling (By similarity).
PTM: The activity of TIMP1 is dependent on the presence of disulfide bonds.
Sequence Mass (Da): 22937
Sequence Length: 207
Subcellular Location: Secreted
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P50122 | MALFAPTVSGILLLLWLTAPSRACTCVPPHPQTAFCNSEVVIRAKFVGTAEVNETALYQRYEIKMTKMFKGFSALRDAPDIRFIYTPAMESVCGYFHRSQNRSEEFLIAGQLSNGHLHITTCSFVAPWNSMSSAQRRGFTKTYAAGCEECTVFPCSSIPCKLQSDTHCLWTDQLLTGSDKGFQSRHLACLPREPGMCTWQSLRPRGA | Function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling (By similarity).
PTM: The activity of TIMP1 is dependent on the presence of disulfide bonds.
Sequence Mass (Da): 23058
Sequence Length: 207
Subcellular Location: Secreted
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Q60453 | RACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP | Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.
PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds.
Sequence Mass (Da): 21941
Sequence Length: 196
Subcellular Location: Secreted
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O77717 | KAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKADGNGKMHITLCDFIVPWDTLST | Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them.
PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds.
Sequence Mass (Da): 9998
Sequence Length: 91
Subcellular Location: Secreted
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P16035 | MGAAARTLRLALGLLLLATLLRPADACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP | Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.
PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds.
Sequence Mass (Da): 24399
Sequence Length: 220
Subcellular Location: Secreted
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P30121 | MGAAARSLRLALGLLLLATLLRPADACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSITQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP | Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.
PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds.
Sequence Mass (Da): 24356
Sequence Length: 220
Subcellular Location: Secreted
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P0DTS9 | MSVLETKLKSQMSKSAKIARNMNKLPDEIDRLRKRIERINKKRKPTSSNIRDLEKSNKQLVTKQQKLADLQVEYTKIEKKINETKINLQKEQSRNQKKLSSMLDKNTKGNEEIMEKLLTNSDQINEISNQIKKAVNQKEIIEYDVFLSHSSLDKEDYVSKISEKLIEKGLKVFEDVKVFEIGKSQTETMNMGILNSRFVVVFLSPNFIESGWSRYEFLSFLNREINEEHVIILPIWHKVSVEDVRAYNPYLVDKYALNTSDFSIEEIVEKIYQVIVNSKN | Function: Virulence factor that suppresses host Toll-like receptor 2 (TLR2)-mediated NF-kappa-B signaling upon infection . NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide . Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules . Able to reduce NAD(+) levels in host cells .
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Sequence Mass (Da): 32811
Sequence Length: 280
Domain: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Subcellular Location: Secreted
EC: 3.2.2.6
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B7UM99 | MPIGNLGNNVNGNHLIPPAPPLPSQTDGAARGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAATSETCLLGGFEVLHDKGPLDILNTQIGPSAFRVEVQADGTHAAIGEKNGLEVSVTLSPQEWSSLQSIDTEGKNRFVFTGGRGGSGHPMVTVASDIAEARTKILAKLDPDNHGGRQPKDVDTRSVGVGSASGIDDGVVSETHTSTTNSSVRSDPKFWVSVGAIAAGLAGLAATGIAQALALTPEPDDPTTTDPDQAANAAESATKDQLTQEAFKNPENQKVNIDANGNAIPSGELKDDIVEQIAQQAKEAGEVARQQAVESNAQAQQRYEDQHARRQEELQLSSGIGYGLSSALIVAGGIGAGVTTALHRRNQPAEQTTTTTTHTVVQQQTGGNTPAQGGTDATRAEDASLNRRDSQGSVASTHWSDSSSEVVNPYAEVGGARNSLSAHQPEEHIYDEVAADPGYSVIQNFSGSGPVTGRLIGTPGQGIQSTYALLANSGGLRLGMGGLTSGGESAVSSVNAAPTPGPVRFV | Function: Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion. In strain E2348/69, acts mainly via the host adaptor proteins NCK1 and NCK2. Once clustered and phosphorylated at Tyr-474, Tir binds to NCK proteins, which in turn bind and activate host WASL/N-WASP, leading to actin polymerization. Can also trigger an inefficient, NCK-independent pedestal formation. This pathway involves phosphorylation of Tyr-454 and probably a putative host adaptor. Acts also via direct binding to the host cytoskeletal protein alpha-actinin in a NCK- and phosphotyrosine-independent manner. This interaction may stabilize the pedestal, but is not essential for its formation.
PTM: Phosphorylated on Tyr-474 by host kinases. Tyr-454 can also be phosphorylated, although at lower efficiency. Phosphorylation is stimulated by clustering of Tir by intimin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56510
Sequence Length: 550
Domain: The intracellular N-terminal region interacts with host alpha-actinin and is not required for pedestal formation. The central extracellular region (amino acids 277-332) is involved in bacterial intimin binding. The intracellular C-terminal region binds to host NCK.
Subcellular Location: Secreted
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A5A627 | MNLVDIAILILKLIVAALQLLDAVLKYLK | Function: Toxic component of a type I toxin-antitoxin (TA) system (Probable). Overexpression causes cessation of growth, induces stress-response, a number of membrane protein genes, and leads to cell death . Inhibits ATP synthesis, ATP levels drop drastically quickly after induction . Part of the programmed response to DNA damage; damage leads to increased accumulation of the protein which slows or stops bacterial growth, probably allowing DNA repair before cells continue to grow .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3222
Sequence Length: 29
Subcellular Location: Cell inner membrane
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Q07352 | MTTTLVSATIFDLSEVLCKGNKMLNYSAPSAGGCLLDRKAVGTPAGGGFPRRHSVTLPSSKFHQNQLLSSLKGEPAPALSSRDSRFRDRSFSEGGERLLPTQKQPGGGQVNSSRYKTELCRPFEENGACKYGDKCQFAHGIHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRALAGARDLSADRPRLQHSFSFAGFPSAAATAAATGLLDSPTSITPPPILSADDLLGSPTLPDGTNNPFAFSSQELASLFAPSMGLPGGGSPTTFLFRPMSESPHMFDSPPSPQDSLSDQEGYLSSSSSSHSGSDSPTLDNSRRLPIFSRLSISDD | Function: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis . Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery . Functions by recruiting the CCR4-NOT deadenylase complex and components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes . Induces also the degradation of ARE-containing mRNAs even in absence of poly(A) tail (By similarity). Binds to 3'-UTR ARE of numerous mRNAs . Positively regulates early adipogenesis by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) (By similarity). Promotes ARE-mediated mRNA decay of mineralocorticoid receptor NR3C2 mRNA in response to hypertonic stress . Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA . Positively regulates monocyte/macrophage cell differentiation by promoting ARE-mediated mRNA decay of the cyclin-dependent kinase CDK6 mRNA . Promotes degradation of ARE-containing pluripotency-associated mRNAs in embryonic stem cells (ESCs), such as NANOG, through a fibroblast growth factor (FGF)-induced MAPK-dependent signaling pathway, and hence attenuates ESC self-renewal and positively regulates mesendoderm differentiation (By similarity). May play a role in mediating pro-apoptotic effects in malignant B-cells by promoting ARE-mediated mRNA decay of BCL2 mRNA . In association with ZFP36L2 maintains quiescence on developing B lymphocytes by promoting ARE-mediated decay of several mRNAs encoding cell cycle regulators that help B cells progress through the cell cycle, and hence ensuring accurate variable-diversity-joining (VDJ) recombination and functional immune cell formation (By similarity). Together with ZFP36L2 is also necessary for thymocyte development and prevention of T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1 mRNA (By similarity). Participates in the delivery of target ARE-mRNAs to processing bodies (PBs) . In addition to its cytosolic mRNA-decay function, plays a role in the regulation of nuclear mRNA 3'-end processing; modulates mRNA 3'-end maturation efficiency of the DLL4 mRNA through binding with an ARE embedded in a weak noncanonical polyadenylation (poly(A)) signal in endothelial cells . Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion . Plays a role in vasculogenesis and endocardial development (By similarity). Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis . Plays a role in myoblast cell differentiation (By similarity).
PTM: Phosphorylated . Phosphorylated by RPS6KA1 at Ser-334 upon phorbol 12-myristate 13-acetate (PMA) treatment; this phosphorylation results in dissociation of the CCR4-NOT deadenylase complex and induces p38 MAPK-mediated stabilization of the low-density lipoprotein receptor LDLR mRNA . Phosphorylated by protein kinase AKT1 at Ser-92 and Ser-203 in response to insulin; these phosphorylations stabilize ZFP36L1, increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization . AKT1-mediated phosphorylation at Ser-92 does not impair ARE-containing RNA-binding . Phosphorylated at Ser-54, Ser-92 and Ser-203 by MAPKAPK2; these phosphorylations increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization in a protein kinase AKT1-independent manner . MAPKAPK2-mediated phosphorylations at Ser-54, Ser-92 and Ser-203 do not impair ARE-containing RNA-binding . Phosphorylations increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization during early adipogenesis in a p38 MAPK- and AKT-dependent manner (By similarity).
Sequence Mass (Da): 36314
Sequence Length: 338
Subcellular Location: Nucleus
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P23950 | MTTTLVSATIFDLSEVLCKGNKMLNYSTPSAGGCLLDRKAVGTPAGGGFPRRHSVTLPSSKFHQNQLLSSLKGEPAPSLSSRDSRFRDRSFSEGGERLLPTQKQPGSGQVNSSRYKTELCRPFEENGACKYGDKCQFAHGIHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRALAGGRDLSADRPRLQHSFSFAGFPSAAATAAATGLLDSPTSITPPPILSADDLLGSPTLPDGTNNPFAFSSQELASLFAPSMGLPGGGSPTTFLFRPMSESPHMFDSPPSPQDSLSDHEGYLSSSSSSHSGSDSPTLDNSRRLPIFSRLSISDD | Function: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis . Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (By similarity). Functions by recruiting the CCR4-NOT deadenylating complex and components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (By similarity). Induces also the degradation of ARE-containing mRNAs even in absence of poly(A) tail (By similarity). Binds to 3'-UTR ARE of numerous mRNAs . Positively regulates early adipogenesis by promoting ARE-mediated mRNA decay of immediate early genes (IEGs) . Promotes ARE-mediated mRNA decay of mineralocorticoid receptor NR3C2 mRNA in response to hypertonic stress . Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA (By similarity). Positively regulates monocyte/macrophage cell differentiation by promoting ARE-mediated mRNA decay of the cyclin-dependent kinase CDK6 mRNA (By similarity). Promotes degradation of ARE-containing pluripotency-associated mRNAs in embryonic stem cells (ESCs), such as NANOG, through a fibroblast growth factor (FGF)-induced MAPK-dependent signaling pathway, and hence attenuates ESC self-renewal and positively regulates mesendoderm differentiation . May play a role in mediating pro-apoptotic effects in malignant B-cells by promoting ARE-mediated mRNA decay of BCL2 mRNA (By similarity). In association with ZFP36L2 maintains quiescence on developing B lymphocytes by promoting ARE-mediated decay of several mRNAs encoding cell cycle regulators that help B cells progress through the cell cycle, and hence ensuring accurate variable-diversity-joining (VDJ) recombination and functional immune cell formation . Together with ZFP36L2 is also necessary for thymocyte development and prevention of T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1 mRNA . Involved in the delivery of target ARE-mRNAs to processing bodies (PBs) (By similarity). In addition to its cytosolic mRNA-decay function, plays a role in the regulation of nuclear mRNA 3'-end processing; modulates mRNA 3'-end maturation efficiency of the DLL4 mRNA through binding with an ARE embedded in a weak noncanonical polyadenylation (poly(A)) signal in endothelial cells (By similarity). Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion (By similarity). Plays a role in vasculogenesis and endocardial development . Involved in the regulation of keratinocyte proliferation, differentiation and apoptosis (By similarity). Plays a role in myoblast cell differentiation .
PTM: Phosphorylated . Phosphorylated by RPS6KA1 at Ser-334 upon phorbol 12-myristate 13-acetate (PMA) treatment; this phosphorylation results in dissociation of the CCR4-NOT deadenylase complex and induces p38 MAPK-mediated stabilization of the low-density lipoprotein receptor LDLR mRNA. Phosphorylated by protein kinase AKT1 at Ser-92 and Ser-203 in response to insulin; these phosphorylations stabilize ZFP36L1, increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization. AKT1-mediated phosphorylation at Ser-92 does not impair ARE-containing RNA-binding. Phosphorylated at Ser-54, Ser-92 and Ser-203 by MAPKAPK2; these phosphorylations increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization in a protein kinase AKT1-independent manner. MAPKAPK2-mediated phosphorylations at Ser-54, Ser-92 and Ser-203 do not impair ARE-containing RNA-binding (By similarity). Phosphorylations increase the association with 14-3-3 proteins and mediate ARE-containing mRNA stabilization during early adipogenesis in a p38 MAPK- and AKT-dependent manner .
Sequence Mass (Da): 36385
Sequence Length: 338
Subcellular Location: Nucleus
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Q805B4 | MSTTLLSAFYDIDLLYKNEKALNNLALSTMLDKKAVGSPVSSTNSNLFPGFLRRHSATNLQALSGSTNLAKFCPNNNNNPLKDPAVSSTALLNRENKFRDRSFSENGERSQHLLHLQQQQQQQKAGAQVNSTRYKTELCRPFEENGACKYGEKCQFAHGFHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRQAPGAGERPKLHHSLSFSGFPNHSLDSPLLESPTSRTPPPQSSGSLYCQELLQLNNNNPCANNAFTFSGQELGLIAPLAIHTQNQSYCRQPCSSPPLSFQPLRRVSESPVFDAPPSPPDSLSDRDSYLSGSLSSGSLSGSDSPTLDSNRRLPIFSRLSISDD | Function: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis . Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (By similarity). Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (By similarity). Binds to 3'-UTR ARE of numerous mRNAs . Induces also the degradation of ARE-containing mRNAs even in absence of poly(A) tail (By similarity). Required for tubulogenesis during pronephros development .
PTM: Phosphorylated (By similarity).
Sequence Mass (Da): 40329
Sequence Length: 364
Subcellular Location: Nucleus
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P47974 | MSTTLLSAFYDVDFLCKTEKSLANLNLNNMLDKKAVGTPVAAAPSSGFAPGFLRRHSASNLHALAHPAPSPGSCSPKFPGAANGSSCGSAAAGGPTSYGTLKEPSGGGGTALLNKENKFRDRSFSENGDRSQHLLHLQQQQKGGGGSQINSTRYKTELCRPFEESGTCKYGEKCQFAHGFHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNADERRPAPSGGASGDLRAFGTRDALHLGFPREPRPKLHHSLSFSGFPSGHHQPPGGLESPLLLDSPTSRTPPPPSCSSASSCSSSASSCSSASAASTPSGAPTCCASAAAAAAAALLYGTGGAEDLLAPGAPCAACSSASCANNAFAFGPELSSLITPLAIQTHNFAAVAAAAYYRSQQQQQQQGLAPPAQPPAPPSATLPAGAAAPPSPPFSFQLPRRLSDSPVFDAPPSPPDSLSDRDSYLSGSLSSGSLSGSESPSLDPGRRLPIFSRLSISDD | Function: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis . Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery . Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes . Binds to 3'-UTR ARE of numerous mRNAs . Promotes ARE-containing mRNA decay of the low-density lipoprotein (LDL) receptor (LDLR) mRNA in response to phorbol 12-myristate 13-acetate (PMA) treatment in a p38 MAPK-dependent manner . Positively regulates early adipogenesis by promoting ARE-mediated mRNA decay of immediate early genes (IEGs). Plays a role in mature peripheral neuron integrity by promoting ARE-containing mRNA decay of the transcriptional repressor REST mRNA. Plays a role in ovulation and oocyte meiotic maturation by promoting ARE-mediated mRNA decay of the luteinizing hormone receptor LHCGR mRNA. Acts as a negative regulator of erythroid cell differentiation: promotes glucocorticoid-induced self-renewal of erythroid cells by binding mRNAs that are induced or highly expressed during terminal erythroid differentiation and promotes their degradation, preventing erythroid cell differentiation. In association with ZFP36L1 maintains quiescence on developing B lymphocytes by promoting ARE-mediated decay of several mRNAs encoding cell cycle regulators that help B cells progress through the cell cycle, and hence ensuring accurate variable-diversity-joining (VDJ) recombination process and functional immune cell formation. Together with ZFP36L1 is also necessary for thymocyte development and prevention of T-cell acute lymphoblastic leukemia (T-ALL) transformation by promoting ARE-mediated mRNA decay of the oncogenic transcription factor NOTCH1 mRNA.
PTM: Phosphorylated by RPS6KA1 at Ser-490 and Ser-492 upon phorbol 12-myristate 13-acetate (PMA) treatment; this phosphorylation results in dissociation of the CCR4-NOT-deadenylase complex and induces p38 MAPK-mediated stabilization of the low-density lipoprotein (LDL) receptor (LDLR) mRNA . Phosphorylation occurs during early preadipocyte differentiation (By similarity).
Sequence Mass (Da): 51063
Sequence Length: 494
Subcellular Location: Nucleus
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Q9ZD67 | MLPPKIFFEKVKEIIWPIERKELKLFIPMALMMLCILFNFGALRSIKDSLVVPSMGAEIISFLKLWLVLPSCVIFTILYVKLSNKLNFEYIFYSIVGTFLLFFLLFAYIIYPNQDIYHPNDAMINNLIASYPNLKWFIKIGSKWSYALMYIFSELWSAVVINLMFWQFANHIFDTAKAKRFYPVLGMVGNIGLIIAGSVLVFFSSGQYIIDSELLTDSYNSSSNNSIMLQPIISIIVTAGIIAMFLFRIINKFILTNSINVLDVKKVAAKTKTKLALIESIKLIIHSKYIGRIALLIICYGLLINIVEGPWKAKIKELHPNTVDYVNFMGMFNIWMGISCVTFMIIGSNILRRLGWLISALLTPIMLSITGFMFFIFIIFIEEIGTCFGDFNLLYVAIIVGAIQNILSKSSKYSLFDSTKEMAYIPLSLELRTKGKAAVEVIGTKFGKSLGAFIQSLIFIIIPTATFDSIIIYLLVIFIVMMNLWIWNIIKLNKEYIKLCQ | Function: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57182
Sequence Length: 501
Subcellular Location: Cell membrane
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F1NZP5 | MGPGWRAPSAALVGGSVALFGALRRAALALPRPAAVRSRPGRVWRWRNLLVSFAHSVLAGLWALFSLWQSPELLSDIQDGYSVSGHLLVCFSSGYFIHDSLDIIFNQQSRSSWEYLVHHAMAISAFVSLIITGRFLVAAMLLLLVEVSNIFLTIRMLLKMSNVPSPALYEANKYVNLVMYFAFRLAPQVYLTWYFVRYVEVQGQGAFLMANLLLLDAMILMYFSRLLRSDFFPSLRKGSVGRDVDGEKFLID | Function: Regulates the composition and fluidity of the plasma membrane (By similarity). Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity (By similarity). Does not appear to have any effect on LCPUFA synthesis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28348
Sequence Length: 252
Subcellular Location: Cell membrane
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Q96CP7 | MPRLLHPALPLLLGATLTFRALRRALCRLPLPVHVRADPLRTWRWHNLLVSFAHSIVSGIWALLCVWQTPDMLVEIETAWSLSGYLLVCFSAGYFIHDTVDIVASGQTRASWEYLVHHVMAMGAFFSGIFWSSFVGGGVLTLLVEVSNIFLTIRMMMKISNAQDHLLYRVNKYVNLVMYFLFRLAPQAYLTHFFLRYVNQRTLGTFLLGILLMLDVMIIIYFSRLLRSDFCPEHVPKKQHKDKFLTE | Function: Regulates the composition and fluidity of the plasma membrane . Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity . Does not appear to have any effect on LCPUFA synthesis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28548
Sequence Length: 247
Subcellular Location: Cell membrane
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A8WGS4 | MELNSVILTTGSSVGFFKLVNYGLGKLPIPETARRNAWKWNNISTSFVHSLITGVWSVLCFCMHPQMAEDLIETHSVFSHALVSVSIGYFIYDFLDMVINQKIIHSWELLFHHVVVITCFGISVLTCRYVGFAVVALLVEINSVFLHLRQVLRMANLAKSTFYRVNSMINLGTYVVFRINTLAWMTRWLVLNRDLIPLFSYTIGSVGLAIMTAMNIVLFYRLMRSDFMKASREKELRKEKEKEKDM | Function: Regulates the composition and fluidity of the plasma membrane (By similarity). Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity (By similarity). Does not appear to have any effect on LCPUFA synthesis (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28334
Sequence Length: 246
Subcellular Location: Cell membrane
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A6NGC4 | MAPTGLLVAGASFLAFRGLHWGLRRLPTPESAARDRWQWWNLCVSLAHSLLSGTGALLGLSLYPQMAADPIHGHPRWALVLVAVSVGYFLADGADLLWNQTLGKTWDLLCHHLVVVSCLSTAVLSGHYVGFSMVSLLLELNSACLHLRKLLLLSRQAPSLAFSVTSWASLATLALFRLVPLGWMSLWLFRQHHQVPLALVTLGGIGLVTVGIMSIILGIRILVNDVLQSRPHPPSPGHEKTRGTRTRRDNGPVTSNSSTLSLKD | Function: Regulates the composition and fluidity of the plasma membrane . Inhibits the incorporation of membrane-fluidizing phospholipids containing omega-3 long-chain polyunsaturated fatty acids (LCPUFA) and thereby promotes membrane rigidity . Does not appear to have any effect on LCPUFA synthesis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28733
Sequence Length: 264
Subcellular Location: Cell membrane
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Q9ZD47 | MTINASNIENSFSKINSHFSKLTDYIWPIKRHEISKFLFITLLMFCILFIQNLIRALKDSIVTTMIGAETISFLKFWGVMPSAFLITVIYVKLVNRMKAENIFYLIISIFLTFFALFAYVIFPNHEMLHLRPVTVHNLTASLPNLKWFILLLSKWSFSLFYIIAELWPNVVFALLFWQFVNNITTVEESKRFYPLFGLLSQTGIYLAGHFLENLSNINYYVTNKFALQSSFHTLSIQIILTIVLILGIVSIKTFWLLNHKVLDKKHMALLRFKTKNKSITIAKSFQMILSSRHIRLIATLLICYGIAINLVEGPWKAAATKIYKTPTEYAAFIGSYLSYTGVFTIFFVLLGSNIVRRMGWFTSAVITPSIVFITGILFFAVNNFEGFAGLIIANFILTDPALVAITIGAIQNVLSKSSKYTLFDSTKEMAYVPLEPEIKISGKAAADVIGTKLGKSGSAFLQSLIFIILPSASYQSISICLMIIFILTCVTWIWATKELNKEYKNSIKFSQK | Function: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58208
Sequence Length: 512
Subcellular Location: Cell membrane
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P50694 | MMKTLVVVLSLSLTILSFGGAHAATISFKNNCPYMVWPGTLTSDQKPQLSTTGFELASQASFQLDTPVPWNGRFWARTGCSTDASGKFVCATADCASGQVMCNGNGAIPPATLAEFNIPAGGGQDFYDVSLVDGFNLPMSVTPQGGTGDCKTASCPANVNAVCPSELQKKGSDGSVVACLSACVKFGTPQYCCTPPQNTPETCPPTNYSEIFHNACPDAYSYAYDDKRGTFTCNGGPNYAITFCP | Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 25707
Sequence Length: 245
Subcellular Location: Secreted
EC: 3.2.1.39
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Q9BXR5 | MRLIRNIYIFCSIVMTAEGDAPELPEERELMTNCSNMSLRKVPADLTPATTTLDLSYNLLFQLQSSDFHSVSKLRVLILCHNRIQQLDLKTFEFNKELRYLDLSNNRLKSVTWYLLAGLRYLDLSFNDFDTMPICEEAGNMSHLEILGLSGAKIQKSDFQKIAHLHLNTVFLGFRTLPHYEEGSLPILNTTKLHIVLPMDTNFWVLLRDGIKTSKILEMTNIDGKSQFVSYEMQRNLSLENAKTSVLLLNKVDLLWDDLFLILQFVWHTSVEHFQIRNVTFGGKAYLDHNSFDYSNTVMRTIKLEHVHFRVFYIQQDKIYLLLTKMDIENLTISNAQMPHMLFPNYPTKFQYLNFANNILTDELFKRTIQLPHLKTLILNGNKLETLSLVSCFANNTPLEHLDLSQNLLQHKNDENCSWPETVVNMNLSYNKLSDSVFRCLPKSIQILDLNNNQIQTVPKETIHLMALRELNIAFNFLTDLPGCSHFSRLSVLNIEMNFILSPSLDFVQSCQEVKTLNAGRNPFRCTCELKNFIQLETYSEVMMVGWSDSYTCEYPLNLRGTRLKDVHLHELSCNTALLIVTIVVIMLVLGLAVAFCCLHFDLPWYLRMLGQCTQTWHRVRKTTQEQLKRNVRFHAFISYSEHDSLWVKNELIPNLEKEDGSILICLYESYFDPGKSISENIVSFIEKSYKSIFVLSPNFVQNEWCHYEFYFAHHNLFHENSDHIILILLEPIPFYCIPTRYHKLKALLEKKAYLEWPKDRRKCGLFWANLRAAINVNVLATREMYELQTFTELNEESRGSTISLMRTDCL | Function: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 94564
Sequence Length: 811
Subcellular Location: Membrane
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Q6R5P0 | MPRMERHQFCSVLLILILLTLVSLTLTGWAWTIPDCIIADSLLFPNLSYYIPFCTSAPGLHLLASCSNVKNLNQTLKRVPRNTEVLCLQGMVPTLPAKAFIRFHSLQLLRLQLRTTSVTSRTFQGLDQLQYLFFDHHAPCCLSLFLSPNCFESLRSLSSLSFQGYCLTYSQSIYLPTSLRHLTLRNSCLTKFQDLQRLFPDLLLSTSSTPNIKPGAPFLETLDLSYNLQLKQAGVRDLYGLTLHSLILDGTPLKALDLTDSGLLHLHFLSLVGTGIEKVPASLTGYSELRALDLGKNQIQNILENGEIPGYKALEFLSLHDNHLQTLPTRFLHTLPQLQKLNLSMNKLGPILELPEGLFSTNLKVLDLSYNQLCDVPHGALSLLSQLQELWLSGNNISSLSNESLQGLRQLRTLDLSWNQIKVLKPGWLSHLPALTTLNLLGTYLEYILGIQLQGPKMLRHLQLGSYPILDIYPPWPPTLLSLEIQAESCIQFMIHSGQPFLFLENLTLETSILLLKPDNITIHFPSLRRLTLRGYSFIFSTSQLQRFFPQQLPLLEHFFIWCENSYAVDLYLFGMPRLRVLELGYLNFFYESSTMKLEMLLKEVPQLQVLALSHLNLRNLSVSSFKSLQDLKLLLFNSERALEMNSNLQEFIPQMPQYVYFSDVTFTCQCEASWLESWATRAPNTFVYGLEKSICIANASDYSKTLLFSFLATNCPHGTEFWGFLTSFILLLLLIILPLISCPKWSWLHHLWTLFHTCWWKLCGHRLRGQFNYDVFISYCEEDQAWVLEELVPVLEKAPPEGEGLRLCLPARDFGIGNDRMESMIASMGKSRATLCVLTGQALASPWCNLELRLATYHLVARPGTTHLLLLFLEPLDRQRLHSYHRLSRWLQKEDYFDLSQGKVEWNSFCEQLKRRLSKAGQERD | Function: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 105873
Sequence Length: 926
Subcellular Location: Membrane
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Q6QNU9 | MGRYWLLPGLLLSLPLVTGWSTSNCLVTEGSRLPLVSRYFTFCRHSKLSFLAACLSVSNLTQTLEVVPRTVEGLCLGGTVSTLLPDAFSAFPGLKVLALSLHLTQLLPGALRGLGQLQSLSFFDSPLRRSLFLPPDAFSDLISLQRLHISGPCLDKKAGIRLPPGLQWLGVTLSCIQDVGELAGMFPDLVQGSSSRVSWTLQKLDLSSNWKLKMASPGSLQGLQVEILDLTRTPLDAVWLKGLGLQKLDVLYAQTATAELAAEAVAHFELQGLIVKESKIGSISQEALASCHSLKTLGLSSTGLTKLPPGFLTAMPRLQRLELSGNQLQSAVLCMNETGDVSGLTTLDLSGNRLRILPPAAFSCLPHLRELLLRYNQLLSLEGYLFQELQQLETLKLDGNPLLHLGKNWLAALPALTTLSLLDTQIRMSPEPGFWGAKNLHTLSLKLPALPAPAVLFLPMYLTSLELHIASGTTEHWTLSPAIFPSLETLTISGGGLKLKLGSQNASGVFPALQKLSLLKNSLDAFCSQGTSNLFLWQLPKLQSLRVWGAGNSSRPCLITGLPSLRELKLASLQSITQPRSVQLEELVGDLPQLQALVLSSTGLKSLSAAAFQRLHSLQVLVLEYEKDLMLQDSLREYSPQMPHYIYILESNLACHCANAWMEPWVKRSTKTYIYIRDNRLCPGQDRLSARGSLPSFLWDHCPQTLELKLFLASSALVFMLIALPLLQEARNSWIPYLQALFRVWLQGLRGKGDKGKRFLFDVFVSHCRQDQGWVIEELLPALEGFLPAGLGLRLCLPERDFEPGKDVVDNVVDSMLSSRTTLCVLSGQALCNPRCRLELRLATSLLLAAPSPPVLLLVFLEPISRHQLPGYHRLARLLRRGDYCLWPEEEERKSGFWTWLRSRLG | Function: Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Plays a role in preventing infection of internal organs of the urogenital system.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 99945
Sequence Length: 906
Subcellular Location: Membrane
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Q6R5N8 | MSGLYRILVQLEQSPYVKTVPLNMRRDFFFLVVTWMPKTVKMNGSSFVPSLQLLLMLVGFSLPPVAETYGFNKCTQYEFDIHHVLCIRKKITNLTEAISDIPRYTTHLNLTHNEIQVLPPWSFTNLSALVDLRLEWNSIWKIDEGAFRGLENLTLLNLVENKIQSVNNSFEGLSSLKTLLLSHNQITHIHKDAFTPLIKLKYLSLSRNNISDFSGILEAVQHLPCLERLDLTNNSIMYLDHSPRSLVSLTHLSFEGNKLRELNFSALSLPNLTNLSASRNGNKVIQNVYLKTLPQLKSLNLSGTVIKLENLSAKHLQNLRAMDLSNWELRHGHLDMKTVCHLLGNLPKLETLVFQKNVTNAEGIKQLAKCTRLLFLDLGQNSDLIYLNDSEFNALPSLQKLNLNKCQLSFINNRTWSSLQNLTSLDLSHNKFKSFPDFAFSPLKHLEFLSLSRNPITELNNLAFSGLFALKELNLAACWIVTIDRYSFTQFPNLEVLDLGDNNIRTLNHGTFRPLKKLQSLILSHNCLKILEPNSFSGLTNLRSLDLMYNSLSYFHEHLFSGLEKLLILKLGFNKITYETTRTLQYPPFIKLKSLKQLNLEGQRHGIQVVPSNFFQGLGSLQELLLGKNPSVFLDHHQFDPLINLTKLDISGTKDGDRSLYLNASLFQNLKRLKILRLENNNLESLVPDMFSSLQSLQVFSLRFNNLKVINQSHLKNLKSLMFFDVYGNKLQCTCDNLWFKNWSMNTEEVHIPFLRSYPCQQPGSQSLLIDFDDAMCNFDLGKVYFLCSFSMVLSTMVFSWFSTKMIASLWYGLYICRAWYLTKWHKTEKKFLYDAFVSFSATDEAWVYKELVPALEQGSQTTFKLCLHQRDFEPGIDIFENIQNAINTSRKTLCVVSNHYLHSEWCRLEVQLASMKMFYEHKDVIILIFLEEIPNYKLSSYHRLRKLINKQTFITWPDSVHQQPLFWARIRNALGKETVEKENTHLIVVE | Function: Component of innate and adaptive immunity that recognizes and binds 23S rRNA from bacteria. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Specifically binds the 5'-CGGAAAGACC-3' sequence on bacterial 23S rRNA, a sequence also bound by MLS group antibiotics (including erythromycin). May also recognize vesicular stomatitis virus; however, these data require additional evidences.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 114443
Sequence Length: 991
Subcellular Location: Endosome membrane
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P30974 | MSEIVDTELLVNCTILAVRRFELNSIVNTTLLGSLNRTEVVSLLSSIIDNRDNLESINEAKDFLTECLFPSPTRPYELPWEQKTIWAIIFGLMMFVAIAGNGIVLWIVTGHRSMRTVTNYFLLNLSIADLLMSSLNCVFNFIFMLNSDWPFGSIYCTINNFVANVTVSTSVFTLVAISFDRYIAIVHPLKRRTSRRKVRIILVLIWALSCVLSAPCLLYSSIMTKHYYNGKSRTVCFMMWPDGRYPTSMADYAYNLIILVLTYGIPMIVMLICYSLMGRVLWGSRSIGENTDRQMESMKSKRKVVRMFIAIVSIFAICWLPYHLFFIYAYHNNQVASTKYVQHMYLGFYWLAMSNAMVNPLIYYWMNKRFRMYFQRIICCCCVGLTRHRFDSPKSRLTNKNSSNRHTRAETKSQWKRSTMETQIQQAPVTSSCREQRSAQQQQPPGSGTNRAAVECIMERPADGSSSPLCLSINNSIGERQRVKIKYISCDEDNNPVELSPKQM | Function: Receptor for tachykinin-like peptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58020
Sequence Length: 504
Subcellular Location: Cell membrane
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Q86T26 | MYRHGISSQRSWPLWTTIFIFLGVAAILGVTIGLLVHFLAVEKTYYYQGDFHISGVTYNDNCENAASQASTNLSKDIETKMLNAFQNSSIYKEYVKSEVIKLLPNANGSNVQLQLKFKFPPAEGVSMRTKIKAKLHQMLKNNMASWNAVPASIKLMEISKAASEMLTNNCCGRQVANSIITGNKIVNGKSSLEGAWPWQASMQWKGRHYCGASLISSRWLLSAAHCFAKKNNSKDWTVNFGIVVNKPYMTRKVQNIIFHENYSSPGLHDDIALVQLAEEVSFTEYIRKICLPEAKMKLSENDNVVVTGWGTLYMNGSFPVILQEDFLKIIDNKICNASYAYSGFVTDTMLCAGFMSGEADACQNDSGGPLAYPDSRNIWHLVGIVSWGDGCGKKNKPGVYTRVTSYRNWITSKTGL | Function: Serine protease.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46337
Sequence Length: 416
Subcellular Location: Cell membrane
EC: 3.4.21.-
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Q14C59 | MYRPVIASRKSIPPWLIILCVLGVLAALGIIIGLLVHFLAVENKIYYYQGGFKVLDIPYDRNYERETSLESNYLSKILENKMVEAFQNSNIYKQYINSQVITLVPDNNSVTAHIWLVFKDPWSNKENLRRRIESILRQMLENNPESLTTDPGSLKLTEISKVDAEKIINNRCGRRPRMSATYDRITGGSTAHKGEWPWQASLRVNGKHYCGASLIGERFLLTAAHCFQGTNNPKNLTVSFGTRVTPAYMQHSVQEIIIHEDYVKGEHHDDVAVIKLTEKVSFNNDVHRVCLPESTQIFPPGEGVVVTGWGSFSYNGKSPLLLQKASIKIIDTNTCNSEEAYGGRIVDTMLCAGYLEGSIDACQGDSGGPLVHPNSRDIWYLVGIVSWGHECGRVNKPGVYMRVTSYRNWIASKTGI | Function: Serine protease.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46713
Sequence Length: 416
Subcellular Location: Cell membrane
EC: 3.4.21.-
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Q1JRP2 | MARGQPRRSEEQWTALQNRTECKTKIKLTRCGKITLGILTAVLAAVLIGLIAYFAACGKDSFYYHVSFKVNNIDYDSKFAKPYSQEYMDLNKRIVSLMNETFHESKLRKQYVKAHTVQVSKAKGKVVIHAVLKFKACYRNNVEKYWESVETTLYQKLKGQTGLLIDSSSFKFSDIAMPIAEDLLNTCCGRRTIIHRGHKVAGGQDAEEGEWPWQASLQQNSVHRCGATLISNYWLITAAHCFIRAANPKDWKVSFGFLLSKPQAPRAVKNIIIHENYSYPAHDNDIAVVRLSSPVLYESNIRRACLPEATQKFPPNSDVVVTGWGTLKSDGDSPNILQKGKVKIIDNKTCNSGKAYGGMITPGMMCAGFLKGRVDACQGDSGGPLVSEDSKGIWFLAGIVSWGDECALPNKPGVYTRVTYYRDWITSKTGL | Function: Serine protease which has a preference for Arg or Lys in position P1 and uncharged residues in positions P2 and P3. Shows specificity towards FGF2 in vitro.
PTM: Proteolytically cleaved via an autocatalytic mechanism.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48073
Sequence Length: 431
Subcellular Location: Cell membrane
EC: 3.4.21.-
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O60235 | MYRPARVTSTSRFLNPYVVCFIVVAGVVILAVTIALLVYFLAFDQKSYFYRSSFQLLNVEYNSQLNSPATQEYRTLSGRIESLITKTFKESNLRNQFIRAHVAKLRQDGSGVRADVVMKFQFTRNNNGASMKSRIESVLRQMLNNSGNLEINPSTEITSLTDQAAANWLINECGAGPDLITLSEQRILGGTEAEEGSWPWQVSLRLNNAHHCGGSLINNMWILTAAHCFRSNSNPRDWIATSGISTTFPKLRMRVRNILIHNNYKSATHENDIALVRLENSVTFTKDIHSVCLPAATQNIPPGSTAYVTGWGAQEYAGHTVPELRQGQVRIISNDVCNAPHSYNGAILSGMLCAGVPQGGVDACQGDSGGPLVQEDSRRLWFIVGIVSWGDQCGLPDKPGVYTRVTAYLDWIRQQTGI | Function: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Proteolytically cleaves and activates the human coronavirus 229E (HCoV-229E) spike glycoprotein which facilitate virus-cell membrane fusions; spike proteins are synthesized and maintained in precursor intermediate folding states and proteolysis permits the refolding and energy release required to create stable virus-cell linkages and membrane coalescence. Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides, cleaving Boc-Phe-Ser-Arg-4-methylcoumaryl-7-amide most efficiently and having an optimum pH of 8.6 with this substrate.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46263
Sequence Length: 418
Subcellular Location: Cell membrane
EC: 3.4.21.-
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Q8VHJ4 | MYRPRSMVSPSRFFNPFMVALIVIITVGLLAMTAGLLIHFLAFDKRAYFYHSNFHILNVDYTEALNSPATHEYRTLSERIESMITDAFRESNLRSEFIRTHVVKLRKEGSGVVADVVMKFRSSKRNNKKAIKTRIQSVLQRLSSSGNLEIAPSNGITSLTDQDTENVLTQECGARPDLITLSEERIIGGTQAETGDWPWQVSLQLNNVHHCGGTLISNLWVLTAAHCFRSYSNPQQWTATFGVSTISPRLRVRVRAILAHAEYNSITRDNDIAVVQLDRPVTFTRNIHRVCLPAATQNIMPDSVAYVTGWGSLTYGGNTVTNLQQGEVRIVSSEVCNEPAGYGGSVLPGMLCAGVRSGAVDACQGDSGGPLVQEDTRRLWFVVGIVSWGYQCGLPNKPGVYTRVTAYRNWIRQQTGI | Function: May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions. Plays a role in the proteolytic processing of ACE2. Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides (By similarity). Isoform 2 may play a key role in regulating adrenal proliferation by specifically cleaving N-POMC.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46288
Sequence Length: 417
Subcellular Location: Cell membrane
EC: 3.4.21.-
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Q9UL52 | MMYRPDVVRARKRVCWEPWVIGLVIFISLIVLAVCIGLTVHYVRYNQKKTYNYYSTLSFTTDKLYAEFGREASNNFTEMSQRLESMVKNAFYKSPLREEFVKSQVIKFSQQKHGVLAHMLLICRFHSTEDPETVDKIVQLVLHEKLQDAVGPPKVDPHSVKIKKINKTETDSYLNHCCGTRRSKTLGQSLRIVGGTEVEEGEWPWQASLQWDGSHRCGATLINATWLVSAAHCFTTYKNPARWTASFGVTIKPSKMKRGLRRIIVHEKYKHPSHDYDISLAELSSPVPYTNAVHRVCLPDASYEFQPGDVMFVTGFGALKNDGYSQNHLRQAQVTLIDATTCNEPQAYNDAITPRMLCAGSLEGKTDACQGDSGGPLVSSDARDIWYLAGIVSWGDECAKPNKPGVYTRVTALRDWITSKTGI | Function: Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 47696
Sequence Length: 423
Subcellular Location: Cell membrane
EC: 3.4.21.-
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Q5S248 | MYRSCVVRARKRTCVEPWVIGIISFLSLIVLAVCIGLTVHYVRYNHRRTYNYYSTLSFTSDKLYSEFGREASKNFTEMSQRIETMVKHAFHKSPLRGQLVKAHIIKFSKEDDGVLAHMLLIFRIRSTEDPETVHKIIEYVLHEKLKYATGPPNVDPESVKIKKINKTESDNYFNHCCGTRRNKSTVQTSVRIVGGTPVEEEEWPWQSSLRWDGSHRCGATLINNTWLVTAAHCFRTHKDPSRWSATFGATLQPRKLTTGIRRIIVHEKYKYPSHDYDIALAELSKPVPCTNAVHKVCLPDANHEFQPGQRMFVTGFGALKNDGFTQNNLRQVQVDYIDTQTCNQPQSYNGAITPRMLCAGFLKGEKDACQGDSGGPLVTADVRDIWYLAGVVSWGDECGQPNKPGVYTRVTAFRHWIASNTGI | Function: Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48065
Sequence Length: 423
Subcellular Location: Cell membrane
EC: 3.4.21.-
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Q6ZWK6 | MMYAPVEFSEAEFSRAEYQRKQQFWDSVRLALFTLAIVAIIGIAIGIVTHFVVEDDKSFYYLASFKVTNIKYKENYGIRSSREFIERSHQIERMMSRIFRHSSVGGRFIKSHVIKLSPDEQGVDILIVLIFRYPSTDSAEQIKKKIEKALYQSLKTKQLSLTINKPSFRLTPIDSKKMRNLLNSRCGIRMTSSNMPLPASSSTQRIVQGRETAMEGEWPWQASLQLIGSGHQCGASLISNTWLLTAAHCFWKNKDPTQWIATFGATITPPAVKRNVRKIILHENYHRETNENDIALVQLSTGVEFSNIVQRVCLPDSSIKLPPKTSVFVTGFGSIVDDGPIQNTLRQARVETISTDVCNRKDVYDGLITPGMLCAGFMEGKIDACKGDSGGPLVYDNHDIWYIVGIVSWGQSCALPKKPGVYTRVTKYRDWIASKTGM | Function: Probable serine protease.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49410
Sequence Length: 438
Subcellular Location: Membrane
EC: 3.4.21.-
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Q5QSK2 | MYQPGILGRRKRVCKPWTVALTTTAALLALAVLIGLLVYFLVYEEKTHYYQASFWIPSIKYSSDLSEEQSKLQINLKQKINNEIDVIFQRSSLKHHYVKSQVVNFRPSNDGVKADILIKFQIPRKNADTLRSEADSILNKKLQSSQSFLKRDISLPYLREMNAAQAEHILNSNCGLGMEYPRIARIADGKPAGSNSWPWQSSLQVEGIHLCGASLIGSQWLVTSAHCFDNYKNPKLWTVSFGRTLGNPLTTRKVESIIIHENYAAHKHDDDIAVVKLSSPVLFSENLRTVCLPEATFQVLPKSKVFVTGWGALKANGPFPNSLQEVEIEIISNDVCNQVNVYGGAISSGMICAGFLTGKLDACEGDSGGPLVISDNRNKWYLLGIVSWGIDCGKENKPGIYTRVTHYRNWIKSKTNI | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46593
Sequence Length: 417
Subcellular Location: Membrane
EC: 3.4.21.-
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Q8QFN3 | MVLPPPDKRHVCLTTIVIMTSMAFMDAYLVEQNQGPRKIGVCIIVLVGDICFLIVLRYVAVWVGAEVKTAKRGYAMILWFLYIFVLEIKLYFIFQNYKADKKNLETVARKALTLLLSICVPGLYLVLVALDSMEYIRTFRKKEDLRGRLFWVALDLLDILDIQANLWEPHRTGLPIWAEGLMFFYCYILLLILPCVSLSEISMQGEHIAPQKMMLYPVLSLVTINIVTIFIRAINMVLFQDSRVSTIFIGKNIIAIATKACTFLEYKRQVKEFPQNAIALELQQNSLSHNQTLHSTQGIPHEPSPTSEILDT | Function: May play a role in MAPK signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35676
Sequence Length: 312
Subcellular Location: Membrane
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Q9BTD3 | MVLPPPDRRHVCLTTLVIMGSMAVMDAYLVEQNQGPRKIGVCIIVLVGDVCFLLVLRYVAVWVGAEVRTAKRGYAMILWFLYIFVLEIKLYFIFQNYKAARRGAADPVARKALTLLLSVCVPGLFLLLVALDRMEYVRTFRKREDLRGRLFWVALDLLDLLDMQASLWEPPRSGLPLWAEGLTFFYCYMLLLVLPCVALSEVSMQGEHIAPQKMMLYPVLSLATVNVVAVLARAANMALFRDSRVSAIFVGKNVVALATKACTFLEYRRQVRDFPPPALSLELQPPPPQRNSVPPPPPPLHGPPGRPHMSSPTRDPLDT | Function: May play a role in MAPK signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35814
Sequence Length: 319
Subcellular Location: Membrane
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Q5ZK32 | MAPKGKAGTKGKKQIFEENRETLRFYLRIILGASAVYAAVNLVVFYPAASAWTWLAFAFSSAVYGASYRSMSSMARPAFADDGSLADGGIDLNMEQGWQSECPHPHEPRHLKDVILLTAMVQVLSCFSLYVWYFWLLAPGRALYLLWVNILGPWFTAESSAPGQEPNEKKQRRTGTPPE | Function: May function as a negative regulator of endoplasmic reticulum-stress induced autophagy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19967
Sequence Length: 179
Subcellular Location: Endoplasmic reticulum membrane
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Q9BTX3 | MAPKGKVGTRGKKQIFEENRETLKFYLRIILGANAIYCLVTLVFFYSSASFWAWLALGFSLAVYGASYHSMSSMARAAFSEDGALMDGGMDLNMEQGMAEHLKDVILLTAIVQVLSCFSLYVWSFWLLAPGRALYLLWVNVLGPWFTADSGTPAPEHNEKRQRRQERRQMKRL | Function: May function as a negative regulator of endoplasmic reticulum-stress induced autophagy.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19642
Sequence Length: 173
Subcellular Location: Endoplasmic reticulum membrane
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Q9NX78 | MSPHGDGRGQAQGRAVRVGLRRSGGIRGGVAVFAAVAAVFTFTLPPSVPGGDSGELITAAHELGVAHPPGYPLFTLVAKLAITLFPFGSIAYRVNLLCGLFGAVAASLLFFTVFRLSGSSAGGILAAGVFSFSRLTWQWSIAAEVFSLNNLFVGLLMALTVHFEEAATAKERSKVAKIGAFCCGLSLCNQHTIILYVLCIIPWILFQLLKKKELSLGSLLKLSLYFSAGLLPYVHLPISSYLNHARWTWGDQTTLQGFLTHFLREEYGTFSLAKSEIGSSMSEILLSQVTNMRTELSFNIQALAVCANICLATKDRQNPSLVWLFTGMFCIYSLFFAWRANLDISKPLFMGVVERFWMQSNAVVAVLAGIGLAAVVSETNRVLNSNGLQCLEWLSATLFVVYQIYSNYSVCDQRTNYVIDKFAKNLLTSMPHDAIILLRGDLPGNSLRYMHYCEGLRPDISLVDQEMMTYEWYLPKMAKHLPGVNFPGNRWNPVEGILPSGMVTFNLYHFLEVNKQKETFVCIGIHEGDPTWKKNYSLWPWGSCDKLVPLEIVFNPEEWIKLTKSIYNWTEEYGRFDPSSWESVANEEMWQARMKTPFFIFNLAETAHMPSKVKAQLYAQAYDLYKEIVYLQKEHPVNWHKNYAIACERMLRLQARDADPEVLLSETIRHFRLYSQKAPNDPQQADILGALKHLRKELQSLRNRKNV | Function: O-mannosyl-transferase that transfers mannosyl residues to the hydroxyl group of serine or threonine residues of proteins . Specifically glycosylates the IPT/TIG domain of target proteins, such as MET and MST1R/RON . TMEM260-mediated O-mannosylated residues are composed of single mannose glycans that are not elongated or modified .
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79536
Sequence Length: 707
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.109
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E9PQX1 | MWLQDRIATFFFPKGMMLTTAALMLFFLHLGIFIRDVHNFCITYHYDHMSFHYTVVLMFSQVISICWAAMGSLYAEMTENKYVCFSALTILMLNGAMFFNRLSLEFLAIEYREEHH | Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13758
Sequence Length: 116
Subcellular Location: Cell projection
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Q3SYV1 | MNQTDKNQQEIPSYLSDEPPEGSMKDHPQQQPGMLSRVTGGIFSVTKGAVGATIGGVAWIGGKSLEVTKTAVTTVPSMGIGLVKGGVSAVAGGVTAVGSAVVNKVPLTGKKKDKSD | Function: May play a role in bone development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11721
Sequence Length: 116
Subcellular Location: Membrane
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Q5ZLA9 | MNQTDKSHQEVPSYLHDEPPEGSIKDHPQQQPSMLSRVTGGIFSVTKGAVGATIGGVAWIGGKSLEITKTAVTSVPSMGVGLVKGSVSAVAGGVTAVGSAVASKVPLTGKKKDKSD | Function: May be involved in the growth pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11712
Sequence Length: 116
Subcellular Location: Membrane
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Q8WUH6 | MNQTDKNQQEIPSYLNDEPPEGSMKDHPQQQPGMLSRVTGGIFSVTKGAVGATIGGVAWIGGKSLEVTKTAVTTVPSMGIGLVKGGVSAVAGGVTAVGSAVVNKVPLTGKKKDKSD | Function: May play a role in bone development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11748
Sequence Length: 116
Subcellular Location: Membrane
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Q2M3C6 | MAVAPSFNMTNPQPAIEGGISEVEIISQQVDEETKSIAPVQLVNFAYRDLPLAAVDLSTAGSQLLSNLDEDYQREGSNWLKPCCGKRAAVWQVFLLSASLNSFLVACVILVVILLTLELLIDIKLLQFSSAFQFAGVIHWISLVILSVFFSETVLRIVVLGIWDYIENKIEVFDGAVIILSLAPMVASTVANGPRSPWDAISLIIMLRIWRVKRVIDAYVLPVKLEMEMVIQQYEKAKVIQDEQLERLTQICQEQGFEIRQLRAHLAQQDLDLAAEREAALQAPHVLSQPRSRFKVLEAGTWDEETAAESVVEELQPSQEATMKDDMNSYISQYYNGPSSDSGVPEPAVCMVTTAAIDIHQPNISSDLFSLDMPLKLGGNGTSATSESASRSSVTRAQSDSSQTLGSSMDCSTAREEPSSEPGPSPPPLPSQQQVEEATVQDLLSSLSEDPCPSQKALDPAPLARPSPAGSAQTSPELEHRVSLFNQKNQEGFTVFQIRPVIHFQPTVPMLEDKFRSLESKEQKLHRVPEA | Function: Voltage-sensor protein present on the post-synaptic side of glutamatergic mossy fibers and granule cells in the cerebellum . Despite the presence of a voltage-sensor segment, does not form a functional ion channel and its precise role remains unclear . Undergoes both rapid and slow structural rearrangements in response to changes in voltage . Contains a zinc-binding site that can regulate the slow conformational transition .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58444
Sequence Length: 531
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position . Transplantation of the transmembrane segment S4 into HVCN1, generates a functional voltage-activated proton channel .
Subcellular Location: Cell membrane
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Q8BZB3 | MALVTSFNMANPQPAIEGGISEVEIISQQVDEETKSIAPVQLVNFAYRDLPLAAVDLSTGGSQLLSNLDEEYQREGSDWLKPCCGKRAAVWQVFLLSASLNSFLVACVILVVILLTLELLIDTKLLQFSNAFQFAGVIHWISLVILSVFFSETVLRIVVLGIWDYIENKIEVFDGAVIILSLAPMVASTVANGPRSPWDAISLIIMFRIWRVKRVIDAYVLPVKLEMEMVTQQYEKAKAIQDEQLERLTQICQEQGFEIRQLRAHLAQQDLDLAAEREAALQAPHVLSQPRSRYKVVEAGTWAEETAAESIVEELRPSQEATVKDDMNSYISQYYNGPSSDSGAPEPAVCVVTTAAIDIHQPNVPSDLFSVDLPLKLSGNSTCASATSETTSHSTCGSVTRAQSASSQTLGSSTDCSTPREELLPSKPRSSPLPLLLPPQQLVAEATVQDLMSSLSKDPCPSHKALDPAPLAQPTPLGSVQTSPELEHRVSLFNQKNQEALPVLQINPVIHLQPTAGLEEKFRSLESKEPKLHTVPEA | Function: Voltage-sensor protein present on the post-synaptic side of glutamatergic mossy fibers and granule cells in the cerebellum. Despite the presence of a voltage-sensor segment, does not form a functional ion channel and its precise role remains unclear. Undergoes both rapid and slow structural rearrangements in response to changes in voltage. Contains a zinc-binding site that can regulate the slow conformational transition.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58897
Sequence Length: 538
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Transplantation of the transmembrane segment S4 into HVCN1, generates a functional voltage-activated proton channel.
Subcellular Location: Cell membrane
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Q6UXY8 | MSAYYRNNWSEEDPDYPDYSGSQNRTQGYLKTQGYPDVPGPLNNPDYPGTRSNPYSVASRTRPDYPGSLAEPNYPRSLSNPDYSGTRSNAYSAASRTSPDHPTSLPEPDYSEFQSHPYHRASSRQPDYPGSQRNPDFAGSSSSGNYAGSRTHPDHFGSLEPDYPGAQSNSDHPGPRANLNHPGSRKNLEHTSFRINPYADSLGKPDYPGADIQPNSPPFFGEPDYPSAEDNQNLPSTWREPDYSDAENGHDYGSSETPKMTRGVLSRTSSIQPSFRHRSDDPVGSLWGENDYPEGIEMASMEMANSYGHSLPGAPGSGYVNPAYVGESGPVHAYGNPPLSECDWHKSPQGQKLIASLIPMTSRDRIKAIRNQPRTMEEKRNLRKIVDKEKSKQTHRILQLNCCIQCLNSISRAYRRSKNSLSEILNSISLWQKTLKIIGGKFGTSVLSYFNFLRWLLKFNIFSFILNFSFIIIPQFTVAKKNTLQFTGLEFFTGVGYFRDTVMYYGFYTNSTIQHGNSGASYNMQLAYIFTIGACLTTCFFSLLFSMAKYFRNNFINPHIYSGGITKLIFCWDFTVTHEKAVKLKQKNLSTEIRENLSELRQENSKLTFNQLLTRFSAYMVAWVVSTGVAIACCAAVYYLAEYNLEFLKTHSNPGAVLLLPFVVSCINLAVPCIYSMFRLVERYEMPRHEVYVLLIRNIFLKISIIGILCYYWLNTVALSGEECWETLIGQDIYRLLLMDFVFSLVNSFLGEFLRRIIGMQLITSLGLQEFDIARNVLELIYAQTLVWIGIFFCPLLPFIQMIMLFIMFYSKNISLMMNFQPPSKAWRASQMMTFFIFLLFFPSFTGVLCTLAITIWRLKPSADCGPFRGLPLFIHSIYSWIDTLSTRPGYLWVVWIYRNLIGSVHFFFILTLIVLIITYLYWQITEGRKIMIRLLHEQIINEGKDKMFLIEKLIKLQDMEKKANPSSLVLERREVEQQGFLHLGEHDGSLDLRSRRSVQEGNPRA | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 114797
Sequence Length: 1006
Subcellular Location: Membrane
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Q7Z403 | MAQPLAFILDVPETPGDQGQGPSPYDESEVHDSFQQLIQEQSQCTAQEGLELQQREREVTGSSQQTLWRPEGTQSTATLRILASMPSRTIGRSRGAIISQYYNRTVQLRCRSSRPLLGNFVRSAWPSLRLYDLELDPTALEEEEKQSLLVKELQSLAVAQRDHMLRGMPLSLAEKRSLREKSRTPRGKWRGQPGSGGVCSCCGRLRYACVLALHSLGLALLSALQALMPWRYALKRIGGQFGSSVLSYFLFLKTLLAFNALLLLLLVAFIMGPQVAFPPALPGPAPVCTGLELLTGAGCFTHTVMYYGHYSNATLNQPCGSPLDGSQCTPRVGGLPYNMPLAYLSTVGVSFFITCITLVYSMAHSFGESYRVGSTSGIHAITVFCSWDYKVTQKRASRLQQDNIRTRLKELLAEWQLRHSPRSVCGRLRQAAVLGLVWLLCLGTALGCAVAVHVFSEFMIQSPEAAGQEAVLLVLPLVVGLLNLGAPYLCRVLAALEPHDSPVLEVYVAICRNLILKLAILGTLCYHWLGRRVGVLQGQCWEDFVGQELYRFLVMDFVLMLLDTLFGELVWRIISEKKLKRRRKPEFDIARNVLELIYGQTLTWLGVLFSPLLPAVQIIKLLLVFYVKKTSLLANCQAPRRPWLASHMSTVFLTLLCFPAFLGAAVFLCYAVWQVKPSSTCGPFRTLDTMYEAGRVWVRHLEAAGPRVSWLPWVHRYLMENTFFVFLVSALLLAVIYLNIQVVRGQRKVICLLKEQISNEGEDKIFLINKLHSIYERKEREERSRVGTTEEAAAPPALLTDEQDA | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90045
Sequence Length: 805
Subcellular Location: Endoplasmic reticulum membrane
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Q7TN60 | MAQSLALALDVPETTGDEGLEPSPYEESEVHDSFHQLIQEQSLRVAEEGLELLPLGLGRGDQTLPGLEGAPALSSATLRILASMPSRTIGRSRGAIISQYYNRTVRLRRRSSRPLLGNVVPSARPSLRLYDLELDSTILEEDEKRSLLVKELQGLSAAQRDHMVRNMPLSLGEKRCLREKSWSPKGKRRHLQGRSGAFSCCSRLRYTCMLALHSLGLALLSGLYAARPWRYALKQIGGQFGSSVLSYFLFLKTLLAFNALMLLPLLAFLVGVQAAFPPDPAGPVPTFSGLELLTGGGRFTHTVMYYGYYSNSTLSPSCDAPREGGQCSPRLGSLPYNMPLAYLFTMGATFFLTCIILVYSMSHSFGESYRVGSTKGIHALTVFCSWDYKVTQKRASRVQQDSICTQLKELLAEWHLRKRPRSVCGQLRQVVVLGLGWLLCLGSTMGCTVAVLTFSEVMIQRPASGGQGVEALALPLVVSVLNLGASYLFRGLATLERHDSPVLEVYMAICRNLILKMAVLGVLCYHWLGRRVATLQGQCWEDFVGQELYRFMVVDFIFMLLDSLFGELVWRLISEKKLKRGQKPEFDIARNVLDLIYGQTLTWLGVLFSPLLPAVQILRLLFLFHIKKASLMANCQAPRRPWLASHMSTVFLTLLCFPSFLGAAVFLCYAVWQVRPSSTCGPFRTLNTMYEAGTVWVRRLEHAGSGASWLPWLHHFLVENTFFLFLASALLLAVIYFNIQVVKGQRKVICLLKEQIRNEGEDKIFLINKLHSVYEEEGRSRPGRTQDATEPPAWHEDGGDQKEPCNPRSP | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90546
Sequence Length: 810
Subcellular Location: Endoplasmic reticulum membrane
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Q5YCC5 | MSEFGAGAELPGWVTESRSRGEFFSPEESHAAAPAGFLQELPSYRSVLWRRAAAGDVQERWGNLRGIASAERREPQPDGGERGAIPLWELPFSIAEKRDSQQGDIKYSSGWNHWKRTSSKSWKKALKDIKELSSYMQLWRHDIHSIEGKFGTGIQSYFSFLRFLVLLNFLMFILMFSFVTLPAVISNYGIFNSSSTKISPNNTEPYCTVYTPSGNKGLVYFYTYLKDLLTGTGFLEVTVLFYGYYTIDAAWFSVLRYNLPLAYLLTTFAYLALSFVWIIKRSVERFRQHLVDDEDQFQSYCNKVFAGWDFCITDLNAARLKHRSLLYELQTNLEEERLKQKIAERTMKEKLQIYSLRIFINIIVIAVLSGCFYSIYRATVFSQENSSVSIRRNVMIANLLVQYLPSIVITSANFIAPQIFSFLIRFEDYSAAFEIRLTLIRCVFVRLANVGVLLFSLWSQIHCDNDQCKACGYDYELYPCWESAVGQEMYKLLIFDFMIIIAMTLFVDFPRKLLVTYCSWKLVQWWGLQEFGISDNVLEIIYGQTICWIGTFFSPLLPAIATIKYFIIFYIKKISLIHTRKPASRPIRASSSNFFFLAVLLIGLILAFVPLGVSIALISSSKACGPFRNFNTSWAIVPYTILEFPIGLQKFLYGIASEAFAVPFFVIACLFMFYFIALAGAHKRVVEQLREQLVTESRDKLFLLEKLSEAQKNSGKPQKARKLTSSWLLEPLDKG | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84377
Sequence Length: 735
Subcellular Location: Membrane
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Q7Z402 | MSESSGSALQPGRPSRQPAVHPENLSLDSSCFSSPPVNFLQELPSYRSIARRRTTVHSRDKQSGTLLKPTDSYSSQLEDRIAENLSSHSLRNYALNISEKRRLRDIQETQMKYLSEWDQWKRYSSKSWKRFLEKAREMTTHLELWREDIRSIEGKFGTGIQSYFSFLRFLVLLNLVIFLIIFMLVLLPVLLTKYKITNSSFVLIPFKDMDKQCTVYPVSSSGLIYFYSYIIDLLSGTGFLEETSLFYGHYTIDGVKFQNFTYDLPLAYLLSTIASLALSLLWIVKRSVEGFKINLIRSEEHFQSYCNKIFAGWDFCITNRSMADLKHSSLRYELRADLEEERMRQKIAERTSEETIRIYSLRLFLNCIVLAVLGACFYAIYVATVFSQEHMKKEIDKMVFGENLFILYLPSIVITLANFITPMIFAKIIRYEDYSPGFEIRLTILRCVFMRLATICVLVFTLGSKITSCDDDTCDLCGYNQKLYPCWETQVGQEMYKLMIFDFIIILAVTLFVDFPRKLLVTYCSSCKLIQCWGQQEFAIPDNVLGIVYGQTICWIGAFFSPLLPAIATLKFIIIFYVKEWSLLYTCRPSPRPFRASNSNFFFLLVLLIGLCLAIIPLTISISRIPSSKACGPFTNFNTTWEVIPKTVSTFPSSLQSFIHGVTSEAFAVPFFMIICLIMFYFIALAGAHKRVVIQLREQLSLESRDKCYLIQKLTEAQRDMRN | Function: Probable ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83502
Sequence Length: 723
Subcellular Location: Membrane
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