wanglab/gogpt-training-data huggingface dataset:
Protein: Acyl-CoA ligase sidI (EC 6.2.1.-) (Siderophore biosynthesis protein I) (Q4WR83)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Acyl-CoA ligase; part of the siderophore biosynthetic pathway. Aspergillus fumigatus produces 4 types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA. Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split. For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively. The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL. FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation. Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively. Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC. Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence.
Subcellular location: Peroxisome {ECO:0000269|PubMed:23617799}. Note=Targeted to peroxisomes via its PTS2-type peroxisomal targeting signal and the corresponding receptor pexG (PubMed:23617799). {ECO:0000269|PubMed:23617799}.
Interaction partners:
- Mevalonyl-coenzyme A hydratase sidH
- N
- Probable enoyl-CoA hydratase, mitochondrial
- Enoyl-CoA hydratase
- Enoyl-CoA hydratase/isomerase family protein
- Acyltransferase sidL
Sequence:
MATIRRLQQTLSHLRPPKAPQLLSIVEGPTQPELLDITLGELLTLQSLQYGDYECLVFPWTGARWTYTDLKDEADRVARGLLAMGIQKGDRIGIMAGNCEQYISVFFAAARVGAILVVLNNTYTPSELYYALGHTDCRLLFLTPRIGRHSLEEVLAKLGPRPKEQGTSSALEEIIILRGQYSGFSTYEHVIQRGLPLPSHALQDREAELHSTDVCNLQFTSGSTGNPKAAMLTHHNLVNNSRFIGDRMNLTSFDILCCPPPLFHCFGLVLGMLAVVTHGSKIIFPSETFDPTAVLHAISDEKCTALHGVPTMFEAILSLPKPPNFDCSNLRTGIIAGAPVPRPLMKRLLEELNMTEYTSSYGLTEASPTCFNALTTDSIERRLTTVGKVMPHAKAKIIDTQGHIVPIGQRGELCIAGYQLTKGYWNNPEKTAEALITDSDGVTWLKTGDEAIFDEEGYCSITGRFKDIIIRGGENIYPLEIEERLAAHPAIEVASVIGIPDQKYGEVVGAFLALAADVSARPSDEELRAWTRETLGRHKAPQYFFVFGEEGVDRTIPVTGSGKVRKVDLRKIAASVLERRLAKTAAIKEK
Protein: Zinc finger E-box-binding homeobox 2a (Zinc finger E-box-binding homeobox 2a isoform X1) (F1QY45)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKERSPCGLLPSDPLLSMKQEIMAEGPRCKRRKQANPRRKNVLSYENVVDAGSGSDDEDRLLGSEGEGSPAGVPSLEASPRVAHALLSCRGDEENESQDGAGAHVWRHGELNGSEERKAEYNSMSPDISLHGIGNGTVKGIDASSELESFFAKRKLDDGEGHAASIAEYLQDTVIIYPEDPEEGTRLGTPEANGQDENENDLALRTPDAFAQLLTCPYCDRGYKRLTSLKEHIKYRHEKNDESFPCPLCSDTFAYRTQLERHMATHKPARDQPQLLNEGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECSNCKKRFSHSGSYSSHISSKKCIGLISINGRVRHGVNNKPGSSPNSAASSPGSPALAQLRHKLENGRSMSLQDPSAHTDIKSEPMDFNEYRLMIASQQEYGASGAFLNGGGRGGSPPGMHSSSQNPLQHLGIGSDSHPLGYTGFINNMSEVQKVLQIVDNTVCRQKMDGNPEEISKLRAYMKELGSQMEEQNRVLASQQSFLGVGHNSPTKTIIDYTLEKVNEAKACLQSLTEDSKRRLMDIKKERPSHAMDLLSEDKALERDAQYAPFSCQYCKETFSGPIPLHQHERYLCKMNEEIKAVLKPNDTVPTGRRGLFGSEQQAGVISSSLERNATSPVNPYKDHMSLLNVYFSMNTEPNSEELRKISMAVGLPQEFVKDAFVQWKAQSHHSFSRKRSPPPERSGETNHVRDSAFARSPVSLGQYGDSTAEIQAITNGDSGHKLSRTHQITGTRQTNEKPLDSVDHLRGETPSPLNLSSSSSKHSHSSSYTPNSLTSEDAHGEPLDLSLPKQVSKAERRAKPNGFSIEHTSNSTAREPGTEPLNLAHIKKEFNGPNSLGNENQMDKSSSPIFSINPFGGGHMYTSLPPHGAFPPPTFMSTTQASIPGLRPYPGLDPMSFLPPMAYTYAAGAATFAEMQQRRKYQRKQGFQGDLLDSAGDYLSGLEDLTDSESLLARKKIKKTESGMYACDLCDKTFQKTSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAKQENHNNGGPLEPTELLMRRAYLQGLGPLGFSDPEDQAEDITRENTILRDGTESGARETEETYAEVTDRQETGLMGEEEMEGQRFDTRSPDGTAKDEKESEVTGGTEDESSEEGKRNHDGENEDAD
Protein: Delayed rectifier potassium channel Kv2 (Potassium voltage-gated channel subfamily B member 2) (Q98SV4)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}.
Interaction partners:
- 40S ribosomal protein S30
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein uL29
- 60S ribosomal protein L29
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL42
Sequence:
MADKVGLGVPKTSSRSSTSLPPEPIEIIRTKARTRRVRINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHELLMEVCDDYSLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEEQRREAETLRERDGEGEFDHSCCPDKRKKLWDLLEKPSSSVAAKILAIISILFIILSTIALSLNTLPELQVIDEFGQANDNPQLAHIEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPQTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVVVEKSEDKPSFDNHLSPSRWGIPKRASSDASLRPFDRKVGSRECFKSSSPQHLNVQKLEEMYNQMSKARSLSDLDKNQNASGPKLEAQNAKSGRQRNRPVSDVPHMASTDSFGSCTDELREASKLTPSSKDDDKRSVKNTTSLVESSNPVETPLDTFQISPEQRSQFDYAPSGHVTYNEDEECIVDDNTFLIQSINPGMRVNFLESTDDVPLTPPSTSSAQELSISLLEDDNSPEQESSTPFPESVILARIPEQGLILSPKLPVGDFHPNETLSLLEEHERESTEEDIAGTSIPSPKFTAQNCTQDGVGDNAEGKTESNQSGHIVDNHMFTPEIHLMPGDGDISQTSM
Protein: Type III secretion T3S chaperone (O84677)
Organism: Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
Interaction partners:
- Uncharacterized protein CT_671
- Low Calcium Response D
- Uncharacterized protein
- Uncharacterized protein
- Adenylate cyclase-like protein
- Type 3 secretion system ATPase
- Flagellar Motor Switch Domain/YscQ family
- Uncharacterized protein CT_665
- S/T Protein Kinase
- Uncharacterized protein CT_666
Sequence:
MVRYPLEPVLSIKKDRVDRAEKVVKEKRRLLELEQEKLRERESERDKVKNHYMQKIRQLREQLDDGTTSDAILKMKAYIKVVAIQLSEEEEKVNKQKENVLAASKELERAEVELTKRRKEEEKTRLHKEEWMKEALKEEARQEEKEQDEMGQLLHQLHKQKQRESGEN
Protein: Small GTP-binding rab protein, putative (Q57WL6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Rab GDP dissociation inhibitor
Sequence:
MRVEDPKSLDAVADAEESVKVEAPLEGRNTREEKDEQMFVFKIAVVGDYNVGKTSIVKRLLDIPYENISPLPQAENKQTRANGAEKGDDKSGNSANVSAEGANKYEAEVNSAQNGANTRTDCNDKADVALMTKNVLEPLPATTPTVGTDFFSRVVRSVRPGQHVRLQFWDTAGLERYASVHDSTFRRASALIVVFDVRNRESFAHVTSQHLKRAMQYNPDISGRHIFIVGNKVDLVDNSEPEDMDRFVTQSELQSGLFSAFPDVHYYETSAQTNYGVWEVLHGLCQSLPDNYAATTSGEAKEEKAAVTERDPLHSLLPLCYEPETTLDEGTVAEDPALTADGTLASLSSPSSIKSRDVRKDTKASEDELFSPRECADEDDVCHGGADAADNLKSARGRGSNGTVATVMADPIDGDGIDVDVDVDVEGEDEDVIADAAAEPECTVNSSKHVDPNKSSPVKEEGEEDAVAVHSERSAPGDGVVDKKVKCNGSDGEVETEDATDVECFPQEDNAAPPSVQNTARFGGNSLQARASSFANGGDGVLSCSRAARGKSGEDSKADENPQVTSHRKRIDDMLKRIDEDAGVEDFSEGGRRVEQMQEEASDQRKKEKSPVKLSRCFCFGSKGGGSKRSGC
Protein: Transmembrane protein (Q8VZT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 beta subcomplex subunit 2
Sequence:
MGGGDHGHGAEGGDFRAKVWSMTGGPNCRPKHWRRNTAIAMFGVFLVCIPIAKLSAKLEQRPHMPVRPIPSQIWCKNFGTKDDYEKEH
Protein: ATP-sensitive inward rectifier potassium channel 8 (Inward rectifier K(+) channel Kir6.1) (Potassium channel, inwardly rectifying subfamily J member 8) (uKATP-1) (Q63664)
Organism: Rattus norvegicus (Rat)
Function: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-binding cassette sub-family C member 9
- ATP-binding cassette sub-family C member 8
- ATP-sensitive inward rectifier potassium channel 11
- Protein kinase C epsilon type
Sequence:
MLARKSIIPEEYVLARIAAENLRKPRIRDRLPKARFIAKSGACNLAHKNIREQGRFLQDIFTTLVDLKWRHTLVIFTMSFLCSWLLFAIMWWLVAFAHGDIYAYMEKGITEKSGLESAVCVTNVRSFTSAFLFSIEVQVTIGFGGRMMTEECPLAITVLILQNIVGLIINAVMLGCIFMKTAQAHRRAETLIFSRHAVIAVRNGKLCFMFRVGDLRKSMIISASVRIQVVKKTTTPEGEVVPIHQQDIPVDNPIESNNIFLVAPLIICHVIDKRSPLYDISATDLVNQDLEVIVILEGVVETTGITTQARTSYIAEEIQWGHRFVSIVTEEEGVYSVDYSKFGNTVRVAAPRCSARELDEKPSILIQTLQKSELSHQNSLRKRNSMRRNNSMRRSNSIRRNNSSLMVPKVQFMTPEGNQCPSES
Protein: Phosducin-like protein 3 (Q4KLJ8)
Organism: Rattus norvegicus (Rat)
Function: Acts as a chaperone for the angiogenic VEGF receptor KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination and degradation (By similarity). Inhibits the folding activity of the chaperonin-containing T-complex (CCT) which leads to inhibition of cytoskeletal actin folding (By similarity). Acts as a chaperone during heat shock alongside HSP90 and HSP40/70 chaperone complexes. Modulates the activation of caspases during apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
Interaction partners:
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit zeta
- Chaperonin containing TCP1 subunit 6B)
Sequence:
MQDPNADTEWNDILRKKGILPPKESLKELEEEEEGKEEQRLQQSVVKTYEDMTLEELQENEDEFSEEDERAIEMYRQQRLAEWKATQLRNKFGEVLEISGKDYVQEVTKAGEGLWVVLHLYKQGIPLCSLINHHLSGLARKFPDVKFIKAISTTCIPNYPDRNLPTVFVYREGDIKAQFIGPLVFGGMNLTIDELEWKLSESGAIKTELEENPKKAIKDVLLSSVRDPVPMRRDSDSEDD
Protein: Nuclear receptor corepressor 1 (J3KS51)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSSGYPPNQGAFSTEQSRYPPHSVQYTFPNTRHQQEFAVPDYRSSHLEVSQASQLLQQQQQQQLRRRPSLLSEFHPGSDRPQERRTSYEPFHPGPSPVDHDSLESKRPRLEQVSDSHFQRVSAAVLPLVHPLPEGLRASADAKKDPAFGGKHEAPSSPISGQPCGDDQNASPSKLSKEELIQSMDRVDREIAKVEQQILKLKKKQQQLEEEAAKPPEPEKPVSPPPVEQKHRSIVQIIYDENRKKAEEAHKIFEGLGPKVELPLYNQPSDTKVYHENIKTGVPARRMMKNQVMRKKLILFFKRRNHARKQREQKICQRYDQLMEAWEKKVDRIENNPRRKAKESKTREYYEKQFPEIRKQREQQERFQRVGQRGAGLSATIARSEHEISEIIDGLSEQENNEKQMRQLSVIPPMMFDAEQRRVKFINMNGLMEDPMKVYKDRQFMNVWTDHEKEIFKDKFIQHPKNFGLIASYLERKSVPDCVLYYYLTKKNENYKALVRRNYGKRRGRNQQQIARPSQEEKVEEKEEDKAEKTEKKEEEKKDEE
Protein: Mitochondrial distribution and morphology protein 34 (Mitochondrial outer membrane protein MMM2) (P53083)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10 (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03105, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14981098, ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19556461}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03105, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14981098, ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19556461}. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03105}.
Interaction partners:
- Mitochondrial distribution and morphology protein 12
- Mitochondrial distribution and morphology protein 10
- Maintenance of mitochondrial morphology protein 1
- Mitochondrial Rho GTPase 1
- Peroxisomal membrane protein PMP27
- Dynamin-related protein DNM1
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM40
- Mitochondrial import receptor subunit TOM7
- Sorting assembly machinery 50 kDa subunit
Sequence:
MSFRFNEAVFGDNSFNERIREKLSTALNSPSKKKLDILKSGIKVQKVDFPTIPQLEILDLDIITQPKSLAKGICKISCKDAMLRIQTVIESNLLLINEQDTPSFTMPQLINNGSFTIPITMTFSSIELEAITNIFVKNPGIGISFNDVDLDFKFDCSVKILQSTIERRLKESMHVVFKDVLPSLIFNTSQNWFTNRGESTSTIPGKREHHHQQTTMSRNVILDGSDFQELSPINMLRLSSIVSSRSTLSLHSTVMNSLSAIPGCLERQNLYRFISRMPSLNNYYSSQSFPQPKSSTVSSKQLVKPFYCSHNLLPKTVLDSSQYDLATITKIQSRLFDRSNSNDDNAKPRRRKIKCKKTRTPSNLQSQGEQAVDDSTAIETVTSTPVQTPIPELEEQSPPYLKTTVSIRDKYVIPEKISLNLDSKKDTSKKKPFYFIGLNSQEPSNNWKWGMEDSPPPYH
Protein: ATP-dependent RNA helicase DDX50 (EC 3.6.4.13) (DEAD box protein 50) (Gu-beta) (Nucleolar protein Gu2) (Q9BQ39)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12027455, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:38773330}. Cytoplasm {ECO:0000269|PubMed:28181036, ECO:0000269|PubMed:35215908}. Note=Accumulates in the cytoplasm to activate signaling upstream of IRF3 during viral infection. {ECO:0000269|PubMed:35215908}.
Interaction partners:
- Armadillo repeat-containing protein 8
- ATP-dependent RNA helicase DDX54
- Pescadillo homolog
- ATP-dependent RNA helicase DDX18
- Probable ATP-dependent RNA helicase DDX56
- Interferon-inducible double-stranded RNA-dependent protein kinase activator A
Sequence:
MPGKLLWGDIMELEAPLEESESQKKERQKSDRRKSRHHYDSDEKSETRENGVTDDLDAPKAKKSKMKEKLNGDTEEGFNRLSDEFSKSHKSRRKDLPNGDIDEYEKKSKRVSSLDTSTHKSSDNKLEETLTREQKEGAFSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKTDSEDNPQTLLFSATCPQWVYKVAKKYMKSRYEQVDLVGKMTQKAATTVEHLAIQCHWSQRPAVIGDVLQVYSGSEGRAIIFCETKKNVTEMAMNPHIKQNAQCLHGDIAQSQREITLKGFREGSFKVLVATNVAARGLDIPEVDLVIQSSPPQDVESYIHRSGRTGRAGRTGICICFYQPRERGQLRYVEQKAGITFKRVGVPSTMDLVKSKSMDAIRSLASVSYAAVDFFRPSAQRLIEEKGAVDALAAALAHISGASSFEPRSLITSDKGFVTMTLESLEEIQDVSCAWKELNRKLSSNAVSQITRMCLLKGNMGVCFDVPTTESERLQAEWHDSDWILSVPAKLPEIEEYYDGNTSSNSRQRSGWSSGRSGRSGRSGGRSGGRSGRQSRQGSRSGSRQDGRRRSGNRNRSRSGGHKRSFD
Protein: Predicted GPI-anchored protein 45 (Q5AA33)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Secreted, cell wall {ECO:0000269|PubMed:18712765}.
Interaction partners:
Sequence:
MQFLFTFIFLLIPLVYSLPAASPKSGTDFDFNQEIETFVEQAFNQDDPSQAAAAAASFEEFLVNVFNYDQADGQVDGQVLKVFEKRDANTEQTIEGILKAVNNSGVIWTLLDSVADDPSRIEYIGNLTSSFLKNYNITLNIADLLSESSSLTENLNITGLLSAVENSGLITSLLDGILLDENFRPRLVDLIDRLVLSQKNVLLYIFAGVLSKRDLMADGELVNVLLKRATSNDDSYSGSLGSFLNNAASTVLSSSLVSNAVADVLNALNDTGFLVYATKRFLSSDSYINMTVALVNDIVSSSSVTIDTSGLNITELISGTLGNPKEIAALVGSLLSGDSSQTSQLSNYLGRYSGALSQILQDLEKKGLFAELNSYIFGDSTTKASATATATATATSSANGKNVANNNNKDAATSGSATSNSSTSTNTKSASNGAGAVIYTGSNTQTTFLKALTILFGGALLFL
Protein: Ras-related protein Rab-1A (EC 3.6.5.2) (P62822)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Required to modulate the compacted morphology of the Golgi. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria (By similarity). Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:P62820}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P62820}. Early endosome {ECO:0000250|UniProtKB:P62820}. Cytoplasm, cytosol {ECO:0000269|PubMed:1429835}. Membrane {ECO:0000269|PubMed:1429835}. Melanosome {ECO:0000250|UniProtKB:P62821}. Note=Alternates between membrane-associated and cytosolic forms. {ECO:0000269|PubMed:1429835}.
Interaction partners:
- Chromosome 11 C9orf72 homolog.
- RAB1B, member RAS oncogene family.
- USO1 vesicle transport factor.
- TBC1 domain family member 20.
- Trafficking protein particle complex subunit
- Trafficking protein particle complex 8.
- Syntaxin 5
- Trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit
- Golgi brefeldin A resistant guanine nucleotide exchange factor 1.
Sequence:
MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC
Protein: Transmembrane emp24 domain-containing protein 2 (COPI-coated vesicle membrane protein p24) (Membrane protein p24A) (Sid 394) (p24 family protein beta-1) (p24beta1) (Q9R0Q3)
Organism: Mus musculus (Mouse)
Function: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing (By similarity). Required for morphogenesis of embryo and placenta.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q15363}; Single-pass type I membrane protein {ECO:0000255}. Note=Cycles between compartments of the early secretatory pathway. {ECO:0000250|UniProtKB:Q15363}.
Interaction partners:
- Transmembrane emp24 domain-containing protein 10
- Transmembrane emp24 domain-containing protein 9
- Transmembrane emp24 domain-containing protein 7
- Transmembrane emp24 domain-containing protein 3
- Transmembrane emp24 domain-containing protein 4
- Transmembrane emp24 domain-containing protein 11
- Surfeit locus protein 4
- Syntaxin-5
- Protein SEC13 homolog
- Protein transport protein Sec23A
Sequence:
MVTLAELLALLAALLATASGYFVSIDAHAEECFFERVTSGTKMGLIFEVAEGGFLDIDVEITGPDNKGIYKGDRESSGKYTFAAHMDGTYKFCFSNRMSTMTPKIVMFTIDIGEAPKGQDMETEAHQNKLEEMINELAVAMTAVKHEQEYMEVRERIHRAINDNTNSRVVLWSFFEALVLVAMTLGQIYYLKRFFEVRRVV
Protein: Lipid droplet organization protein LDO16 (Lipid droplet organization 16 KDa protein) (Outer spore wall protein 5) (P40219)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in spore wall assembly.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:29187528}; Multi-pass membrane protein. Lipid droplet {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21748599, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:26572621, ECO:0000305|PubMed:29187528}. Note=Contains a predicted membrane hairpin, a motif allowing association with both ER bilayers and LD monolayers. {ECO:0000305|PubMed:29187528}.
Interaction partners:
- Lipid droplet organization protein LDO45
- Protein LDB16
- Seipin
- Protein PET10
- Outer spore wall protein 2
- Outer spore wall protein 1
- Outer spore wall protein 4
Sequence:
MVSTATFFFFVYLTLFVVIGFFSSLFIIPLLGISFVFAIGVVSFGFCSNMSFKMAQLIYVRADAFLKKVLDKMALQTQPAQLQEPQEPLSTLRPVSNPTIPSPLRQTARPSKFVTEEDVIFEPVSAQSAIARSLETTANKAGNKFQLS
Protein: Testin (Q2LAP6)
Organism: Rattus norvegicus (Rat)
Function: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Note=Detected along actin stress fibers. {ECO:0000250}.
Interaction partners:
Sequence:
MDLETKMKKMGLGHEQGFGAPCLKCKENCEGFELHFWRKICRNCKCGQEEHDVLLSTEEDRKVGRLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPKEVKEMEQFVKKYKSEALGVGDVKLPSEMNAQGDKVHNPAGDRNTPAAVGSKDKSAEAKKTQYSCYCCKNTMREGDPAIYAERAGYDKLWHPACFICSTCGELLVDMIYFWKNGKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDNILAGKIYVMVRDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKMMS