wanglab/gogpt-training-data huggingface dataset:
Protein: Mitochondrial distribution and morphology protein 34 (Q9UUC9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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.
Subcellular location: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03105}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03105}. 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
- Dynamin-related protein dnm1
- Probable mitochondrial import receptor subunit tom70
- Peroxisomal biogenesis factor 11
- Mitochondrial import receptor subunit tom7
- Mitochondrial import receptor subunit tom20
- Probable mitochondrial import receptor subunit tom40
Sequence:
MSFRVKGWSDQFSESFYERATTLLTAALNKGTKHSMIADHITVKELDLGPQPPQLEILEVGDLAPDRFQGLFNLHYSGDASLVLQTKIRANPLSVQKSNVPSFSSRNTMLASRAPLTVPMFLRLSDLKLNGIVVLVFSKQKGITVVFRNDPLESVRVSSSFDSIPAIARFLQREIEVQLVSLFQEELPSIIYKMSRIWFAKSDSNLSFQKIPFTSPNQSHTSLANYNPDLLDGPPDYHESTKVDTHLPIKMGPLDVQTHPNIRSIASLALSRKALLPISSPSIPMSIYRSTPPDTIIQQLTTQSDDISAVSSPATQYSASDYLGSNDTTARPSIFGRSHGTSQFRRRERVKKRHVIKIHEASNKSASSSETFVGSKNVDLTESAFDSIPDTPTKIITNINKLKRNYTITNNWLENLQQKIPSEVDNGKVSGLQYSAFKLLMLQRLMAAKGSF
Protein: At4g22860 (Cell cycle regulated microtubule associated protein) (Q4V3C5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Flowering time control protein FY
- Cleavage stimulation factor subunit 77
- TPX2
- Cleavage stimulating factor 64
- Similarity to unknown protein protein family)
- SNARE associated Golgi protein family
- TPX2
- Subtilisin-like protease SBT2.3
- Glycine-rich protein
- FIP1[III]-like protein
Sequence:
MEMDEDMEIEPMVFEVKEIDLEYEFDAARWYDFTREELPEESQAAEFWFHSAPSYAPSPFVTKLLLREEVYDDKTEASTRSEDEEVVADVCDKYKGTFQQPNHLATDFNKTGSRMRSGIFSSQQQQGCNLKKVPNQPIWKGPTVSNHKHTDKPKFRAKSSIRPTPRSSTLMRPTASQLAKQNNASKFHMQVDQSHDKGSCGTSGTEVQASKRQKLDGGLLRKVADTKQEMSFVHKIPKKDTTLDKNAQHARTKITIPQEPDFATSQRAHRIRHKNDAKLEQEQPAVYRFKARPFNRKIFDAPSLPIRKKSTPKLPEFQEFHLKTSERAMQHSSAVTTRSHAYKESDKSIITDMLDGDNRESRRPSGMDISKHDVSEGSHVFKARPLNKKILSSRGDMGIFKNSKRETTVPLEFSFHSEKRVQPDLPTDLFSKLSIKSEIQPNDGSRTRLFQPKVSKENRINSFQARNEVTRMAAAKPVSSAGQQMQFGNSGITPETNQQWTARRNLGIR
Protein: Tripeptidyl-peptidase sed1 (EC 3.4.14.10) (Sedolisin-A) (Q70DX9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
Subcellular location: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
Sequence:
MRLSHVLLGTAAAAGVLASPTPNDYVVHERRAVLPRSWTEEKRLDKASILPMRIGLTQSNLDRGHDLLMEISDPRSSRYGQHLSVEEVHSLFAPSQETVDRVRAWLESEGIAGDRISQSSNEQFLQFDASAAEVERLLGTEYYLYTHQGSGKSHIACREYHVPHSLQRHIDYITPGIKLLEVEGVKKARSIEKRSFRSPLPPILERLTLPLSELLGNTLLCDVAITPLCISALYNITRGSKATKGNELGIFEDLGDVYSQEDLNLFFSTFAQQIPQGTHPILKAVDGAQAPTSVTNAGPESDLDFQISYPIIWPQNSILFQTDDPNYTANYNFSGFLNTFLDAIDGSYCSEISPLDPPYPNPADGGYKGQLQCGVYQPPKVLSISYGGAEADLPIAYQRRQCAEWMKLGLQGVSVVVASGDSGVEGRNGDPTPTECLGTEGKVFAPDFPATCPYLTTVGGTYLPLGADPRKDEEVAVTSFPSGGGFSNIYERADYQQQAVEDYFSRADPGYPFYESVDNSSFAENGGIYNRIGRAYPDVAAIADNVVIFNKGMPTLIGGTSAAAPVFAAILTRINEERLAVGKSTVGFVNPVLYAHPEVFNDITQGSNPGCGMQGFSAATGWDPVTGLGTPNYPALLDLFMSLP
Protein: Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (Phosphotyrosyl phosphatase activator) (PTPA) (Q9VQQ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000255|RuleBase:RU361210, ECO:0000269|PubMed:26586222}. Nucleus {ECO:0000269|PubMed:26586222}. Note=Enriched in nuclei during interphase and dispersed evenly throughout the cytoplasm after breakdown of the nuclear envelope in mitosis. {ECO:0000269|PubMed:26586222}.
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase PP2A
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Serine/threonine-protein phosphatase
- Uncharacterized protein, isoform B
- LD07294p
- Serine/threonine-protein phosphatase 2B catalytic subunit 2
- Serine/threonine-protein phosphatase 2B catalytic subunit 3
Sequence:
MASGINQAAGKLPAIAKKVQNLGDMGVWQKSRAFHDLIGYINGTSSAIQGIKTTDEIFESEMLKKLLRLFDALEKLVEQNPPLEQPQRFGNKAYRDWAQAMRELLPELLEQLLPDDKKRYQVELGQYLTESFGNATRIDYGTGHELSFLFFLCSLFKAEILQERDIVSAALRLFNRYLELARQLQRTYNMEPAGSQGVWSLDDFQFVPFIWGSAQLAVKSPFDPSKFVDEAIITEYKDHFMFISCIDYICKVKTGHFGEHSNQLWSITDVPTWAKINAGLVKMYQKEILSKFPVIQHVYFGELMTFEPVSSGTTLSNARLGHVAPPPSKRICIGTPNLVPPVPVATAPPPPAESLSIEQNVGDSSSESSDNSVVLRPSTSSSSLVAAAEGSGDKPSKE
Protein: Vacuolar ATPase assembly integral membrane protein VMA21 (Myopathy with excessive autophagy protein) (Q3ZAQ7)
Organism: Homo sapiens (Human)
Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:23315026}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:23315026}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000255|HAMAP-Rule:MF_03058, ECO:0000269|PubMed:19379691, ECO:0000269|PubMed:23315026}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03058}.
Interaction partners:
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit d 1
- V-type proton ATPase 116 kDa subunit a 2
- V-type proton ATPase 21 kDa proteolipid subunit c''
- Renin receptor
- Vacuolar ATPase assembly protein VMA12
- Emerin
- V-type proton ATPase 116 kDa subunit a 4
- V-type proton ATPase 116 kDa subunit a 3
Sequence:
MERPDKAALNALQPPEFRNESSLASTLKTLLFFTALMITVPIGLYFTTKSYIFEGALGMSNRDSYFYAAIVAVVAVHVVLALFVYVAWNEGSRQWREGKQD
Protein: Cx9C motif-containing protein 4 (Mature T-cell proliferation 1 neighbor protein) (Mature T-cell proliferation-1 type A) (MTCP-1 type A) (Protein p8 MTCP-1) (p8MTCP1) (P56277)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:7784073}.
Interaction partners:
- COX assembly mitochondrial protein 2 homolog
- Cytochrome c oxidase assembly factor 4 homolog, mitochondrial
Sequence:
MPQKDPCQKQACEIQKCLQANSYMESKCQAVIQELRKCCAQYPKGRSVVCSGFEKEEEENLTRKSASK
Protein: Dynein axonemal assembly factor 11 (DNAAF11) (Leucine-rich repeat-containing protein 6) (Leucine-rich testis-specific protein) (Protein tilB homolog) (Testis-specific leucine-rich repeat protein) (O88978)
Organism: Mus musculus (Mouse)
Function: Involved in dynein arm assembly, is important for expression and transporting outer dynein arm (ODA) proteins from the cytoplasm to the cilia. Acts as a crucial component in the formation and motility of spermatozoal flagella (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10775177, ECO:0000269|PubMed:27353389}. Cell projection, cilium {ECO:0000250|UniProtKB:Q86X45}. Dynein axonemal particle {ECO:0000305|PubMed:27353389}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q86X45}.
Interaction partners:
- Zinc finger MYND domain-containing protein 10
- Dynein axonemal assembly factor 6
- Dynein axonemal assembly factor 5
- Dynein axonemal assembly factor 19
- Dynein axonemal assembly factor 3
- Dynein axonemal intermediate chain 1
- Sperm-associated antigen 1
- Coiled-coil domain-containing protein 39
- Dynein axonemal assembly factor 4
- Dynein axonemal intermediate chain 2
Sequence:
MGRITEDLIRRNAEHNDCVIFSLEELSLHQQEIERLEHIDKWCRDLKILYLQNNLIGKIENVSKLKKLEYLNLALNNIERIENLEGCEWLTKLDLTVNFIGELSSVKTLTHNIHLKELFLMGNPCADFDGYRQFVVVTLQQLKWLDGKEIERSERIQALQNYTSVEQQIREQEKAYCLRRAKEKEEAQRKLEEENESEDKKKSSTGFDGHWYTDIHTACPSATENQDYPQVPETQEEQHNTKESDDIEDDLAFWNKPSLFTPESRLETLRHMEKQRKAQDKLSEKKKKAKPPRTLITEDGKVLNVNEAKLDFSLKDDEKHNQIILDLAVYRYMDTSLIEVDVQPTYVRVMVKGKPFQLALSTEVQPDRSSAKRSQTTGHLLICMPKVGEMITGGQRTPTSVKTTSTSSREQTNPRKKQIERLEVDPSKHSCPDVSTIVQEKRHRPKRMESQPRDEPSEEDPDFEDNPEVPPLI
Protein: Uncharacterized protein (Q386K6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MECKTNLAGGLRNDERSNGSKDALFSPLNAMRKLQEALRSADVFELEEAILVAERSVNTVSVPRQMAVSLRTLLEHSRDTLNNHLQAREPHLKPRQQVHRDGSSKKALVVLEQTAAGFPEQPCRMETDVGLSEVLHSDVMRDMKNDVAPLETDHWEESGSSLASRSSAEAGAYDSLSVSMWSKKGVRTQPRICTTVVGSATVERAGAACRSHGKIVDLNSPFNDLAEGEDVMRSAVEQEEYTNRVRYFEYALAEQAKLLARAEEFAWSSEQGDEGNTVDAHLSHCSSFTSLYFSSDSGEWDVVAASGVASPEIIPLSTNVLRGLRSDGVGPSRLRASSTPSSPFSSESSDIGMVFR
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase (Q5A6L6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase
- Phosphatidylinositol N-acetylglucosaminyltransferase
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Phosphatidylinositol N-acetylglucosaminyltransferase
- N-acetylglucosaminylphosphatidylinositol deacetylase
- GPI mannosyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Ras-like protein 1
Sequence:
MEEIHISSSILQDSDSAPPNHFQHAQQQEQPSWKKLLYLQQPFPDNYTDQSFLSQLKRNTTVAKYSYKNLVQAFSFIVFYISCILLVILMFIGIYEKQWDPIIPTLISTGISLVGFFSLKNLSMNMRSLMVITFILLIVSPILKSLTKSTSSDSIWAISCVLCLANSIFHDYSMKVSYRPIVSTNISLSNAIVLASRLSTTLDVFLFVLFAIEVNILLPLFDAKIRLSGLETIHWPIAFLTFNLTSYLMYILLNYKFLVYWILSVFVMVVIMPIYFLSLQRYKNEIQGPWDVAKPKLMKSSIQS
Protein: Serine/threonine-protein kinase 17B (EC 2.7.11.1) (DAP kinase-related apoptosis-inducing protein kinase 2) (O94768)
Organism: Homo sapiens (Human)
Function: Phosphorylates myosin light chains (By similarity). Acts as a positive regulator of apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:9786912}. Cell membrane {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Colocalizes with STK17B at the plasma membrane. {ECO:0000250}.
Interaction partners:
- Kalirin
Sequence:
MSRRRFDCRSISGLLTTTPQIPIKMENFNNFYILTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSCPRVINLHEVYENTSEIILILEYAAGGEIFSLCLPELAEMVSENDVIRLIKQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGIIAYMLLTHTSPFVGEDNQETYLNISQVNVDYSEETFSSVSQLATDFIQSLLVKNPEKRPTAEICLSHSWLQQWDFENLFHPEETSSSSQTQDHSVRSSEDKTSKSSCNGTCGDREDKENIPEDSSMVSKRFRFDDSLPNPHELVSDLLC
Protein: DPY30 domain-containing protein 1 (Q8WWB3)
Organism: Homo sapiens (Human)
Function: Plays a crucial role during acrosome biogenesis.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9D9T0}.
Interaction partners:
- Nucleoside diphosphate kinase homolog 5
- Protein dpy-30 homolog
- DPY30 domain-containing protein 2
Sequence:
MESIYLQKHLGACLTQGLAEVARVRPVDPIEYLALWIYKYKENVTMEQLRQKEMAKLERERELALMEQEMMERLKAEELLLQQQQLALQLELEMQEKERQRIQELQRAQEQLGKEMRMNMENLVRNEDILHSEEATLDSGKTLAEISDRYGAPNLSRVEELDEPMFSDIALNIDQDL
Protein: Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Initiation factor 2-associated 67 kDa glycoprotein) (Peptidase M) (p67) (p67eIF2) (A0A140VJE3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03175}. Note=About 30% of expressed METAP2 associates with polysomes. {ECO:0000256|HAMAP-Rule:MF_03175}.
Interaction partners:
Sequence:
MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKESGASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY
Protein: Lissencephaly-1 homolog (DdLIS1) (Q8I0F4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the coupling of the nucleus and centrosome and dynein/dynactin-mediated interactions of microtubule tips with the cell cortex.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:15800059}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:15800059}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:15800059}. Note=Localizes to microtubules and to the centrosome throughout the entire cell cycle. Is part of the centrosomal corona.
Interaction partners:
- Membrane bound O-acyl transferase family protein
- Microtubule-associated protein RP/EB family member 1
- Dynein heavy chain, cytoplasmic
- Lis-interacting protein
Sequence:
MVLTSKQKEELNGSILDYFESSQYKSSFEEFKKETGTELDVKKKGLLEKKWTSVIRLQKKVLDLEAKVAQLEEELNSGGGRGGGRGRGKEDALPRPPEKHILTGHRNCINSVKFHPSFSLMVSASEDATIKVWDFESGEFERTLKGHTNAVQDIDFDKTGNLLASCSADLTIKLWDFQTYDCVKTLHGHDHNVSCVRFTPSGDQLISSSRDKTIKVWEAATGYCIKTLVGHEDWVRKITVSEDGSCIASCSNDQTIKTWNIVKGECLATYREHSHVVECLAFSTANIIDIPGSLLSTPEGKSKVKQGPGGNLVGQCGYLATGSRDKTIKIWELATGRCLATYIGHDNWVRAVRFHPCGKFLLSVGDDKTIRVWDIAQGRCIKTINEAHTHFISCLDFCLHNPHIATGGVDDVIKVWKLQ
Protein: Mitochondrial intermediate peptidase (MIP) (EC 3.4.24.59) (Octapeptidyl aminopeptidase) (Q10415)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Intermediate cleaving peptidase 55
- Mitochondrial inner membrane protease atp23
- Probable mitochondrial-processing peptidase subunit alpha
- ATPase synthesis protein 25
- UBA domain-containing protein Mud1
- Lon protease homolog, mitochondrial
- Putative zinc metalloproteinase C607.06c
- Probable mitochondrial-processing peptidase subunit beta
Sequence:
MQVRTLLTLGKKKVIGNRQCILSLYRKYSNVQSRKAEDQLLRQIFDDQNIAVNQITKRNGIQGVGLFRNHFLSDKDTGFLRLAETASEKCKAVIEDLLLEDTEDGSIVVSKFDRISNLLCSVIDLFEFVRCAHPDKMVVMKAEEAYSYLFELMNTLNTHQGLYEKLKCSLQQTPTLKDTDPEAYTVGRVFLQDFEKSGVNLESSKRNSFVKKSSESATLGRAFFNNSMNRPQRYLTISKQRLAGSDPYFVRSLSKNDKNFIMIPTVGYEGTQALISVANPDVRKEIYMEGHKGTVEEVELLNSYLRSKAEVAKLVGKSSFADLQLIDKMANAPKHVVEFLENLSLKNSSVLKKILNNLALMKKKELNLNFLPSFDVWDREYYTARYKQSLINQKPSLNPSITNYRRFFSVGTVIQGLSRLFSSLYGLRFVPADISPGEVWHPDVNKVNVYNENDHVMGVIYFDLFARTGKTDGAAHFTIRSSRELDLTSFDDSISLGFDDATNIRVKDNKRYQIPVISLLCNFVRSSGMDPTFLDLWDVKTLFHEMGHAMHSILGHTKYQNLAGTRCATDFVELPSIIMEFFMSNPAVLPLYARYEGTEIPLPVQVLNHHNMVENSSAPLDLQSQICMAMVDQLFHSKVVLDPSFNSIDEVTNVTRKFSGFESAPPAAWYLQFSHLYGYSATYYSYIFDTVLASLIFSKLFAGNPLSREAGEKFRKAILRWGGSRSPWECVAEALEQPILATGGEEAMRRIGSEGIKATSTF
Protein: Rubredoxin (Rd) (EC 1.-.-.-) (Q9AL94)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Function: Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Functions as an intermediate component in the electron transfer chain: NADH->NROR->Rd->FprA1/2 in which Rd serves as the proximal electron donor to the FDPs that exhibit H(2)O-forming NADH oxidase activity. Also functions as the proximal electron donor to the Dfx and revRbr proteins that display superoxide reductase (SOR) and NADH peroxidase activity, respectively. Therefore, is a key electron carrier in an efficient multienzyme complex that can scavenge O(2) and reactive oxygen species (ROS), and thus plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium.
Interaction partners:
- NADH-rubredoxin oxidoreductase
- Desulfoferrodoxin
- Glutaredoxin
- BFD-like [2Fe-2S]-binding domain-containing protein
- Flavo-diiron protein FprA2
- Flavo-diiron protein FprA1
- Rubrerythrin-1
- Rubrerythrin-2
- Reverse rubrerythrin-1
- Reverse rubrerythrin-2
Sequence:
MKKYVCVVCGYIYDPAEGDPDNGVNPGTSFEDIPDDWVCPLCGVGKDQFEPSEE
Protein: Kazal-like domain-containing protein (Q9VYH8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- Mucin 4B, isoform B
- MIP13722p
- Uncharacterized protein
- HDC17346
- GEO10309p1
- Uncharacterized protein, isoform B
- Mucin related 11Da
- Femcoat
- Mucin 12Ea
Sequence:
MTAFLVSIGFALLAGARAWDYGVPYYPAPHYFEQQQPYDLPCPPSGPESLVCAGAPGAQPSTFPSPCEVQRFRALTGINWEIIHENRCETLEVCPDNCQDQYNPVCGKYKDTRRNFRSECELQLVKCRTGHPWRKQHDGPCESRYPVPQSPRVQNYNPYAINPYQPNVGSRGAYGSQGPYGSQGPYGSQGPYGPQSPPQPYPSSSFVSPRPNYEAPIYQPYQISWENLPTEYAGTSKPYPNPTYETTPTTTSTTASTTTSTTTSTTTTTTTPKTTTDKITTTPQPGDSETTEASTVTPNPRRNIKVNAVIEDTPKPSTTTGQPEESTESSSTESSVTTTPLKKYITTASPQHATTTARPSKPSLSINAVQVPEQEAEKTTSTEPTTTYKSFNSYNSYASYTTTEAPVTEDTTKVPVDEIIKINKVQISAENTTEKADETTQSTTRKPKPTYPSYPIYPTSSVYKTYPVYNSTAAPTNENTTQLPFDKVVKINAVEESTEKIDEETTKANGYETYPVYGSTEASKDTETTKKSLDKVVKINAVEESTEKVDETHTTYPSYATYPSSSVYQTYPDYKSSVTPKNDVTTQAPLEKIVKVNAIEEINEKQDEQTTETATVSESTTSKSQPTYPSYPTYPSTNVYQTYPVYGSTEASKDDETTKKSLDKVVKINAVEKEDETTQKAEPTYSSYPTYSASSVYKTYPTYASTEAPKNDETTKMALDKLVKINKAQISTEKAVNETTTTTEPITTKAPTTYPSYQTYTSSSVYKSYSSSETPDDEEDEESTANPLNKSIKINAVSDPETIQNTTFATTPFPETTKGSFHGVEKGPEIDADSVAKSAKTESAEIPEIVKTESVSKNGTQLNLEVTCKRENKKLKLDTLSSDRSNIYFIFLGC
Protein: Cytochrome P450 monooxygenase gliF (EC 1.-.-.-) (Gliotoxin biosynthesis protein F) (Q4WMJ0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. Gliotoxin contributes to pathogenesis during invasive aspergillosis. In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- O-methyltransferase gliM
- N-methyltransferase gliN
- Thioredoxin reductase gliT
- Glutathione S-transferase gliG
- Nonribosomal peptide synthetase gliP
Sequence:
MDQVYLPQSVRTAVAVSFGVGLLYWVYRLLLQKTKSLKALDLPVLQSVGDQDIVKTLEEGHAKYPDTPFALGVPGQQLVVLPVSEIDTVKALPENQLSIKKHHYNQFLGEYSYMGTKADEFDDAMRYLLVRNTPAVLASFTAEIDYAMSTVLQVPPNSWTRVKPRSIMPKVATILSGRAFVGLPLSREPDWIESNVNYTQDVSRAWMVLRFYPHWIRPLVAPFLREVKTLEQNKALIGRKIAKLLADQEAQKLSPAQEKIPGGDMIDWFKSRYQAQGKTATAQQLTRDQLLATFASIYNLSNALTYVMFDLAANPAAVDELREELDQVLGPNVGAESIDKTALPRLIKLDSFVRESQRLSPTSLVNIPRIVTDPNGLRLKTGHVIPPGYLVMVRAQPINQSPTLYPNPERFDAFRFARLRQQGGANENRWQHTSTGADNINFGHGIWACPGRFFASAEIKVVVAYVIRHYDLRLIEGRPHPKPKYGGLAIFPDAGAEVELKPRV
Protein: Cytoglobin-2 (Nitric oxygen dioxygenase CYGB) (EC 1.14.12.-) (Nitrite reductase CYGB) (EC 1.7.-.-) (Pseudoperoxidase CYGB) (EC 1.11.1.-) (Superoxide dismutase CYGB) (EC 1.15.1.1) (Q575S8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8WWM9}. Nucleus {ECO:0000250|UniProtKB:Q8WWM9}.
Interaction partners:
- Myoglobin
- Androglobin
Sequence:
MEKEREDEETEGRERPEPLTDVERGIIKDTWARVYASCEDVGVTILIRFFVNFPSAKQYFSQFQDMEDPEEMEKSSQLRKHARRVMNAINTVVENLHDPEKVSSVLVLVGKAHAFKYKVEPIYFKILSGVILEILAEEFGECFTPEVQTSWSKLMAALYWHITGAYTEVGWVKLSSSAV
Protein: Transmembrane protein 132D (Mature oligodendrocytes transmembrane protein) (Mature OL transmembrane protein) (Q14C87)
Organism: Homo sapiens (Human)
Function: May serve as a cell-surface marker for oligodendrocyte differentiation.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MCPSEMGTLWHHWSPVLISLAALFSKVTEGRGILESIQRFSLLPTYLPVTYHINNADVSFFLKEANQDIMRNSSLQSRVESFLIYKSRRLPVLNASYGPFSIEQVVPQDLMLPSNPFGFTNKFSLNWKLKAHILRDKVYLSRPKVQVLFHIMGRDWDDRSAGEKLPCLRVFAFRETREVRGSCRLQGDLGLCVAELELLSSWFSPPTVVAGRRKSVDQPEGTPVELYYTVHPGGERGDCVREDARRSNGIRTGHSDIDESGPPLQRIGSIFLYQTHRKPSLRELRLDNSVAIHYIPKTVRKGDVLTFPVSISRNSTEDRFTLRAKVKKGVNIIGVRASSPSIWDVKERTDYTGKYAPAVIVCQKKAAGSENSADGASYEVMQIDVEVEEPGDLPATQLVTWQVEYPGEITSDLGVSKIYVSPKDLIGVVPLAMEAEILNTAILTGKTVAVPVKVVSVEDDGTVTELLESVECRSSDEDVIKVSDRCDYVFVNGKEMKGKVNVVVNFTYQHLSSPLEMTVWVPRLPLQIEVSDTELNQIKGWRVPIVSSRRPAGDSEEEEDDERRGRGCTLQYQHAMVRVLTQFVAEAAGPGGHLAHLLGSDWQVDITELINDFMQVEEPRIAKLQGGQILMGQELGMTTIQILSPLSDTILAEKTITVLDEKVTITDLGVQLVTGLSLSLQLSPGSNRAIFATAVAQELLQRPKQEAAISCWVQFSDGSVTPLDIYDGKDFSLMATSLDEKVVSIHQDPKFKWPIIAAETEGQGTLVKVEMVISESCQKSKRKSVLAVGTANIKVKFGQNDANPNTSDSRHTGAGVHMENNVSDRRPKKPSQEWGSQEGQYYGSSSMGLMEGRGTTTDRSILQKKKGQESLLDDNSHLQTIPSDLTSFPAQVDLPRSNGEMDGNDLMQASKGLSDLEIGMYALLGVFCLAILVFLINCVTFALKYRHKQVPFEEQEGMSHSHDWVGLSNRTELLENHINFASSQDEQITAIDRGMDFEESKYLLSTNSQKSINGQLFKPLGPIIIDGKDQKSEPPTSPTSKRKRVKFTTFTAVSSDDEYPTRNSIVMSSEDDIKWVCQDLDPGDCKELHNYMERLHENV
Protein: At5g55210 (Q9FLP2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein TIC 21, chloroplastic
- Protein TIC 40, chloroplastic
- Translocase of chloroplast 34, chloroplastic
- Protein TOC75-3, chloroplastic
- Stress-response A/B barrel domain-containing protein HS1
Sequence:
MEGVGSRLSRTSSRYSGPAATAVFSGRVRKWKKKWVRVSTSSVGVFRASKSNGRNNSNNSNSPHHLLLHKWTPLTSATVTASDANGSGETEESPKRRFRYAPIAMLEHREKVISKDSEIEETEEFDTESPLPKAVELDMNLTDSDQTKEAKTGNLNLGLCLNSEGTEE