E9PY61 · GP179_MOUSE
- ProteinG-protein coupled receptor 179
- GeneGpr179
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2293 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Orphan receptor involved in vision (PubMed:22325362, PubMed:24114537, PubMed:24790204, PubMed:30282023).
Required for signal transduction through retinal depolarizing bipolar cells (PubMed:22325362, PubMed:24114537, PubMed:24790204, PubMed:33922602).
Acts as an atypical G-protein coupled receptor that recruits and regulates the R7 group RGS-GNB5 complexes instead of activating G proteins: promotes the GTPase activator activity of R7 RGS proteins, increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:22689652, PubMed:24790204).
Associates with components of metabotropic signaling cascade in retina ON-bipolar neurons, such as TRPM1 and GRM6: may control the ability of the GRM6 cascade to gate TRPM1 (PubMed:24114537, PubMed:24790204).
Required for signal transduction through retinal depolarizing bipolar cells (PubMed:22325362, PubMed:24114537, PubMed:24790204, PubMed:33922602).
Acts as an atypical G-protein coupled receptor that recruits and regulates the R7 group RGS-GNB5 complexes instead of activating G proteins: promotes the GTPase activator activity of R7 RGS proteins, increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:22689652, PubMed:24790204).
Associates with components of metabotropic signaling cascade in retina ON-bipolar neurons, such as TRPM1 and GRM6: may control the ability of the GRM6 cascade to gate TRPM1 (PubMed:24114537, PubMed:24790204).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell tip | |
Cellular Component | dendrite | |
Cellular Component | dendrite terminus | |
Cellular Component | postsynaptic membrane | |
Molecular Function | G protein-coupled receptor activity | |
Biological Process | protein localization to plasma membrane | |
Biological Process | response to light stimulus | |
Biological Process | visual perception |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameG-protein coupled receptor 179
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionE9PY61
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Postsynaptic cell membrane ; Multi-pass membrane protein
Note: Specifically localizes to the tips of retinal ON-bipolar dendrites.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 383-403 | Helical; Name=1 | ||||
Sequence: AVLACQACCMLAVFLSMLVAY | ||||||
Transmembrane | 416-436 | Helical; Name=2 | ||||
Sequence: IVLLETILFGSLLLYFPVFIL | ||||||
Transmembrane | 445-465 | Helical; Name=3 | ||||
Sequence: CVALRWVRLLGFAVVYGTIIL | ||||||
Transmembrane | 494-514 | Helical; Name=4 | ||||
Sequence: LGQLLLLVLGFLVVWTAGALE | ||||||
Transmembrane | 544-564 | Helical; Name=5 | ||||
Sequence: YIMVVAEMLLLCWGSFLCYAT | ||||||
Transmembrane | 585-602 | Helical; Name=6 | ||||
Sequence: LLLSTAFHTARFVLVPSL | ||||||
Transmembrane | 608-628 | Helical; Name=7 | ||||
Sequence: LLLFFLHTHSTVTATLALIFI |
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Disruption phenotype
Mice display impaired night vision due to a failure to transmit the photoreceptor signal through the depolarizing bipolar cells (PubMed:33922602).
Mice also show myopic features, probably caused by a decrease in both retinal dopamine and 3,4-dihydroxyphenylacetic acid (PubMed:36613663).
Mice also show myopic features, probably caused by a decrease in both retinal dopamine and 3,4-dihydroxyphenylacetic acid (PubMed:36613663).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 171 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MGARAVVISSLAWGLLSCCFLCSGALG | ||||||
Chain | PRO_5003245698 | 28-2293 | G-protein coupled receptor 179 | |||
Sequence: SQRPLRSLPPLPSQAKPRSEPMWMPPKGAEAALAFLYSGDVQRLSGANCSEKYEVRGAEGKAGVPPVLQRAAGTLAQAANFLNMLLQANDIRESSVEEDVEWYQALVRSVAEGDPKAYRALLTFNPAPGASHLQLALQATRMGDETVLQDLSGNKVQEETPGEDLDRPVLQKRVLTNDLRSLDSPKWPRGDGYVGDIQQVKLSPPFLECHEGQLRPGWLVTVSATFYGLKPDLTPEVRGQVQMDIDLQSVDINQCASGPGWYSNTHLCDLNSTQCVPLESQGFVLGRYLCRCRPGFYGASGSGGLEESATQAAGQFGSPQDSLGKLLRCQPCPEGCTSCLDATPCLVEEALALRTAVLACQACCMLAVFLSMLVAYRCRGSKRIRASGIVLLETILFGSLLLYFPVFILYFKPSVFRCVALRWVRLLGFAVVYGTIILKLYRVLQLFLSRTAQRVPHPSSGQLLRRLGQLLLLVLGFLVVWTAGALEPGTQHTALVTRGHTPTGRHFYLCHHDHWDYIMVVAEMLLLCWGSFLCYATRAVPSAFHEPRYMSIALHNELLLSTAFHTARFVLVPSLHPDWTLLLFFLHTHSTVTATLALIFIPKFWKPGAPPREEILDEVYEDELDLQRSGSYLNSSIASAWSERSLEPGDIRDELKKLYAQLEIRKTKEMAANNPHLPKKRGSSHQGLGRSFMRYLAEFPEALARQHSRDSGSLGLGSLPGSSRRRLLSSSLQETEKPPALRKTRSTYDHHREHNTLPFDSTLRRTLSKKASPTDGRESLADGPPALGFRSASAHNLTVGERLPRARPISLQKSLSVAAGSREKALLVASQAYLEETYRQAKEREERKKAEAAMVSPVRRPSTRRLEWPLRAPLSAPPSPGKSSSMDSSQTTARPHEEAGRRLPHPPIRHQVSTPVLALSGICLGEPRMLSPTPASTLAPILLPAPAPAPAPVLAPVSKPPQSPTLLTFICPWENAELPGKKENVVQEDPAGPERSGHSPASARTKIWRALSVAVEKRGTGESEALTEGGHVQGEADDTDEEKPKVFSKSHSLKTPLQQGSVRSLGLAIKALTRSRSTYKEKDGGEGTPETEKGKPTEVSTGAPLRSPRLGRPKAVSKQVALAPCEDEESLQNQQNAHTSRMLHVCQKEGSREQEDRNKRVAPGPGERKVERTGKITMTTLRQVFGEKNAEQAKESPAGYQEVPNPALQSLGSADHRVAEVCPWEVTEPESGMDPPESVNKAKVYSWERTEGGSLEKKPSRQVLSRSWEEREKVLAESETEGVGAIPRKKPERLVRSQEAVCPWESPDSGGLSPQLVHQESDRTGGRFVVVSKGDAHPEALPSHAAKAELCLWEMSDVGEGTSTQRVQELPEERQKSPKKATFWGERNLGGDLVSLCPWESTDFRGPSAVSLQAPGSSGSLGSGIAEVCPWEAENIANDKKAEVCPWELGEELAGSDGLNPGADGKSLPGKETPSRKGCLAESGEQTVRAKPTVPQGQESVCPWEDEAPERSSPQPDKASSKAGEKLLSHGGSQVLQVCPWEAVKPEEKQATLSTAEICPWEVDGQPETRTSEHPSKGEVHKDEEKMPGRARIKAQEEAEGRIQKQEAICPWESMAPGSTPQRDTEKAQASLQRQGSVAGRAAEICPWEVGTEVGEERTIGAEASEARPNDAGHASTDSGSRQVAASAPKKSERLGSEKEVVCPWDSLSPGDSSQQPDTPNTEKLKDELQEHGSSRPIEVCPWEAEEVPTGEKAKICPWELNEGTVGKGLEREPGCEPERQRRQNLEEAGLPFQEEGTSKGDTKLCREQEGEAICPWKPPAQVPKVSDLPLSTVGQGVEGQSLEASDRASEKGELRQDLKMGSLPEYITQVVPVDGGGASSELQPISLQEGMVLAGSSSHPHIQCPDQPRVSSQPLVSTGDGTAEVCPWDAPDSDSDTKVEPCAQKVTGRVTETEMSRQDEKEKSQEEKERAPETRDHEGVAVQKMPQTSNFGKQEAVCPRESQDFGVQAATDASDGSKGGSEKVCPWEVEEVPSIKEAEICPWEASPGAVGEGALDLGQDGESQGEGRAERHLLKAAETVCPLEGTMSSGLFTQEDVVDTDLPKVGLHGASSPGKGLAELCVWEVTDPEGNKIKGTMADICPWEETRAQSDESGPLALPVTQAGVPAAPEKSVCLSVHGPLESFLPESKSVRPDISKPPGSSRPEGVREQEPLELETGAKSVPKPSPTETEAPESFTLTDDQGLMASEGEAGELSPPPDYPWDCE | ||||||
Glycosylation | 75 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 76↔236 | |||||
Sequence: CSEKYEVRGAEGKAGVPPVLQRAAGTLAQAANFLNMLLQANDIRESSVEEDVEWYQALVRSVAEGDPKAYRALLTFNPAPGASHLQLALQATRMGDETVLQDLSGNKVQEETPGEDLDRPVLQKRVLTNDLRSLDSPKWPRGDGYVGDIQQVKLSPPFLEC | ||||||
Glycosylation | 298 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 445↔537 | |||||
Sequence: CVALRWVRLLGFAVVYGTIILKLYRVLQLFLSRTAQRVPHPSSGQLLRRLGQLLLLVLGFLVVWTAGALEPGTQHTALVTRGHTPTGRHFYLC | ||||||
Glycosylation | 661 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 823 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer (PubMed:34333057).
Associates with the R7 group RGS-GNB5 complexes, composed of an R7 group RGS subunit (RGS6, RGS7, RGS9 or RGS11) and GNB5, promoting their localization to the cell membrane and regulating the GTPase activator activity of R7 RGS proteins (PubMed:22689652).
Interacts with TRPM1 (PubMed:24114537, PubMed:24790204).
Interacts with GRM6 (PubMed:24114537).
Interacts with EGFLAM; transsynaptic interaction is required for synaptic organization of photoreceptor cells (PubMed:30282023).
Associates with the R7 group RGS-GNB5 complexes, composed of an R7 group RGS subunit (RGS6, RGS7, RGS9 or RGS11) and GNB5, promoting their localization to the cell membrane and regulating the GTPase activator activity of R7 RGS proteins (PubMed:22689652).
Interacts with TRPM1 (PubMed:24114537, PubMed:24790204).
Interacts with GRM6 (PubMed:24114537).
Interacts with EGFLAM; transsynaptic interaction is required for synaptic organization of photoreceptor cells (PubMed:30282023).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 62-245 | Cache-like region | ||||
Sequence: FLYSGDVQRLSGANCSEKYEVRGAEGKAGVPPVLQRAAGTLAQAANFLNMLLQANDIRESSVEEDVEWYQALVRSVAEGDPKAYRALLTFNPAPGASHLQLALQATRMGDETVLQDLSGNKVQEETPGEDLDRPVLQKRVLTNDLRSLDSPKWPRGDGYVGDIQQVKLSPPFLECHEGQLRPGW | ||||||
Region | 733-812 | Disordered | ||||
Sequence: QHSRDSGSLGLGSLPGSSRRRLLSSSLQETEKPPALRKTRSTYDHHREHNTLPFDSTLRRTLSKKASPTDGRESLADGPP | ||||||
Compositional bias | 738-764 | Polar residues | ||||
Sequence: SGSLGLGSLPGSSRRRLLSSSLQETEK | ||||||
Compositional bias | 765-786 | Basic and acidic residues | ||||
Sequence: PPALRKTRSTYDHHREHNTLPF | ||||||
Region | 872-935 | Disordered | ||||
Sequence: EERKKAEAAMVSPVRRPSTRRLEWPLRAPLSAPPSPGKSSSMDSSQTTARPHEEAGRRLPHPPI | ||||||
Compositional bias | 905-920 | Polar residues | ||||
Sequence: PSPGKSSSMDSSQTTA | ||||||
Region | 1046-1235 | Disordered | ||||
Sequence: GTGESEALTEGGHVQGEADDTDEEKPKVFSKSHSLKTPLQQGSVRSLGLAIKALTRSRSTYKEKDGGEGTPETEKGKPTEVSTGAPLRSPRLGRPKAVSKQVALAPCEDEESLQNQQNAHTSRMLHVCQKEGSREQEDRNKRVAPGPGERKVERTGKITMTTLRQVFGEKNAEQAKESPAGYQEVPNPAL | ||||||
Compositional bias | 1058-1076 | Basic and acidic residues | ||||
Sequence: HVQGEADDTDEEKPKVFSK | ||||||
Compositional bias | 1102-1120 | Basic and acidic residues | ||||
Sequence: SRSTYKEKDGGEGTPETEK | ||||||
Compositional bias | 1155-1169 | Polar residues | ||||
Sequence: EESLQNQQNAHTSRM | ||||||
Compositional bias | 1172-1202 | Basic and acidic residues | ||||
Sequence: VCQKEGSREQEDRNKRVAPGPGERKVERTGK | ||||||
Region | 1275-1294 | Disordered | ||||
Sequence: ERTEGGSLEKKPSRQVLSRS | ||||||
Compositional bias | 1277-1294 | Basic and acidic residues | ||||
Sequence: TEGGSLEKKPSRQVLSRS | ||||||
Region | 1326-1345 | Disordered | ||||
Sequence: EAVCPWESPDSGGLSPQLVH | ||||||
Region | 1388-1411 | Disordered | ||||
Sequence: GTSTQRVQELPEERQKSPKKATFW | ||||||
Compositional bias | 1394-1408 | Basic and acidic residues | ||||
Sequence: VQELPEERQKSPKKA | ||||||
Region | 1479-1560 | Disordered | ||||
Sequence: ELAGSDGLNPGADGKSLPGKETPSRKGCLAESGEQTVRAKPTVPQGQESVCPWEDEAPERSSPQPDKASSKAGEKLLSHGGS | ||||||
Region | 1578-1770 | Disordered | ||||
Sequence: ATLSTAEICPWEVDGQPETRTSEHPSKGEVHKDEEKMPGRARIKAQEEAEGRIQKQEAICPWESMAPGSTPQRDTEKAQASLQRQGSVAGRAAEICPWEVGTEVGEERTIGAEASEARPNDAGHASTDSGSRQVAASAPKKSERLGSEKEVVCPWDSLSPGDSSQQPDTPNTEKLKDELQEHGSSRPIEVCPW | ||||||
Compositional bias | 1594-1631 | Basic and acidic residues | ||||
Sequence: PETRTSEHPSKGEVHKDEEKMPGRARIKAQEEAEGRIQ | ||||||
Compositional bias | 1645-1663 | Polar residues | ||||
Sequence: GSTPQRDTEKAQASLQRQG | ||||||
Compositional bias | 1699-1713 | Polar residues | ||||
Sequence: AGHASTDSGSRQVAA | ||||||
Region | 1792-1828 | Disordered | ||||
Sequence: TVGKGLEREPGCEPERQRRQNLEEAGLPFQEEGTSKG | ||||||
Compositional bias | 1793-1813 | Basic and acidic residues | ||||
Sequence: VGKGLEREPGCEPERQRRQNL | ||||||
Region | 1844-1882 | Disordered | ||||
Sequence: WKPPAQVPKVSDLPLSTVGQGVEGQSLEASDRASEKGEL | ||||||
Region | 1924-2051 | Disordered | ||||
Sequence: SSSHPHIQCPDQPRVSSQPLVSTGDGTAEVCPWDAPDSDSDTKVEPCAQKVTGRVTETEMSRQDEKEKSQEEKERAPETRDHEGVAVQKMPQTSNFGKQEAVCPRESQDFGVQAATDASDGSKGGSEK | ||||||
Compositional bias | 1928-1947 | Polar residues | ||||
Sequence: PHIQCPDQPRVSSQPLVSTG | ||||||
Compositional bias | 1980-2008 | Basic and acidic residues | ||||
Sequence: ETEMSRQDEKEKSQEEKERAPETRDHEGV | ||||||
Region | 2212-2293 | Disordered | ||||
Sequence: FLPESKSVRPDISKPPGSSRPEGVREQEPLELETGAKSVPKPSPTETEAPESFTLTDDQGLMASEGEAGELSPPPDYPWDCE | ||||||
Compositional bias | 2256-2270 | Polar residues | ||||
Sequence: TETEAPESFTLTDDQ |
Sequence similarities
Belongs to the G-protein coupled receptor 3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,293
- Mass (Da)248,715
- Last updated2011-04-05 v1
- ChecksumDB9EB2BA17CD6785
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 738-764 | Polar residues | ||||
Sequence: SGSLGLGSLPGSSRRRLLSSSLQETEK | ||||||
Compositional bias | 765-786 | Basic and acidic residues | ||||
Sequence: PPALRKTRSTYDHHREHNTLPF | ||||||
Compositional bias | 905-920 | Polar residues | ||||
Sequence: PSPGKSSSMDSSQTTA | ||||||
Compositional bias | 1058-1076 | Basic and acidic residues | ||||
Sequence: HVQGEADDTDEEKPKVFSK | ||||||
Compositional bias | 1102-1120 | Basic and acidic residues | ||||
Sequence: SRSTYKEKDGGEGTPETEK | ||||||
Compositional bias | 1155-1169 | Polar residues | ||||
Sequence: EESLQNQQNAHTSRM | ||||||
Compositional bias | 1172-1202 | Basic and acidic residues | ||||
Sequence: VCQKEGSREQEDRNKRVAPGPGERKVERTGK | ||||||
Compositional bias | 1277-1294 | Basic and acidic residues | ||||
Sequence: TEGGSLEKKPSRQVLSRS | ||||||
Compositional bias | 1394-1408 | Basic and acidic residues | ||||
Sequence: VQELPEERQKSPKKA | ||||||
Compositional bias | 1594-1631 | Basic and acidic residues | ||||
Sequence: PETRTSEHPSKGEVHKDEEKMPGRARIKAQEEAEGRIQ | ||||||
Compositional bias | 1645-1663 | Polar residues | ||||
Sequence: GSTPQRDTEKAQASLQRQG | ||||||
Compositional bias | 1699-1713 | Polar residues | ||||
Sequence: AGHASTDSGSRQVAA | ||||||
Compositional bias | 1793-1813 | Basic and acidic residues | ||||
Sequence: VGKGLEREPGCEPERQRRQNL | ||||||
Compositional bias | 1928-1947 | Polar residues | ||||
Sequence: PHIQCPDQPRVSSQPLVSTG | ||||||
Compositional bias | 1980-2008 | Basic and acidic residues | ||||
Sequence: ETEMSRQDEKEKSQEEKERAPETRDHEGV | ||||||
Compositional bias | 2256-2270 | Polar residues | ||||
Sequence: TETEAPESFTLTDDQ |
Keywords
- Technical term