Q9BZV3 · IMPG2_HUMAN
- ProteinInterphotoreceptor matrix proteoglycan 2
- GeneIMPG2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1241 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Chondroitin sulfate- and hyaluronan-binding proteoglycan involved in the organization of interphotoreceptor matrix; may participate in the maturation and maintenance of the light-sensitive photoreceptor outer segment. Binds heparin.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | extracellular matrix | |
Cellular Component | extracellular region | |
Cellular Component | interphotoreceptor matrix | |
Cellular Component | membrane | |
Cellular Component | receptor complex | |
Molecular Function | extracellular matrix structural constituent | |
Molecular Function | heparin binding | |
Molecular Function | hyaluronic acid binding | |
Biological Process | extracellular matrix organization | |
Biological Process | protein localization | |
Biological Process | retina morphogenesis in camera-type eye | |
Biological Process | visual perception |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInterphotoreceptor matrix proteoglycan 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BZV3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Photoreceptor outer segment membrane ; Single-pass type I membrane protein
Photoreceptor inner segment membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-1099 | Extracellular | ||||
Sequence: DFPSLTAQTYLSIEEIQEPKSAVSFLLPEESTDLSLATKKKQPLDRRETERQWLIRRRRSILFPNGVKICPDESVAEAVANHVKYFKVRVCQEAVWEAFRTFWDRLPGREEYHYWMNLCEDGVTSIFEMGTNFSESVEHRSLIMKKLTYAKETVSSSELSSPVPVGDTSTLGDTTLSVPHPEVDAYEGASESSLERPEESISNEIENVIEEATKPAGEQIAEFSIHLLGKQYREELQDSSSFHHQHLEEEFISEVENAFTGLPGYKEIRVLEFRSPKENDSGVDVYYAVTFNGEAISNTTWDLISLHSNKVENHGLVELDDKPTVVYTISNFRDYIAETLQQNFLLGNSSLNPDPDSLQLINVRGVLRHQTEDLVWNTQSSSLQATPSSILDNTFQAAWPSADESITSSIPPLDFSSGPPSATGRELWSESPLGDLVSTHKLAFPSKMGLSSSPEVLEVSSLTLHSVTPAVLQTGLPVASEERTSGSHLVEDGLANVEESEDFLSIDSLPSSSFTQPVPKETIPSMEDSDVSLTSSPYLTSSIPFGLDSLTSKVKDQLKVSPFLPDASMEKELIFDGGLGSGSGQKVDLITWPWSETSSEKSAEPLSKPWLEDDDSLLPAEIEDKKLVLVDKMDSTDQISKHSKYEHDDRSTHFPEEEPLSGPAVPIFADTAAESASLTLPKHISEVPGVDDYSVTKAPLILTSVAISASTDKSDQADAILREDMEQITESSNYEWFDSEVSMVKPDMQTLWTILPESERVWTRTSSLEKLSRDILASTPQSADRLWLSVTQSTKLPPTTISTLLEDEVIMGVQDISLELDRIGTDYYQPEQVQEQNGKVGSYVEMSTSVHSTEMVSVAWPTEGGDDLSYTQTSGALVVFFSLRVTNMMFSEDLFNKNSLEYKALEQRFLELLVPYLQSNLTGFQNLEILNFRNGSIVVNSRMKFANSVPPNVNNAVYMILEDFCTTAYNTMNLAIDKYSLDVESGDEANPCKFQACNEFSECLVNPWSGEAKCRCFPGYLSVEERPCQSLCDLQPDFCLNDGKCDIMPGHGAICRCRVGENWWYRGKHCEEFVSEP | ||||||
Transmembrane | 1100-1120 | Helical | ||||
Sequence: VIIGITIASVVGLLVIFSAII | ||||||
Topological domain | 1121-1241 | Cytoplasmic | ||||
Sequence: YFFIRTLQAHHDRSERESPFSGSSRQPDSLSSIENAVKYNPVYESHRAGCEKYEGPYPQHPFYSSASGDVIGGLSREEIRQMYESSELSREEIQERMRVLELYANDPEFAAFVREQQVEEV |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Retinitis pigmentosa 56 (RP56)
- Note
- DescriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
- See alsoMIM:613581
Natural variants in RP56
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_082176 | 127-1241 | missing | in RP56 | |
VAR_082177 | 171-1241 | missing | in RP56 | |
VAR_082178 | 212-1241 | missing | in RP56 | |
VAR_082181 | 296-302 | missing | in RP56 | |
VAR_082184 | 560-1241 | missing | in RP56 | |
VAR_082186 | 906-1241 | missing | in RP56 | |
VAR_082187 | 964-1241 | missing | in RP56 | |
VAR_082191 | 1088-1241 | missing | in RP56 |
Macular dystrophy, vitelliform, 5 (VMD5)
- Note
- DescriptionA form of macular dystrophy, a retinal disease in which various forms of deposits, pigmentary changes, and atrophic lesions are observed in the macula lutea. Vitelliform macular dystrophies are characterized by yellow, lipofuscin-containing deposits, usually localized at the center of the macula. VMD5 features include late-onset moderate visual impairment and preservation of retinal pigment epithelium reflectivity.
- See alsoMIM:616152
Natural variants in VMD5
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_064336 | 124 | F>L | in VMD5; dbSNP:rs201893545 | |
VAR_082179 | 226-1241 | missing | in VMD5 | |
VAR_082183 | 522-1241 | missing | in VMD5 | |
VAR_082185 | 856-1241 | missing | in VMD5 | |
VAR_072671 | 1077 | C>F | in VMD5; dbSNP:rs713993049 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_064336 | 124 | in VMD5; dbSNP:rs201893545 | |||
Sequence: F → L | ||||||
Natural variant | VAR_082176 | 127-1241 | in RP56 | |||
Sequence: Missing | ||||||
Natural variant | VAR_082177 | 171-1241 | in RP56 | |||
Sequence: Missing | ||||||
Natural variant | VAR_082178 | 212-1241 | in RP56 | |||
Sequence: Missing | ||||||
Natural variant | VAR_082179 | 226-1241 | in VMD5 | |||
Sequence: Missing | ||||||
Natural variant | VAR_082180 | 243 | found in a patient with vitelliform macular dystrophy; uncertain significance; dbSNP:rs1706811719 | |||
Sequence: A → P | ||||||
Natural variant | VAR_082181 | 296-302 | in RP56 | |||
Sequence: Missing | ||||||
Natural variant | VAR_039144 | 344 | in dbSNP:rs34375459 | |||
Sequence: K → N | ||||||
Natural variant | VAR_082182 | 379 | found in a patient with retinitis pigmentosa; uncertain significance | |||
Sequence: S → P | ||||||
Natural variant | VAR_082183 | 522-1241 | in VMD5 | |||
Sequence: Missing | ||||||
Natural variant | VAR_082184 | 560-1241 | in RP56 | |||
Sequence: Missing | ||||||
Natural variant | VAR_039145 | 674 | in dbSNP:rs571391 | |||
Sequence: T → I | ||||||
Natural variant | VAR_082185 | 856-1241 | in VMD5 | |||
Sequence: Missing | ||||||
Natural variant | VAR_082186 | 906-1241 | in RP56 | |||
Sequence: Missing | ||||||
Natural variant | VAR_082187 | 964-1241 | in RP56 | |||
Sequence: Missing | ||||||
Natural variant | VAR_082188 | 1008 | found in a patient with vitelliform macular dystrophy; uncertain significance | |||
Sequence: G → D | ||||||
Natural variant | VAR_039146 | 1013 | in dbSNP:rs116450347 | |||
Sequence: P → L | ||||||
Natural variant | VAR_082189 | 1016 | found in a patient with VMD5; uncertain significance | |||
Sequence: F → S | ||||||
Natural variant | VAR_082190 | 1042 | found in a patient with vitelliform macular dystophy; uncertain significance; dbSNP:rs990633116 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_072671 | 1077 | in VMD5; dbSNP:rs713993049 | |||
Sequence: C → F | ||||||
Natural variant | VAR_082191 | 1088-1241 | in RP56 | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,584 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MIMFPLFGKISLGILIFVLIEG | ||||||
Chain | PRO_0000320149 | 23-1241 | Interphotoreceptor matrix proteoglycan 2 | |||
Sequence: DFPSLTAQTYLSIEEIQEPKSAVSFLLPEESTDLSLATKKKQPLDRRETERQWLIRRRRSILFPNGVKICPDESVAEAVANHVKYFKVRVCQEAVWEAFRTFWDRLPGREEYHYWMNLCEDGVTSIFEMGTNFSESVEHRSLIMKKLTYAKETVSSSELSSPVPVGDTSTLGDTTLSVPHPEVDAYEGASESSLERPEESISNEIENVIEEATKPAGEQIAEFSIHLLGKQYREELQDSSSFHHQHLEEEFISEVENAFTGLPGYKEIRVLEFRSPKENDSGVDVYYAVTFNGEAISNTTWDLISLHSNKVENHGLVELDDKPTVVYTISNFRDYIAETLQQNFLLGNSSLNPDPDSLQLINVRGVLRHQTEDLVWNTQSSSLQATPSSILDNTFQAAWPSADESITSSIPPLDFSSGPPSATGRELWSESPLGDLVSTHKLAFPSKMGLSSSPEVLEVSSLTLHSVTPAVLQTGLPVASEERTSGSHLVEDGLANVEESEDFLSIDSLPSSSFTQPVPKETIPSMEDSDVSLTSSPYLTSSIPFGLDSLTSKVKDQLKVSPFLPDASMEKELIFDGGLGSGSGQKVDLITWPWSETSSEKSAEPLSKPWLEDDDSLLPAEIEDKKLVLVDKMDSTDQISKHSKYEHDDRSTHFPEEEPLSGPAVPIFADTAAESASLTLPKHISEVPGVDDYSVTKAPLILTSVAISASTDKSDQADAILREDMEQITESSNYEWFDSEVSMVKPDMQTLWTILPESERVWTRTSSLEKLSRDILASTPQSADRLWLSVTQSTKLPPTTISTLLEDEVIMGVQDISLELDRIGTDYYQPEQVQEQNGKVGSYVEMSTSVHSTEMVSVAWPTEGGDDLSYTQTSGALVVFFSLRVTNMMFSEDLFNKNSLEYKALEQRFLELLVPYLQSNLTGFQNLEILNFRNGSIVVNSRMKFANSVPPNVNNAVYMILEDFCTTAYNTMNLAIDKYSLDVESGDEANPCKFQACNEFSECLVNPWSGEAKCRCFPGYLSVEERPCQSLCDLQPDFCLNDGKCDIMPGHGAICRCRVGENWWYRGKHCEEFVSEPVIIGITIASVVGLLVIFSAIIYFFIRTLQAHHDRSERESPFSGSSRQPDSLSSIENAVKYNPVYESHRAGCEKYEGPYPQHPFYSSASGDVIGGLSREEIRQMYESSELSREEIQERMRVLELYANDPEFAAFVREQQVEEV | ||||||
Glycosylation | 154 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 190 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 192 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 301 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 320 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 370 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 544 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 556 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 942 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 956 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1014↔1025 | |||||
Sequence: CKFQACNEFSEC | ||||||
Disulfide bond | 1019↔1036 | |||||
Sequence: CNEFSECLVNPWSGEAKC | ||||||
Disulfide bond | 1038↔1050 | |||||
Sequence: CFPGYLSVEERPC | ||||||
Disulfide bond | 1054↔1067 | |||||
Sequence: CDLQPDFCLNDGKC | ||||||
Disulfide bond | 1061↔1077 | |||||
Sequence: CLNDGKCDIMPGHGAIC | ||||||
Disulfide bond | 1079↔1092 | |||||
Sequence: CRVGENWWYRGKHC |
Post-translational modification
Highly glycosylated (N- and O-linked carbohydrates).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the retina (at protein level) (PubMed:10702256, PubMed:29777959).
Expressed by photoreceptors of the interphotoreceptor matrix (IPM) surrounding both rods and cones (at protein level) (PubMed:10542133, PubMed:29777959).
IPM occupies the subretinal space between the apices of the retinal pigment epithelium and the neural retina (PubMed:10542133).
Expressed in the pineal gland (at protein level) (PubMed:10702256).
Expressed by photoreceptors of the interphotoreceptor matrix (IPM) surrounding both rods and cones (at protein level) (PubMed:10542133, PubMed:29777959).
IPM occupies the subretinal space between the apices of the retinal pigment epithelium and the neural retina (PubMed:10542133).
Expressed in the pineal gland (at protein level) (PubMed:10702256).
Developmental stage
Expressed in the retina 17 weeks post-conception (at protein level) (PubMed:29777959).
Expressed in the outer neuroblastic zone and retinal pigment epithelium (at protein level) (PubMed:29777959).
Expressed in the outer neuroblastic zone and retinal pigment epithelium (at protein level) (PubMed:29777959).
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 180-198 | Polar residues | ||||
Sequence: ELSSPVPVGDTSTLGDTTL | ||||||
Region | 180-223 | Disordered | ||||
Sequence: ELSSPVPVGDTSTLGDTTLSVPHPEVDAYEGASESSLERPEESI | ||||||
Domain | 239-353 | SEA 1 | ||||
Sequence: GEQIAEFSIHLLGKQYREELQDSSSFHHQHLEEEFISEVENAFTGLPGYKEIRVLEFRSPKENDSGVDVYYAVTFNGEAISNTTWDLISLHSNKVENHGLVELDDKPTVVYTISN | ||||||
Region | 259-267 | Hyaluronan-binding motif involved in chondroitin sulfate A-binding | ||||
Sequence: QDSSSFHHQ | ||||||
Compositional bias | 660-678 | Basic and acidic residues | ||||
Sequence: QISKHSKYEHDDRSTHFPE | ||||||
Region | 660-684 | Disordered | ||||
Sequence: QISKHSKYEHDDRSTHFPEEEPLSG | ||||||
Domain | 897-1010 | SEA 2 | ||||
Sequence: GALVVFFSLRVTNMMFSEDLFNKNSLEYKALEQRFLELLVPYLQSNLTGFQNLEILNFRNGSIVVNSRMKFANSVPPNVNNAVYMILEDFCTTAYNTMNLAIDKYSLDVESGDE | ||||||
Domain | 1010-1051 | EGF-like 1 | ||||
Sequence: EANPCKFQACNEFSECLVNPWSGEAKCRCFPGYLSVEERPCQ | ||||||
Domain | 1052-1093 | EGF-like 2 | ||||
Sequence: SLCDLQPDFCLNDGKCDIMPGHGAICRCRVGENWWYRGKHCE | ||||||
Region | 1080-1088 | Hyaluronan-binding motif involved in chondroitin sulfate C-binding | ||||
Sequence: RVGENWWYR | ||||||
Region | 1125-1133 | Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding | ||||
Sequence: RTLQAHHDR | ||||||
Region | 1136-1145 | Hyaluronan-binding motif involved in chondroitin sulfate C-binding | ||||
Sequence: RESPFSGSSR | ||||||
Region | 1210-1218 | Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding motif | ||||
Sequence: REEIQERMR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,241
- Mass (Da)138,621
- Last updated2010-05-18 v3
- ChecksumE72D7BFB84824078
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 5 | in Ref. 2; AAF13154 | ||||
Sequence: P → L | ||||||
Sequence conflict | 77 | in Ref. 2; AAF13154 | ||||
Sequence: I → T | ||||||
Compositional bias | 180-198 | Polar residues | ||||
Sequence: ELSSPVPVGDTSTLGDTTL | ||||||
Compositional bias | 660-678 | Basic and acidic residues | ||||
Sequence: QISKHSKYEHDDRSTHFPE | ||||||
Sequence conflict | 668 | in Ref. 2; AAF13154 | ||||
Sequence: E → V | ||||||
Sequence conflict | 715 | in Ref. 1; AAF06999 | ||||
Sequence: Y → C | ||||||
Sequence conflict | 1012 | in Ref. 1; AAG49889 | ||||
Sequence: N → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF173155 EMBL· GenBank· DDBJ | AAF06999.1 EMBL· GenBank· DDBJ | mRNA | ||
AF271379 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271363 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271364 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271365 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271366 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271367 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271368 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271369 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271370 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271371 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271372 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271373 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271374 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271375 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271376 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271377 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF271378 EMBL· GenBank· DDBJ | AAG49889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF157624 EMBL· GenBank· DDBJ | AAF13154.1 EMBL· GenBank· DDBJ | mRNA | ||
AC068764 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |