E2RK30 · PKHD1_CANLF
- ProteinFibrocystin
- GenePKHD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids4074 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Promotes ciliogenesis in renal epithelial cells and therefore participates in the tubules formation and/ or ensures the maintenance of the architecture of the lumen of the kidney (By similarity).
Has an impact on cellular symmetry by ensuring correct bipolar cell division through the regulation of centrosome duplication and mitotic spindle assembly and by maintaining oriented cell division (OCD) during tubular elongation through planar cell polarity (PCP) pathway (By similarity).
During epithelial cell morphogenesis regulates also cell-cell and cell-matrix adhesion and participates in cell motility (PubMed:31398719, PubMed:32698519).
Promotes cell-cell contact through the positive regulation of PTK2 kinase activity leading to either positive regulation of epithelial cell proliferation through the HRAS/RAF1 pathways, or negative regulation of apoptosis through the PDK1/AKT1 pathway (By similarity).
May act in collecting-duct and biliary differentiation (By similarity).
May participate in the regulation of the cholangiocytes proliferation and the CCN2 production in an CXCL8-dependent manner (By similarity).
Has an impact on cellular symmetry by ensuring correct bipolar cell division through the regulation of centrosome duplication and mitotic spindle assembly and by maintaining oriented cell division (OCD) during tubular elongation through planar cell polarity (PCP) pathway (By similarity).
During epithelial cell morphogenesis regulates also cell-cell and cell-matrix adhesion and participates in cell motility (PubMed:31398719, PubMed:32698519).
Promotes cell-cell contact through the positive regulation of PTK2 kinase activity leading to either positive regulation of epithelial cell proliferation through the HRAS/RAF1 pathways, or negative regulation of apoptosis through the PDK1/AKT1 pathway (By similarity).
May act in collecting-duct and biliary differentiation (By similarity).
May participate in the regulation of the cholangiocytes proliferation and the CCN2 production in an CXCL8-dependent manner (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 3616-3617 | Cleavage | ||||
Sequence: RN |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | chromosome, centromeric region | |
Cellular Component | cilium | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | nucleus | |
Cellular Component | spindle | |
Biological Process | branching morphogenesis of an epithelial tube | |
Biological Process | cell-cell junction organization | |
Biological Process | epithelial cell morphogenesis | |
Biological Process | establishment of centrosome localization | |
Biological Process | establishment of mitotic spindle orientation | |
Biological Process | negative regulation of epithelial cell apoptotic process | |
Biological Process | positive regulation of epithelial cell proliferation | |
Biological Process | regulation of cell adhesion | |
Biological Process | regulation of cell-cell adhesion | |
Biological Process | regulation of cell-matrix adhesion | |
Biological Process | regulation of cholangiocyte proliferation | |
Biological Process | regulation of establishment of planar polarity |
Names & Taxonomy
Protein names
- Recommended nameFibrocystin
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionE2RK30
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Note: The intra-cellular C-terminal fragment (ICD) translocates to the nucleus and is not detected in primary cilia (By similarity).
The extracellular domain (PECD) traffics beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) attached to the primary cilium (By similarity).
In the urine, the extracellular domain (PECD) exists as a highly abundant secreted form and a less abundant PECD form that is either tethered to or shed with the C-terminal fragment (PTM) in ELVs (By similarity).
The majority of full length PKHD1 protein resides at the endoplasmic reticulum and cannot pass beyond the mid-Golgi apparatus and is not detected in primary cilia (By similarity).
The intra-cellular C-terminal fragment of 21-kDa translocates to the nucleus. The extracellular domain traffics beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) attached to the primary cilium (By similarity).
The extracellular domain (PECD) traffics beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) attached to the primary cilium (By similarity).
In the urine, the extracellular domain (PECD) exists as a highly abundant secreted form and a less abundant PECD form that is either tethered to or shed with the C-terminal fragment (PTM) in ELVs (By similarity).
The majority of full length PKHD1 protein resides at the endoplasmic reticulum and cannot pass beyond the mid-Golgi apparatus and is not detected in primary cilia (By similarity).
The intra-cellular C-terminal fragment of 21-kDa translocates to the nucleus. The extracellular domain traffics beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) attached to the primary cilium (By similarity).
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 3854-3874 | Helical | ||||
Sequence: IILAVSLCSVASWLALCCLVC |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MIVWLISLMSIEILLLAGPALS | ||||||
Chain | PRO_5003163621 | 23-4074 | Fibrocystin | |||
Sequence: FHIEPKEGSLAGGTWITVIFDGLELEQLYPTNGSQLEIHLVNVAVPALPSIPCDVSPVFLDLPVVMCRTRSLLPEVHEGLYYLEAHAGGQVVGSPSPGLQDCCTFKFSREQTPIVYQVTPPSGVPGKMIHVYGWIITGRSETFDFDAEYIDSPLILEAQGDKWVTACSLINRQTGSCYPLQENHGLGTLQCRVEGNYIGSQNVSFSVFNKGKSMVHKNAWLVSAKLDLFLYQTYSEILSVFPETGSLGGKTDIIITGDFFDNPALVTIAGVPCDIRHMSPRKIECTTRAPGKRARLTAPQAGNRGLLFEVGEAVEGLDLTVATPGYRWQIVPNASSPFGFWFKEGQPFRARLSGFFVAPETNNYTFWIQADNQASLYFSQSEDPRMKVKVASIRVGTADWFDAWEQDRNEGVWQRKTPKLELVGGTRYYLEAEHYGRTPSRGMRIGVQIHNTWLNPDVVSTYLREKHQIRVRAQRLPEIQMLTVSGRGSFFLTWDNVTSQPIPENATAHQIQTAIEELLAVKCKLEPLSANILLWLGFEQGPEGSSFEGDLTSGTEPFCGRFSLHQPRRLVLTPPAAQKDYWLDRYTHLCIAYKGRMKNILKVTVFFTTDFQNFIKKNITCDWNLVGTRPNSWQFTCTDLWETCVHHSMYLQPPLVDSPVLVHRIDLFPLSQETSGFYVDEIIIADTNITVSQADSETAHPGGNLVESLCVVGSPPVYNISFWLVGCGQELPLITASIVPTGGEARRSGLVQVTTQRIQKTSPPLGGYFHIQLPTSVIPDVPVHISASHLRKLLQNNADNFTSRYLNSSDLTVMEDLKSCYEHEWTLSWSSQVGDLPNFIRVSDANLTGVNPAATVRVVYDGGVFLGPVFGDMLVTANQHTQVVVRVNDIPAHCSGSCSFQYLEGSTPQIHSAWYSLDGDISLLIYIFGINFSGDPQALEIMVNKTNCKVIFSNQTNVICQTDLLPVGMHRLFMVVRPFGRAINTSGEALFLSVEPRLDAVEPSRAAEIGGLWATIQGSGLEDVSLVLFGSQSCAINITTSNSRRIQCRVPPRGKDGPVVNLTVVSGDHSAVLPMAFTYVSSLNPVITSLSRNRSNIAGGDTLFIRMALLVNYTDLDVEVCIQNTLAPAHVQMPQGLEVVLPPLPAGLYSISVSINGISIRSPGVDLHIQYITEVFSIEPCCGSLLGGTILSISGIGFIRDPTLVWVFVGNRSCDILNSTETVIWCETPPAALLPDSNIPAIPVPMEIWAGNVSFARESLLNLSFTFLYEAAMTPVVTAMRGEIINNSLRFYVEGNNLSNSVILLGVSHCDLETQTLRNNVSLSGCSFPLHSLEAGFYPLQVRQKQMGFANMSAVPQQYVITPWIMAISPTHGSACGGTVLTVRGLALSSRKRSVQVDLLGPFTCVILSLGHQTILCQINKVNDSFPDVSFTLNVTVIVNGLPSECQGNCTLFLQEETTPIVDSLTTNISGSLTMVLIRGRKLGITAVEPMVFVDDHLPCIVTFFNASYVICWISDLTPGLHYVSVFHARNGYACFGNVSRHFYILPQVFHYFPKNFSIHGGSLLTVEGTALRGKNSTLVYVGQQACLTVSISTELIQCIVPAGNGSVGLVIEVDGLSYQMGVIGYSSAFTPRLLSISQTDDVLTFAVAQVSGAENVDIFIGMSPCVGISGNHTVLQCVVSSLPAGEYPVRGYDRMRGWASSVLVFTSTATISGVTENFGCLGGRLVHVFGAGFSPGNVSAAVCGAPCQVLANATVSAFSCLVLPLNVSLAFLCGLKHSEESCEASSSTYVQCDLTVTVGTETLPQSWPYLYICEESPQCLFAPDHWTESTFPWFSGLFISPKVERDEVLIYNSSCNIAMETEAKMECETPNQPITAKITEIRKSRGQSTQGNFSLQFCLRWSRTHSWFPERVPQDGDNVTVENGQLLLLDTNTSILNLLHIKGGKLIFMDPGPIELRAHAILISDGGELRIGSEDKPFQGKAEIKLYGSSHSTPFFPYGVKFLAVRNGTLSLHGLLPEVTFTHLQAAAYAGDTVLALEDAVDWHPGDEAVIISRIGVGGAKPMEEIVIVEAVHNTDLYLRSPLRYSHNFTENWVAGVLHILKVTVVLLSRSITIQGNLTAERMKHLASCQEASDSEGNLQDCLYSKSEKMLGSRDLGARVIVQSFPEEPSRVQLRGVQFRDLGQAFRKHVSALTLVGAMRDSYVQGCTVWSSFNRGLSMSMTLGLKVDSNIFYNILGHALLVGTDMDIKYISWEAAPEKKPDWSEQGNIIRNNVIISISGTEGLSSPEMLTPSGIYILNPTNVVEGNRVYVAGLGYFFHLVTSQTSQAPLLSFTQNIAHSCTRYGLFIYPQFQPPWDDGRGPTLFQNFTVWGSAGGARISRSSNLHLKNFQVYSCRDFGIDILESDANTSVTDSLLLGHFAHKGSLCMSAGIKTPKRWELIISNTTFVNFDLTDCVSIRTCSGCSRGQGGFTVKTNQLKFINSPNLVAFPFPHAAILEDLDGSLSGRNRSHILASMETLSASCLVNLSFSQIVPGSVCGEDVIFHHMSIGLANAPNVSYDLTITDSRNKTTTVNYVRDTLSNLYGWMALLLDQETYSLQFETPWISRSLQYSATFGSFAPGNYLLLVHTVLWPYPDILVRCGSQEGRSLPSLPLPGQDQGCDWFFNTQLRQLIYLVSGEGQVQVTLQVKEGVPPTISASTSAPESALKWSLPEAWTGIEEGWGGHNHTIPGPGDDILILPNRTVLVDTNLPFLKGLYVMGTLEFPVDRSNVLSVACMVIAGGELKVGTLDNPLEKEQKLLILLRASEGIFCDRLNGIHIDPGTIGVYGKVQLHGACPKKSWTRLAADIASGNERIIVEDAVDWRPHDKIVLSSSSYEPHEAEILTVKEVQAHHVKIYERLKYRHIGSVHVMEDGRCIRLAAEVGLLTRNIQIQPDISCRARLLVGSFRNSSSKEFSGVLQLSNVEIQNFGSPLYSSIEFTNASAGSWIISSSLHQSCSGGIRAAASHGIILNDNIVFGTVGHGIDLEGQNFSLSNNLVVLMTQSAWSTVWVAGIKANQAKDINLYGNVVAGSERIGFHIQGHRCSSPEARWSDNVAHSSLHGLHLYKENGLDNCTGISGFLAFKNFDYGAMLHVENSVEIENITLVDNSIGLLATVYVSSVPKSHIENVQIVLRNSVIIATSSSFDCIQDRVKPRSANLTSSDRAPSNPRGGRVGILWPIFTSEPNWWPQEPWHRVRNGHSTSGILKLQDVTFSNFVKSCYSDDLDICILPNVENTGIMHPIMAEGTRMLKIKDKNKFYFPPLQARKGLGILVCPESDCENPRKYLFKDLDGRALGLPPPVSVFPKTEAEWTGSFFNTGTFREEQKCTYRALIQGYICKQSDQAILILDNADATWAMQKLYPVVSVTRGFVDTFSSVNADAPCSTSGSASTFYSILPTREITKICFVDQTPQVLRFFLLGNRSTSKLLLAVFYHELQNPRVFIGESFIPPIMVQSTSSLLDESIGSNYFSILDNLLYVVLQGQEPIEIHSGVSIHLALTVMFSVLEKGWEIIILERLTDFLQVSQDQIRFIHEMPGNEATLKAIADNKAKRKRNCPTVTCASPYRVGQRRPLMTEMSSYRVPSPTIMETASKVIVIEIGDLPTIRSTRLISYLTSNKLQNLAHQIITAQQTGVLENVLNMTIGALLVTQPKGVTDYGNASSFKTGNFIYIRPYALSVLVQPSDGEVGKELTVQPRLVFLDKQNQRIESLGPPSEPWAISVSLEGTSDPVLKGCTQAESQDGYVSFSNLAVLISGSNWHFIFTVTSPPGANFTARSRSFTVLPAAPSEKSSIILAVSLCSVASWLALCCLVCCWFRKSKSRKIKSEDISEFKTNDQKSHIHMSSKHPRSQETKKEDTMMGEDMKIKVIMDKVNQLPHQSLNGVSRRKVSRRAVREEGSSREEDVVPAPRIISITSQGHTCVPGSPDQQIYLQEAGNWKEAQEQLVSYQLAGQDQRLLLCPDLRRERQQLQGQSQLGQEGGSVGLSQEKKASGGATQASCPHLVHPETIQEQL | ||||||
Glycosylation | 54 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 224 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 355 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 385 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 518 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 527 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 640 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 710 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 741 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 822 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 829 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 868 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 953 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 966 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 976 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1006 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1059 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1083 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1115 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1134 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1233 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1240 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1274 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1284 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1308 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1319 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1342 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1373 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1445 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1456 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1471 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1490 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1528 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1560 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1578 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1598 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1627 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1694 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1760 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1775 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1789 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1875 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1915 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1941 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1955 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2030 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2111 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2140 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2390 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2431 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2467 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2531 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2549 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2579 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2591 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2749 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2764 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2972 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3004 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3053 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3136 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3165 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3221 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3484 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3702 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3721 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3833 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Palmitoylated. Palmitoylation facilitates the trafficking to the cilia and membrane targeting.
N-glycosylated.
Several proteolytic cleavages occur within the extracellular domain, whereas at least one cleavage occurs within the cytoplasmic domain. Cleaved by a probable proprotein convertase which produces an extracellular domain (polyductin extracellular domain, (PECD)) and a C-terminal fragment (polyductin transmembrane fragment (PTM)) which are tethered together by disulfide bonds. This extracellular domain (PECD) is then shed from the primary cilium by activation of a member of the ADAM metalloproteinase disintegrins family, resulting in concomitant release of an intra-cellular C-terminal fragment (ICD) via a gamma-secretase-dependent process. The proteolytic cleavage of the C-terminal intracellular fragment (ICD) is controlled by cytosolic calcium concentration and activation of PKC.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with CAMLG. Interacts with PKD2. Interacts (via CST) with ARF4; this interaction allows an efficient PKHD1 trafficking to the cilium. Interacts (via CST) with RAB8A; this interaction controls trafficking through the endomembrane systeme and to the cilium. Interacts (via CST) with TULP3; this interaction allows PKHD1 trafficking to the cilium.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 258-310 | IPT/TIG 1 | ||||
Sequence: EILSVFPETGSLGGKTDIIITGDFFDNPALVTIAGVPCDIRHMSPRKIECTTR | ||||||
Domain | 323-483 | PA14 | ||||
Sequence: AGNRGLLFEVGEAVEGLDLTVATPGYRWQIVPNASSPFGFWFKEGQPFRARLSGFFVAPETNNYTFWIQADNQASLYFSQSEDPRMKVKVASIRVGTADWFDAWEQDRNEGVWQRKTPKLELVGGTRYYLEAEHYGRTPSRGMRIGVQIHNTWLNPDVVST | ||||||
Domain | 944-1000 | IPT/TIG 2 | ||||
Sequence: SLLIYIFGINFSGDPQALEIMVNKTNCKVIFSNQTNVICQTDLLPVGMHRLFMVVRP | ||||||
Domain | 1018-1101 | IPT/TIG 3 | ||||
Sequence: PRLDAVEPSRAAEIGGLWATIQGSGLEDVSLVLFGSQSCAINITTSNSRRIQCRVPPRGKDGPVVNLTVVSGDHSAVLPMAFTY | ||||||
Domain | 1107-1186 | IPT/TIG 4 | ||||
Sequence: PVITSLSRNRSNIAGGDTLFIRMALLVNYTDLDVEVCIQNTLAPAHVQMPQGLEVVLPPLPAGLYSISVSINGISIRSPG | ||||||
Domain | 1199-1274 | IPT/TIG 5 | ||||
Sequence: SIEPCCGSLLGGTILSISGIGFIRDPTLVWVFVGNRSCDILNSTETVIWCETPPAALLPDSNIPAIPVPMEIWAGN | ||||||
Domain | 1385-1464 | IPT/TIG 6 | ||||
Sequence: PWIMAISPTHGSACGGTVLTVRGLALSSRKRSVQVDLLGPFTCVILSLGHQTILCQINKVNDSFPDVSFTLNVTVIVNGL | ||||||
Domain | 1573-1641 | IPT/TIG 7 | ||||
Sequence: HYFPKNFSIHGGSLLTVEGTALRGKNSTLVYVGQQACLTVSISTELIQCIVPAGNGSVGLVIEVDGLSY | ||||||
Domain | 1928-2049 | G8 1 | ||||
Sequence: HSWFPERVPQDGDNVTVENGQLLLLDTNTSILNLLHIKGGKLIFMDPGPIELRAHAILISDGGELRIGSEDKPFQGKAEIKLYGSSHSTPFFPYGVKFLAVRNGTLSLHGLLPEVTFTHLQA | ||||||
Repeat | 2245-2267 | PbH1 1 | ||||
Sequence: TLGLKVDSNIFYNILGHALLVGT | ||||||
Repeat | 2288-2322 | PbH1 2 | ||||
Sequence: EQGNIIRNNVIISISGTEGLSSPEMLTPSGIYILN | ||||||
Repeat | 2351-2373 | PbH1 3 | ||||
Sequence: APLLSFTQNIAHSCTRYGLFIYP | ||||||
Repeat | 2383-2404 | PbH1 4 | ||||
Sequence: RGPTLFQNFTVWGSAGGARISR | ||||||
Repeat | 2405-2427 | PbH1 5 | ||||
Sequence: SSNLHLKNFQVYSCRDFGIDILE | ||||||
Repeat | 2460-2483 | PbH1 6 | ||||
Sequence: RWELIISNTTFVNFDLTDCVSIRT | ||||||
Domain | 2743-2869 | G8 2 | ||||
Sequence: EGWGGHNHTIPGPGDDILILPNRTVLVDTNLPFLKGLYVMGTLEFPVDRSNVLSVACMVIAGGELKVGTLDNPLEKEQKLLILLRASEGIFCDRLNGIHIDPGTIGVYGKVQLHGACPKKSWTRLAA | ||||||
Repeat | 3029-3051 | PbH1 7 | ||||
Sequence: SHGIILNDNIVFGTVGHGIDLEG | ||||||
Repeat | 3082-3104 | PbH1 8 | ||||
Sequence: AKDINLYGNVVAGSERIGFHIQG | ||||||
Repeat | 3158-3183 | PbH1 9 | ||||
Sequence: ENSVEIENITLVDNSIGLLATVYVSS | ||||||
Region | 3871-3888 | Ciliary targeting sequence (CST) | ||||
Sequence: CLVCCWFRKSKSRKIKSE | ||||||
Region | 3896-3919 | Disordered | ||||
Sequence: NDQKSHIHMSSKHPRSQETKKEDT | ||||||
Region | 3943-3965 | Disordered | ||||
Sequence: NGVSRRKVSRRAVREEGSSREED | ||||||
Region | 3947-3976 | Nuclear localization signal (NLS) | ||||
Sequence: RRKVSRRAVREEGSSREEDVVPAPRIISIT | ||||||
Compositional bias | 3950-3965 | Basic and acidic residues | ||||
Sequence: VSRRAVREEGSSREED | ||||||
Region | 4031-4074 | Disordered | ||||
Sequence: LQGQSQLGQEGGSVGLSQEKKASGGATQASCPHLVHPETIQEQL |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length4,074
- Mass (Da)447,576
- Last updated2012-10-31 v2
- Checksum173062C7FA7FC244
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 3950-3965 | Basic and acidic residues | ||||
Sequence: VSRRAVREEGSSREED |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAEX03008386 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAEX03008387 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAEX03008388 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |