ID PKHD1_CANLF Reviewed; 4074 AA. AC E2RK30; DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2012, sequence version 2. DT 25-MAY-2022, entry version 81. DE RecName: Full=Fibrocystin {ECO:0000250|UniProtKB:P08F94}; DE AltName: Full=Polycystic kidney and hepatic disease 1 protein; DE AltName: Full=Polyductin; DE Flags: Precursor; GN Name=PKHD1 {ECO:0000250|UniProtKB:P08F94}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer; RX PubMed=16341006; DOI=10.1038/nature04338; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., RA Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] RP FUNCTION. RX PubMed=31398719; DOI=10.1088/1478-3975/ab39fa; RA Puder S., Fischer T., Mierke C.T.; RT "The transmembrane protein fibrocystin/polyductin regulates cell mechanics RT and cell motility."; RL Phys. Biol. 16:066006-066006(2019). RN [3] RP FUNCTION. RX PubMed=32698519; DOI=10.3390/ijms21145140; RA Ziegler W.H., Soetje B., Marten L.P., Wiese J., Burute M., Haffner D.; RT "Fibrocystin Is Essential to Cellular Control of Adhesion and Epithelial RT Morphogenesis."; RL Int. J. Mol. Sci. 21:0-0(2020). CC -!- FUNCTION: Promotes ciliogenesis in renal epithelial cells and therefore CC participates in the tubules formation and/ or ensures the maintenance CC of the architecture of the lumen of the kidney (By similarity). Has an CC impact on cellular symmetry by ensuring correct bipolar cell division CC through the regulation of centrosome duplication and mitotic spindle CC assembly and by maintaining oriented cell division (OCD) during tubular CC elongation through planar cell polarity (PCP) pathway (By similarity). CC During epithelial cell morphogenesis regulates also cell-cell and cell- CC matrix adhesion and participates in cell motility (PubMed:32698519, CC PubMed:31398719). Promotes cell-cell contact through the positive CC regulation of PTK2 kinase activity leading to either positive CC regulation of epithelial cell proliferation through the HRAS/RAF1 CC pathways, or negative regulation of apoptosis through the PDK1/AKT1 CC pathway (By similarity). May act in collecting-duct and biliary CC differentiation (By similarity). May participate in the regulation of CC the cholangiocytes proliferation and the CCN2 production in an CXCL8- CC dependent manner (By similarity). {ECO:0000250|UniProtKB:E9PZ36, CC ECO:0000250|UniProtKB:P08F94, ECO:0000269|PubMed:31398719, CC ECO:0000269|PubMed:32698519}. CC -!- SUBUNIT: Interacts with CAMLG. Interacts with PKD2. Interacts (via CST) CC with ARF4; this interaction allows an efficient PKHD1 trafficking to CC the cilium. Interacts (via CST) with RAB8A; this interaction controls CC trafficking through the endomembrane systeme and to the cilium. CC Interacts (via CST) with TULP3; this interaction allows PKHD1 CC trafficking to the cilium. {ECO:0000250|UniProtKB:E9PZ36}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08F94}; CC Single-pass membrane protein {ECO:0000255}. Cytoplasm CC {ECO:0000250|UniProtKB:P08F94}. Apical cell membrane CC {ECO:0000250|UniProtKB:E9PZ36}. Cytoplasm, cytoskeleton, cilium basal CC body {ECO:0000250|UniProtKB:P08F94}. Cell projection, cilium CC {ECO:0000250|UniProtKB:E9PZ36}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000250|UniProtKB:P08F94}. Chromosome, centromere CC {ECO:0000250|UniProtKB:P08F94}. Nucleus {ECO:0000250|UniProtKB:E9PZ36}. CC Secreted, extracellular exosome {ECO:0000250|UniProtKB:E9PZ36}. CC Secreted {ECO:0000250|UniProtKB:E9PZ36}. Endoplasmic reticulum CC {ECO:0000250|UniProtKB:E9PZ36}. Golgi apparatus CC {ECO:0000250|UniProtKB:E9PZ36}. Note=The intra-cellular C-terminal CC fragment (ICD) translocates to the nucleus and is not detected in CC primary cilia (By similarity). The extracellular domain (PECD) traffics CC beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) CC attached to the primary cilium (By similarity). In the urine, the CC extracellular domain (PECD) exists as an highly abundant secreted form CC and a less abundant PECD form that is either tethered to or shed with CC the C-terminal fragment (PTM) in ELVs (By similarity). The majority of CC full length PKHD1 protein resides at the endoplasmic reticulum and CC cannot pass beyond the mid-Golgi apparatus and is not detected in CC primary cilia (By similarity). The intra-cellular C-terminal fragment CC of 21-kDa translocates to the nucleus. The extracellular domain CC traffics beyond the mid-Golgi and localizes on exosome like vesicles CC (ELVs) attached to the primary cilium (By similarity). CC {ECO:0000250|UniProtKB:E9PZ36}. CC -!- PTM: Palmitoylated. Palmitoylation facilitates the trafficking to the CC cilia and membrane targeting. {ECO:0000250|UniProtKB:E9PZ36}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:E9PZ36}. CC -!- PTM: Several proteolytic cleavages occur within the extracellular CC domain, whereas at least one cleavage occurs within the cytoplasmic CC domain. Cleaved by a probable proprotein convertase which produces an CC extracellular domain (polyductin extracellular domain, (PECD)) and a C- CC terminal fragment (polyductin transmembrane fragment (PTM)) which are CC tethered together by disulfide bonds. This extracellular domain (PECD) CC is then shed from the primary cilium by activation of a member of the CC ADAM metalloproteinase disintegrins family, resulting in concomitant CC release of an intra-cellular C-terminal fragment (ICD) via a gamma- CC secretase-dependent process. The proteolytic cleavage of the C-terminal CC intracellular fragment (ICD) is controlled by cytosolic calcium CC concentration and activation of PKC. {ECO:0000250|UniProtKB:E9PZ36}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAEX03008386; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAEX03008387; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAEX03008388; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005627522.1; XM_005627465.1. DR CORUM; E2RK30; -. DR STRING; 9612.ENSCAFP00000003171; -. DR PaxDb; E2RK30; -. DR GeneID; 474934; -. DR KEGG; cfa:474934; -. DR CTD; 5314; -. DR VGNC; VGNC:44605; PKHD1. DR eggNOG; ENOG502QR85; Eukaryota. DR GeneTree; ENSGT00940000160697; -. DR HOGENOM; CLU_000057_1_0_1; -. DR InParanoid; E2RK30; -. DR OMA; ETVHNAD; -. DR OrthoDB; 323806at2759; -. DR TreeFam; TF329582; -. DR Proteomes; UP000002254; Chromosome 12. DR Bgee; ENSCAFG00000002165; Expressed in pancreas and 12 other tissues. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005929; C:cilium; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISS:UniProtKB. DR GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB. DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:UniProtKB. DR GO; GO:0051660; P:establishment of centrosome localization; IMP:UniProtKB. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB. DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; ISS:UniProtKB. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB. DR GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0001952; P:regulation of cell-matrix adhesion; IMP:UniProtKB. DR GO; GO:0010824; P:regulation of centrosome duplication; IEA:InterPro. DR GO; GO:1904054; P:regulation of cholangiocyte proliferation; ISS:UniProtKB. DR GO; GO:0090175; P:regulation of establishment of planar polarity; ISS:UniProtKB. DR Gene3D; 2.160.20.10; -; 2. DR Gene3D; 2.60.40.10; -; 5. DR InterPro; IPR039448; Beta_helix. DR InterPro; IPR019316; G8_domain. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT_dom. DR InterPro; IPR037524; PA14/GLEYA. DR InterPro; IPR006626; PbH1. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR028839; PKHD1. DR PANTHER; PTHR46769:SF1; PTHR46769:SF1; 1. DR Pfam; PF13229; Beta_helix; 1. DR Pfam; PF10162; G8; 2. DR Pfam; PF01833; TIG; 7. DR SMART; SM01225; G8; 2. DR SMART; SM00429; IPT; 5. DR SMART; SM00710; PbH1; 9. DR SUPFAM; SSF51126; SSF51126; 2. DR SUPFAM; SSF81296; SSF81296; 6. DR PROSITE; PS51484; G8; 2. DR PROSITE; PS51820; PA14; 1. PE 3: Inferred from homology; KW Cell membrane; Cell projection; Centromere; Chromosome; Cytoplasm; KW Cytoskeleton; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; KW Membrane; Nucleus; Reference proteome; Repeat; Secreted; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..4074 FT /note="Fibrocystin" FT /evidence="ECO:0000255" FT /id="PRO_5003163621" FT TRANSMEM 3854..3874 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 258..310 FT /note="IPT/TIG 1" FT /evidence="ECO:0000255" FT DOMAIN 323..483 FT /note="PA14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164" FT DOMAIN 944..1000 FT /note="IPT/TIG 2" FT /evidence="ECO:0000255" FT DOMAIN 1018..1101 FT /note="IPT/TIG 3" FT /evidence="ECO:0000255" FT DOMAIN 1107..1186 FT /note="IPT/TIG 4" FT /evidence="ECO:0000255" FT DOMAIN 1199..1274 FT /note="IPT/TIG 5" FT /evidence="ECO:0000255" FT DOMAIN 1385..1464 FT /note="IPT/TIG 6" FT /evidence="ECO:0000255" FT DOMAIN 1573..1641 FT /note="IPT/TIG 7" FT /evidence="ECO:0000255" FT DOMAIN 1928..2049 FT /note="G8 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00817" FT REPEAT 2245..2267 FT /note="PbH1 1" FT /evidence="ECO:0000255" FT REPEAT 2288..2322 FT /note="PbH1 2" FT /evidence="ECO:0000255" FT REPEAT 2351..2373 FT /note="PbH1 3" FT /evidence="ECO:0000255" FT REPEAT 2383..2404 FT /note="PbH1 4" FT /evidence="ECO:0000255" FT REPEAT 2405..2427 FT /note="PbH1 5" FT /evidence="ECO:0000255" FT REPEAT 2460..2483 FT /note="PbH1 6" FT /evidence="ECO:0000255" FT DOMAIN 2743..2869 FT /note="G8 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00817" FT REPEAT 3029..3051 FT /note="PbH1 7" FT /evidence="ECO:0000255" FT REPEAT 3082..3104 FT /note="PbH1 8" FT /evidence="ECO:0000255" FT REPEAT 3158..3183 FT /note="PbH1 9" FT /evidence="ECO:0000255" FT REGION 3871..3888 FT /note="Ciliary targeting sequence (CST)" FT /evidence="ECO:0000250|UniProtKB:E9PZ36" FT REGION 3896..3919 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3943..3965 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3947..3976 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000250|UniProtKB:E9PZ36" FT REGION 4031..4074 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3950..3965 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 3616..3617 FT /note="Cleavage" FT /evidence="ECO:0000250|UniProtKB:P08F94" FT CARBOHYD 54 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 224 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 355 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 385 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 518 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 527 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 640 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 710 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 741 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 822 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 829 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 868 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 953 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 966 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 976 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1006 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1059 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1083 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1115 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1134 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1233 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1240 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1274 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1284 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1308 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1319 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1342 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1373 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1445 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1456 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1471 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1490 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1528 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1560 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1578 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1598 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1627 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1694 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1760 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1775 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1789 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1875 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1915 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1941 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 1955 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2030 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2140 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2390 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2431 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2467 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2531 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2549 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2579 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2591 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2749 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2764 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 2972 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 3004 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 3053 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 3136 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 3165 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 3221 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 3484 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 3702 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 3721 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 3833 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" SQ SEQUENCE 4074 AA; 447576 MW; 173062C7FA7FC244 CRC64; MIVWLISLMS IEILLLAGPA LSFHIEPKEG SLAGGTWITV IFDGLELEQL YPTNGSQLEI HLVNVAVPAL PSIPCDVSPV FLDLPVVMCR TRSLLPEVHE GLYYLEAHAG GQVVGSPSPG LQDCCTFKFS REQTPIVYQV TPPSGVPGKM IHVYGWIITG RSETFDFDAE YIDSPLILEA QGDKWVTACS LINRQTGSCY PLQENHGLGT LQCRVEGNYI GSQNVSFSVF NKGKSMVHKN AWLVSAKLDL FLYQTYSEIL SVFPETGSLG GKTDIIITGD FFDNPALVTI AGVPCDIRHM SPRKIECTTR APGKRARLTA PQAGNRGLLF EVGEAVEGLD LTVATPGYRW QIVPNASSPF GFWFKEGQPF RARLSGFFVA PETNNYTFWI QADNQASLYF SQSEDPRMKV KVASIRVGTA DWFDAWEQDR NEGVWQRKTP KLELVGGTRY YLEAEHYGRT PSRGMRIGVQ IHNTWLNPDV VSTYLREKHQ IRVRAQRLPE IQMLTVSGRG SFFLTWDNVT SQPIPENATA HQIQTAIEEL LAVKCKLEPL SANILLWLGF EQGPEGSSFE GDLTSGTEPF CGRFSLHQPR RLVLTPPAAQ KDYWLDRYTH LCIAYKGRMK NILKVTVFFT TDFQNFIKKN ITCDWNLVGT RPNSWQFTCT DLWETCVHHS MYLQPPLVDS PVLVHRIDLF PLSQETSGFY VDEIIIADTN ITVSQADSET AHPGGNLVES LCVVGSPPVY NISFWLVGCG QELPLITASI VPTGGEARRS GLVQVTTQRI QKTSPPLGGY FHIQLPTSVI PDVPVHISAS HLRKLLQNNA DNFTSRYLNS SDLTVMEDLK SCYEHEWTLS WSSQVGDLPN FIRVSDANLT GVNPAATVRV VYDGGVFLGP VFGDMLVTAN QHTQVVVRVN DIPAHCSGSC SFQYLEGSTP QIHSAWYSLD GDISLLIYIF GINFSGDPQA LEIMVNKTNC KVIFSNQTNV ICQTDLLPVG MHRLFMVVRP FGRAINTSGE ALFLSVEPRL DAVEPSRAAE IGGLWATIQG SGLEDVSLVL FGSQSCAINI TTSNSRRIQC RVPPRGKDGP VVNLTVVSGD HSAVLPMAFT YVSSLNPVIT SLSRNRSNIA GGDTLFIRMA LLVNYTDLDV EVCIQNTLAP AHVQMPQGLE VVLPPLPAGL YSISVSINGI SIRSPGVDLH IQYITEVFSI EPCCGSLLGG TILSISGIGF IRDPTLVWVF VGNRSCDILN STETVIWCET PPAALLPDSN IPAIPVPMEI WAGNVSFARE SLLNLSFTFL YEAAMTPVVT AMRGEIINNS LRFYVEGNNL SNSVILLGVS HCDLETQTLR NNVSLSGCSF PLHSLEAGFY PLQVRQKQMG FANMSAVPQQ YVITPWIMAI SPTHGSACGG TVLTVRGLAL SSRKRSVQVD LLGPFTCVIL SLGHQTILCQ INKVNDSFPD VSFTLNVTVI VNGLPSECQG NCTLFLQEET TPIVDSLTTN ISGSLTMVLI RGRKLGITAV EPMVFVDDHL PCIVTFFNAS YVICWISDLT PGLHYVSVFH ARNGYACFGN VSRHFYILPQ VFHYFPKNFS IHGGSLLTVE GTALRGKNST LVYVGQQACL TVSISTELIQ CIVPAGNGSV GLVIEVDGLS YQMGVIGYSS AFTPRLLSIS QTDDVLTFAV AQVSGAENVD IFIGMSPCVG ISGNHTVLQC VVSSLPAGEY PVRGYDRMRG WASSVLVFTS TATISGVTEN FGCLGGRLVH VFGAGFSPGN VSAAVCGAPC QVLANATVSA FSCLVLPLNV SLAFLCGLKH SEESCEASSS TYVQCDLTVT VGTETLPQSW PYLYICEESP QCLFAPDHWT ESTFPWFSGL FISPKVERDE VLIYNSSCNI AMETEAKMEC ETPNQPITAK ITEIRKSRGQ STQGNFSLQF CLRWSRTHSW FPERVPQDGD NVTVENGQLL LLDTNTSILN LLHIKGGKLI FMDPGPIELR AHAILISDGG ELRIGSEDKP FQGKAEIKLY GSSHSTPFFP YGVKFLAVRN GTLSLHGLLP EVTFTHLQAA AYAGDTVLAL EDAVDWHPGD EAVIISRIGV GGAKPMEEIV IVEAVHNTDL YLRSPLRYSH NFTENWVAGV LHILKVTVVL LSRSITIQGN LTAERMKHLA SCQEASDSEG NLQDCLYSKS EKMLGSRDLG ARVIVQSFPE EPSRVQLRGV QFRDLGQAFR KHVSALTLVG AMRDSYVQGC TVWSSFNRGL SMSMTLGLKV DSNIFYNILG HALLVGTDMD IKYISWEAAP EKKPDWSEQG NIIRNNVIIS ISGTEGLSSP EMLTPSGIYI LNPTNVVEGN RVYVAGLGYF FHLVTSQTSQ APLLSFTQNI AHSCTRYGLF IYPQFQPPWD DGRGPTLFQN FTVWGSAGGA RISRSSNLHL KNFQVYSCRD FGIDILESDA NTSVTDSLLL GHFAHKGSLC MSAGIKTPKR WELIISNTTF VNFDLTDCVS IRTCSGCSRG QGGFTVKTNQ LKFINSPNLV AFPFPHAAIL EDLDGSLSGR NRSHILASME TLSASCLVNL SFSQIVPGSV CGEDVIFHHM SIGLANAPNV SYDLTITDSR NKTTTVNYVR DTLSNLYGWM ALLLDQETYS LQFETPWISR SLQYSATFGS FAPGNYLLLV HTVLWPYPDI LVRCGSQEGR SLPSLPLPGQ DQGCDWFFNT QLRQLIYLVS GEGQVQVTLQ VKEGVPPTIS ASTSAPESAL KWSLPEAWTG IEEGWGGHNH TIPGPGDDIL ILPNRTVLVD TNLPFLKGLY VMGTLEFPVD RSNVLSVACM VIAGGELKVG TLDNPLEKEQ KLLILLRASE GIFCDRLNGI HIDPGTIGVY GKVQLHGACP KKSWTRLAAD IASGNERIIV EDAVDWRPHD KIVLSSSSYE PHEAEILTVK EVQAHHVKIY ERLKYRHIGS VHVMEDGRCI RLAAEVGLLT RNIQIQPDIS CRARLLVGSF RNSSSKEFSG VLQLSNVEIQ NFGSPLYSSI EFTNASAGSW IISSSLHQSC SGGIRAAASH GIILNDNIVF GTVGHGIDLE GQNFSLSNNL VVLMTQSAWS TVWVAGIKAN QAKDINLYGN VVAGSERIGF HIQGHRCSSP EARWSDNVAH SSLHGLHLYK ENGLDNCTGI SGFLAFKNFD YGAMLHVENS VEIENITLVD NSIGLLATVY VSSVPKSHIE NVQIVLRNSV IIATSSSFDC IQDRVKPRSA NLTSSDRAPS NPRGGRVGIL WPIFTSEPNW WPQEPWHRVR NGHSTSGILK LQDVTFSNFV KSCYSDDLDI CILPNVENTG IMHPIMAEGT RMLKIKDKNK FYFPPLQARK GLGILVCPES DCENPRKYLF KDLDGRALGL PPPVSVFPKT EAEWTGSFFN TGTFREEQKC TYRALIQGYI CKQSDQAILI LDNADATWAM QKLYPVVSVT RGFVDTFSSV NADAPCSTSG SASTFYSILP TREITKICFV DQTPQVLRFF LLGNRSTSKL LLAVFYHELQ NPRVFIGESF IPPIMVQSTS SLLDESIGSN YFSILDNLLY VVLQGQEPIE IHSGVSIHLA LTVMFSVLEK GWEIIILERL TDFLQVSQDQ IRFIHEMPGN EATLKAIADN KAKRKRNCPT VTCASPYRVG QRRPLMTEMS SYRVPSPTIM ETASKVIVIE IGDLPTIRST RLISYLTSNK LQNLAHQIIT AQQTGVLENV LNMTIGALLV TQPKGVTDYG NASSFKTGNF IYIRPYALSV LVQPSDGEVG KELTVQPRLV FLDKQNQRIE SLGPPSEPWA ISVSLEGTSD PVLKGCTQAE SQDGYVSFSN LAVLISGSNW HFIFTVTSPP GANFTARSRS FTVLPAAPSE KSSIILAVSL CSVASWLALC CLVCCWFRKS KSRKIKSEDI SEFKTNDQKS HIHMSSKHPR SQETKKEDTM MGEDMKIKVI MDKVNQLPHQ SLNGVSRRKV SRRAVREEGS SREEDVVPAP RIISITSQGH TCVPGSPDQQ IYLQEAGNWK EAQEQLVSYQ LAGQDQRLLL CPDLRRERQQ LQGQSQLGQE GGSVGLSQEK KASGGATQAS CPHLVHPETI QEQL //