PKHD1_CANLF
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 03-AUG-2022, entry version 82.
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}.
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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 eggNOG; ENOG502QR85; Eukaryota.
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 adult mammalian kidney and 8 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
