DZIP1_MOUSE
ID DZIP1_MOUSE Reviewed; 852 AA.
AC Q8BMD2; Q4QQM0; Q6ZQ10; Q9CRK5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cilium assembly protein DZIP1 {ECO:0000305|PubMed:23955340};
DE AltName: Full=DAZ-interacting protein 1 homolog {ECO:0000250|UniProtKB:Q86YF9};
DE AltName: Full=DAZ-interacting zinc finger protein 1 {ECO:0000312|MGI:MGI:1914311};
GN Name=Dzip1 {ECO:0000312|MGI:MGI:1914311}; Synonyms=Kiaa0996;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-502 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 233-852 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Mesonephros;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15081113; DOI=10.1016/j.ygeno.2003.11.005;
RA Moore F.L., Jaruzelska J., Dorfman D.M., Reijo-Pera R.A.;
RT "Identification of a novel gene, DZIP (DAZ-interacting protein), that
RT encodes a protein that interacts with DAZ (deleted in azoospermia) and is
RT expressed in embryonic stem cells and germ cells.";
RL Genomics 83:834-843(2004).
RN [5]
RP FUNCTION, INTERACTION WITH CEP164; GLI3 AND IFT88, SUBCELLULAR LOCATION,
RP AND REGION.
RX PubMed=23955340; DOI=10.1074/jbc.m113.492066;
RA Wang C., Low W.C., Liu A., Wang B.;
RT "Centrosomal protein DZIP1 regulates Hedgehog signaling by promoting
RT cytoplasmic retention of transcription factor GLI3 and affecting
RT ciliogenesis.";
RL J. Biol. Chem. 288:29518-29529(2013).
RN [6]
RP FUNCTION, INTERACTION WITH GDI2 AND RAB8A, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT SER-520 BY GSK3-BETA, REGION, AND MUTAGENESIS OF
RP SER-520.
RX PubMed=25860027; DOI=10.1371/journal.pbio.1002129;
RA Zhang B., Zhang T., Wang G., Wang G., Chi W., Jiang Q., Zhang C.;
RT "GSK3beta-Dzip1-Rab8 cascade regulates ciliogenesis after mitosis.";
RL PLoS Biol. 13:e1002129-e1002129(2015).
RN [7]
RP FUNCTION, SUBUNIT, INTERACTION WITH PCM1, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT SER-210 BY PLK1, REGION, AND MUTAGENESIS OF SER-210.
RX PubMed=27979967; DOI=10.1074/jbc.m116.765438;
RA Zhang B., Wang G., Xu X., Yang S., Zhuang T., Wang G., Ren H., Cheng S.Y.,
RA Jiang Q., Zhang C.;
RT "DAZ-interacting Protein 1 (Dzip1) Phosphorylation by Polo-like Kinase 1
RT (Plk1) Regulates the Centriolar Satellite Localization of the BBSome
RT Protein during the Cell Cycle.";
RL J. Biol. Chem. 292:1351-1360(2017).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-14.
RX PubMed=31118289; DOI=10.1126/scitranslmed.aax0290;
RA Toomer K.A., Yu M., Fulmer D., Guo L., Moore K.S., Moore R., Drayton K.D.,
RA Glover J., Peterson N., Ramos-Ortiz S., Drohan A., Catching B.J.,
RA Stairley R., Wessels A., Lipschutz J.H., Delling F.N., Jeunemaitre X.,
RA Dina C., Collins R.L., Brand H., Talkowski M.E., Del Monte F.,
RA Mukherjee R., Awgulewitsch A., Body S., Hardiman G., Hazard E.S.,
RA da Silveira W.A., Wang B., Leyne M., Durst R., Markwald R.R.,
RA Le Scouarnec S., Hagege A., Le Tourneau T., Kohl P., Rog-Zielinska E.A.,
RA Ellinor P.T., Levine R.A., Milan D.J., Schott J.J., Bouatia-Naji N.,
RA Slaugenhaupt S.A., Norris R.A.;
RT "Primary cilia defects causing mitral valve prolapse.";
RL Sci. Transl. Med. 11:0-0(2019).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32051257; DOI=10.1136/jmedgenet-2019-106479;
RA Lv M., Liu W., Chi W., Ni X., Wang J., Cheng H., Li W.Y., Yang S., Wu H.,
RA Zhang J., Gao Y., Liu C., Li C., Yang C., Tan Q., Tang D., Zhang J.,
RA Song B., Chen Y.J., Li Q., Zhong Y., Zhang Z., Saiyin H., Jin L., Xu Y.,
RA Zhou P., Wei Z., Zhang C., He X., Zhang F., Cao Y.;
RT "Homozygous mutations in DZIP1 can induce asthenoteratospermia with severe
RT MMAF.";
RL J. Med. Genet. 57:445-453(2020).
CC -!- FUNCTION: Molecular adapter that recruits protein complexes required
CC for cilium assembly and function to the cilium basal body
CC (PubMed:23955340, PubMed:25860027, PubMed:31118289, PubMed:32051257).
CC At the exit of mitosis, localizes to the basal body and ciliary base of
CC the forming primary cilium where it recruits and activates RAB8A to
CC direct vesicle-mediated transport of proteins to the cilium
CC (PubMed:25860027). Also recruits the BBSome, a complex involved in
CC cilium biogenesis, by bridging it to PCM1 at the centriolar satellites
CC of the cilium (PubMed:27979967). It is also required for the
CC recruitment to the cilium basal body of the intraflagellar transport
CC (IFT) machinery as well as the ciliary appendage proteins CEP164 and
CC NINEIN (PubMed:23955340). Functions as a regulator of Hedgehog
CC signaling both through its role in cilium assembly but also probably
CC through its ability to retain GLI3 within the cytoplasm
CC (PubMed:23955340). It is involved in spermatogenesis through its role
CC in organization of the basal body and assembly of the sperm flagellum
CC (PubMed:32051257). Also indirectly involved in heart development
CC through its function in ciliogenesis (PubMed:31118289).
CC {ECO:0000269|PubMed:23955340, ECO:0000269|PubMed:25860027,
CC ECO:0000269|PubMed:27979967, ECO:0000269|PubMed:31118289,
CC ECO:0000269|PubMed:32051257}.
CC -!- SUBUNIT: Interacts with DAZ1 (By similarity). Interacts with the
CC BBSome; recruits the BBSome to centriolar satellites of the cilium
CC (PubMed:27979967). Interacts with PCM1; localizes DZIP1 and the
CC associated BBSome to centriolar satellites (PubMed:27979967). Interacts
CC with RAB8A (GDP-bound inactive form); recruits RAB8A to the basal body
CC of the cilium and prevents its inhibition by GDI2 (PubMed:25860027).
CC Interacts with GDI2; negatively regulates the interaction of GDI2 with
CC GDP-bound RAB8A (PubMed:25860027). Interacts with GLI3; retains GLI3
CC within the cytoplasm (PubMed:23955340). Interacts with CEP164
CC (PubMed:23955340). Interacts with IFT88 (PubMed:23955340).
CC {ECO:0000250|UniProtKB:Q86YF9, ECO:0000269|PubMed:23955340,
CC ECO:0000269|PubMed:25860027, ECO:0000269|PubMed:27979967}.
CC -!- INTERACTION:
CC Q8BMD2; Q61598: Gdi2; NbExp=2; IntAct=EBI-7089968, EBI-6665490;
CC Q8BMD2; P55258: Rab8a; NbExp=2; IntAct=EBI-7089968, EBI-398411;
CC Q8BMD2; P50395: GDI2; Xeno; NbExp=2; IntAct=EBI-7089968, EBI-1049143;
CC Q8BMD2-1; P50395: GDI2; Xeno; NbExp=3; IntAct=EBI-16153101, EBI-1049143;
CC Q8BMD2-1; P49841-2: GSK3B; Xeno; NbExp=3; IntAct=EBI-16153101, EBI-15870655;
CC Q8BMD2-1; P61007: RAB8A; Xeno; NbExp=3; IntAct=EBI-16153101, EBI-7473289;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:23955340, ECO:0000269|PubMed:25860027,
CC ECO:0000269|PubMed:31118289}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:27979967}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:25860027}.
CC Nucleus {ECO:0000269|PubMed:15081113}. Nucleus speckle
CC {ECO:0000269|PubMed:31118289}. Cytoplasm {ECO:0000269|PubMed:15081113}.
CC Note=Localizes to the centriole in cells lacking cilia and to the
CC cilium basal body in ciliated cells (By similarity). At the exit of
CC mitosis, when the primary cilium is reassembled in daughter cells,
CC localizes at the mother centriole that acts as the basal body of the
CC assembling primary cilium and also accumulates at the ciliary base that
CC constitutes a diffusion barrier for ciliary proteins (PubMed:25860027).
CC {ECO:0000250|UniProtKB:Q86YF9, ECO:0000269|PubMed:25860027}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BMD2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BMD2-2; Sequence=VSP_010967, VSP_010968, VSP_010969;
CC Name=3;
CC IsoId=Q8BMD2-3; Sequence=VSP_010966;
CC -!- TISSUE SPECIFICITY: Expressed in testis and undifferentiated ES cells.
CC {ECO:0000269|PubMed:15081113}.
CC -!- PTM: Phosphorylation at Ser-210 by PLK1 before mitosis prevents
CC interaction with PCM1 and localization to centriolar satellites.
CC Thereby, it negatively regulates the localization of the BBSome to
CC centriolar satellites (PubMed:27979967). Undergoes postmitotic
CC phosphorylation at Ser-520 by GSK3B. That phosphorylated form of DZIP1
CC interacts with GDI2, disrupting its interaction with RAB8A, leading to
CC RAB8A activation and localization to the cilium where it mediates
CC protein transport and participates to cilium biogenesis
CC (PubMed:25860027). {ECO:0000269|PubMed:25860027,
CC ECO:0000269|PubMed:27979967}.
CC -!- DISRUPTION PHENOTYPE: Male animals were all infertile. Few spermatozoa
CC were collected from the epididymides of the mutant, and no motile
CC spermatozoa were seen. Light microscopy of the mutant spermatozoa
CC showed severe morphologic abnormalities, primarily absent flagella as
CC well as residual cytoplasm and abnormal heads.
CC {ECO:0000269|PubMed:32051257}.
CC -!- SIMILARITY: Belongs to the DZIP C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98066.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129256; BAC98066.1; ALT_INIT; mRNA.
DR EMBL; BC098211; AAH98211.1; -; mRNA.
DR EMBL; AK021163; BAB32310.1; -; mRNA.
DR EMBL; AK032834; BAC28050.1; -; mRNA.
DR CCDS; CCDS37011.1; -. [Q8BMD2-1]
DR RefSeq; NP_080219.2; NM_025943.3. [Q8BMD2-1]
DR RefSeq; XP_006519446.1; XM_006519383.2. [Q8BMD2-1]
DR RefSeq; XP_006519447.1; XM_006519384.2. [Q8BMD2-1]
DR RefSeq; XP_006519454.1; XM_006519391.3. [Q8BMD2-3]
DR RefSeq; XP_011243448.1; XM_011245146.2. [Q8BMD2-1]
DR RefSeq; XP_017171615.1; XM_017316126.1. [Q8BMD2-3]
DR AlphaFoldDB; Q8BMD2; -.
DR SMR; Q8BMD2; -.
DR DIP; DIP-61407N; -.
DR IntAct; Q8BMD2; 9.
DR MINT; Q8BMD2; -.
DR STRING; 10090.ENSMUSP00000039689; -.
DR iPTMnet; Q8BMD2; -.
DR PhosphoSitePlus; Q8BMD2; -.
DR MaxQB; Q8BMD2; -.
DR PaxDb; Q8BMD2; -.
DR PRIDE; Q8BMD2; -.
DR ProteomicsDB; 277430; -. [Q8BMD2-1]
DR ProteomicsDB; 277431; -. [Q8BMD2-2]
DR ProteomicsDB; 277432; -. [Q8BMD2-3]
DR Antibodypedia; 24832; 130 antibodies from 22 providers.
DR DNASU; 66573; -.
DR Ensembl; ENSMUST00000004055; ENSMUSP00000004055; ENSMUSG00000042156. [Q8BMD2-1]
DR Ensembl; ENSMUST00000047208; ENSMUSP00000039689; ENSMUSG00000042156. [Q8BMD2-1]
DR GeneID; 66573; -.
DR KEGG; mmu:66573; -.
DR UCSC; uc007uyy.1; mouse. [Q8BMD2-3]
DR UCSC; uc007uza.2; mouse. [Q8BMD2-1]
DR CTD; 22873; -.
DR MGI; MGI:1914311; Dzip1.
DR VEuPathDB; HostDB:ENSMUSG00000042156; -.
DR eggNOG; ENOG502QRAI; Eukaryota.
DR GeneTree; ENSGT00940000156862; -.
DR HOGENOM; CLU_018051_1_0_1; -.
DR InParanoid; Q8BMD2; -.
DR OMA; DCEQSKE; -.
DR OrthoDB; 1162102at2759; -.
DR PhylomeDB; Q8BMD2; -.
DR TreeFam; TF330044; -.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR BioGRID-ORCS; 66573; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Dzip1; mouse.
DR PRO; PR:Q8BMD2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BMD2; protein.
DR Bgee; ENSMUSG00000042156; Expressed in embryonic brain and 223 other tissues.
DR Genevisible; Q8BMD2; MM.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0097539; C:ciliary transition fiber; IMP:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0062063; F:BBSome binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0044782; P:cilium organization; IMP:MGI.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0032507; P:maintenance of protein location in cell; IMP:MGI.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; IMP:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; IDA:MGI.
DR GO; GO:0033365; P:protein localization to organelle; IMP:MGI.
DR GO; GO:0140706; P:protein-containing complex localization to centriolar satellite; ISS:UniProtKB.
DR GO; GO:0043393; P:regulation of protein binding; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0120316; P:sperm flagellum assembly; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR032714; DZIP1_N.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF13815; Dzip-like_N; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Spermatogenesis; Zinc; Zinc-finger.
FT CHAIN 1..852
FT /note="Cilium assembly protein DZIP1"
FT /id="PRO_0000047107"
FT ZN_FING 183..206
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..351
FT /note="Mediates interaction with GLI3 and localization to
FT the cilium basal body"
FT /evidence="ECO:0000269|PubMed:23955340"
FT REGION 1..188
FT /note="Mediates interaction with PCM1"
FT /evidence="ECO:0000269|PubMed:27979967"
FT REGION 139..262
FT /note="Required for interaction with DAZ1"
FT /evidence="ECO:0000250|UniProtKB:Q86YF9"
FT REGION 430..600
FT /note="Mediates interaction with GDI2 and RAB8A"
FT /evidence="ECO:0000305|PubMed:25860027"
FT REGION 434..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 214..307
FT /evidence="ECO:0000255"
FT COILED 385..429
FT /evidence="ECO:0000255"
FT COILED 488..508
FT /evidence="ECO:0000255"
FT COMPBIAS 489..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:27979967"
FT MOD_RES 520
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:25860027"
FT VAR_SEQ 1..228
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010966"
FT VAR_SEQ 309
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_010967"
FT VAR_SEQ 771..798
FT /note="CTDADDEDWDISSLEEEKSLGSKIEQRE -> FGSVGRQLWSLSVLSDSRCG
FT LNNVRSEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_010968"
FT VAR_SEQ 799..852
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_010969"
FT MUTAGEN 14
FT /note="S->R: Changed cilium assembly. Adult animals develop
FT myxomatous mitral valves and functional mitral valve
FT prolapse."
FT /evidence="ECO:0000269|PubMed:31118289"
FT MUTAGEN 210
FT /note="S->A: Loss of phosphorylation by PLK1. Increased
FT interaction with PCM1."
FT /evidence="ECO:0000269|PubMed:27979967"
FT MUTAGEN 210
FT /note="S->D: Loss of interaction with PCM1."
FT /evidence="ECO:0000269|PubMed:27979967"
FT MUTAGEN 520
FT /note="S->A: Loss of phosphorylation by GSK3-beta.
FT Decreased interaction with GDI2."
FT /evidence="ECO:0000269|PubMed:25860027"
FT MUTAGEN 520
FT /note="S->D: Phosphorylation mimicking mutant. Increased
FT interaction with GDI2."
FT /evidence="ECO:0000269|PubMed:25860027"
FT CONFLICT 118
FT /note="H -> Y (in Ref. 3; BAC28050)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="M -> I (in Ref. 3; BAC28050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 97263 MW; BF786BAE227DBD47 CRC64;
MPFQKHVYYP LANSPEGPDA SAIGAAPMAF VPPSAASGPL PFFQFRPRLE SVDWRRLSAI
DVDKVAGAVD VLTLQENIMN ITFCKLEDEK CPHCQSGVDP VLLKLIRLAQ LTIEYLMHSQ
EFLTSQLNLV EERLRLSLLD YEQSKQLLTK QAGEIKLLKE ECKRRKKMLS TQQLMIEAKA
SYYQCHFCDK AFMNQAFLQS HIQRRHTEDS HLEYNTKAQT DRLQKEIDML KEQLQLTRSQ
LESAQHSHAV RFSKDYEMQK SKEEDFLKLF DRWKEEEKEK LLEEMEKVKG MFMREFKELT
SKNSALEYQL LEIQKSNIQI KSNIGTLRDV TELREDHLPC PQDFQNMLQL LDSQASKWTD
RFQVLNEEHS KEKGQLLSHI EKLRSSMMKD LSADNVFYKR RVEELGQKLQ EQNELIISQK
QQIREFASKP YSSISELKGT PLTRQTLEPK SAAPTTPMTA SATQNLDGAS SLTMVHEQVF
SSHILEPIEE LSSEEEKGRE NEQKLNKKTS LRKPSSTSPS PQELRTNLER ELGNKLRSFG
IGANIQGIPC EILNRSLKAM QVARHDLAKQ MPDIQQIRES LEHQLICKME EKVSLSSDRH
HVPSMTTFPP EEVPKATQLP HKSRPLVRQR TVFTDKVSVP KLKKNTKESH FLRRFPSTKT
PPFSSEEEPD EEDLLHAYLS PDSLATAATQ PPKSSMSHFG KSAVKSDTDW TEGSEMDDSD
FSPKLTGTSI TIQTDTVETM ALPQGSGNKA VPGMNPADTV IKKESLQELK CTDADDEDWD
ISSLEEEKSL GSKIEQREPP PAKRDPSCTQ VQRAWGPVNP REFKEEGLHE NEPSTLKSNL
VTVTDWSDVL DV
