ID DZIP1_HUMAN Reviewed; 867 AA. AC Q86YF9; Q5W078; Q5W079; Q8WY45; Q8WY46; Q9UGA5; Q9Y2K0; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 163. DE RecName: Full=Cilium assembly protein DZIP1 {ECO:0000305|PubMed:19852954}; DE AltName: Full=DAZ-interacting protein 1/2 {ECO:0000303|PubMed:12511597}; DE AltName: Full=DAZ-interacting zinc finger protein 1 {ECO:0000312|HGNC:HGNC:20908}; GN Name=DZIP1 {ECO:0000312|HGNC:HGNC:20908}; GN Synonyms=DZIP, DZIP2, KIAA0996; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE OF 1-776 RP (ISOFORM 1), AND INTERACTION WITH DAZ1. RX PubMed=12511597; DOI=10.1073/pnas.0234478100; RA Moore F.L., Jaruzelska J., Fox M.S., Urano J., Firpo M.T., Turek P.J., RA Dorfman D.M., Reijo Pera R.A.; RT "Human Pumilio-2 is expressed in embryonic stem cells and germ cells and RT interacts with DAZ (Deleted in AZoospermia) and DAZ-like proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 100:538-543(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 615-867, AND VARIANT SER-736. RC TISSUE=Brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP INTERACTION WITH DAZ1, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE RP SPECIFICITY, AND REGION. 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 [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19852954; DOI=10.1016/j.ydbio.2009.10.025; RA Glazer A.M., Wilkinson A.W., Backer C.B., Lapan S.W., Gutzman J.H., RA Cheeseman I.M., Reddien P.W.; RT "The Zn finger protein Iguana impacts Hedgehog signaling by promoting RT ciliogenesis."; RL Dev. Biol. 337:148-156(2010). RN [8] RP FUNCTION, AND INTERACTION WITH GLI3. 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 [9] RP INTERACTION WITH GDI2 AND RAB8A. 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 [10] RP FUNCTION, SUBUNIT, INTERACTION WITH PCM1, AND SUBCELLULAR LOCATION. 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 [11] RP INVOLVEMENT IN MVP3, VARIANT MVP3 ARG-24, CHARACTERIZATION OF VARIANT MVP3 RP ARG-24, AND FUNCTION. 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 [12] RP INVOLVEMENT IN SPGF47, VARIANTS SPGF47 GLN-63 AND 230-TYR--VAL-867 DEL, RP CHARACTERIZATION OF VARIANTS SPGF47 GLN-63 AND 230-TYR--VAL-867 DEL, RP FUNCTION, AND TISSUE SPECIFICITY. 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:19852954, PubMed:23955340, PubMed:27979967, 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 (By CC similarity). Also recruits the BBSome, a complex involved in cilium CC biogenesis, by bridging it to PCM1 at the centriolar satellites of the CC cilium (PubMed:27979967). It is also required for the recruitment to CC the cilium basal body of the intraflagellar transport (IFT) machinery CC as well as the ciliary appendage proteins CEP164 and NINEIN (By CC similarity). Functions as a regulator of Hedgehog signaling both CC through its role in cilium assembly but also probably through its CC ability to retain GLI3 within the cytoplasm (By similarity). It is CC involved in spermatogenesis through its role in organization of the CC basal body and assembly of the sperm flagellum (PubMed:32051257). Also CC indirectly involved in heart development through its function in CC ciliogenesis (PubMed:31118289). {ECO:0000250|UniProtKB:Q8BMD2, CC ECO:0000269|PubMed:19852954, ECO:0000269|PubMed:23955340, CC ECO:0000269|PubMed:27979967, ECO:0000269|PubMed:31118289, CC ECO:0000269|PubMed:32051257}. CC -!- SUBUNIT: Interacts with DAZ1 (PubMed:12511597, PubMed:15081113). CC Interacts with the BBSome; recruits the BBSome to centriolar satellites CC of the cilium (PubMed:27979967). Interacts with PCM1; localizes DZIP1 CC and the associated BBSome to centriolar satellites (PubMed:27979967). CC Interacts with RAB8A (GDP-bound inactive form); recruits RAB8A to the CC basal body of the cilium and prevents its inhibition by GDI2 CC (PubMed:25860027). Interacts with GDI2; negatively regulates the CC interaction of GDI2 with GDP-bound RAB8A (PubMed:25860027). Interacts CC with GLI3; retains GLI3 within the cytoplasm (PubMed:23955340). CC Interacts with CEP164 (By similarity). Interacts with IFT88 (By CC similarity). {ECO:0000250|UniProtKB:Q8BMD2, CC ECO:0000269|PubMed:12511597, ECO:0000269|PubMed:15081113, CC ECO:0000269|PubMed:23955340, ECO:0000269|PubMed:25860027, CC ECO:0000269|PubMed:27979967}. CC -!- INTERACTION: CC Q86YF9; Q9Y383: LUC7L2; NbExp=3; IntAct=EBI-998108, EBI-352851; CC Q86YF9; P00540: MOS; NbExp=3; IntAct=EBI-998108, EBI-1757866; CC Q86YF9; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-998108, EBI-2557469; CC Q86YF9; Q15172: PPP2R5A; NbExp=4; IntAct=EBI-998108, EBI-641666; CC Q86YF9; Q16537: PPP2R5E; NbExp=3; IntAct=EBI-998108, EBI-968374; CC Q86YF9; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-998108, EBI-5280197; CC Q86YF9; Q63HR2: TNS2; NbExp=3; IntAct=EBI-998108, EBI-949753; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body CC {ECO:0000269|PubMed:19852954}. 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:19852954}. CC Nucleus {ECO:0000269|PubMed:15081113}. Nucleus speckle CC {ECO:0000250|UniProtKB:Q8BMD2}. Cytoplasm CC {ECO:0000269|PubMed:15081113}. Note=Localizes to the centriole in cells CC lacking cilia and to the cilium basal body in ciliated cells CC (PubMed:19852954). At the exit of mitosis, when the primary cilium is CC reassembled in daughter cells, localizes at the mother centriole that CC acts as the basal body of the assembling primary cilium and also CC accumulates at the ciliary base that constitutes a diffusion barrier CC for ciliary proteins (By similarity). {ECO:0000250|UniProtKB:Q8BMD2, CC ECO:0000269|PubMed:19852954}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=DZIPt2 {ECO:0000303|PubMed:15081113}, DZIP testis2 CC {ECO:0000303|PubMed:15081113}; CC IsoId=Q86YF9-1; Sequence=Displayed; CC Name=2; Synonyms=DZIPt1 {ECO:0000303|PubMed:15081113}, DZIP testis1 CC {ECO:0000303|PubMed:15081113}; CC IsoId=Q86YF9-2; Sequence=VSP_010965; CC Name=3; Synonyms=DZIPb {ECO:0000303|PubMed:15081113}, DZIP brain CC {ECO:0000303|PubMed:15081113}; CC IsoId=Q86YF9-3; Sequence=VSP_010962, VSP_010963, VSP_010964; CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis (at protein CC level) (PubMed:15081113, PubMed:32051257). Also expressed in fetal CC brain, adult oocytes and ovary (PubMed:15081113). Expressed in CC undifferentiated ES cells (PubMed:15081113). In testis, it is CC specifically expressed in germ cells (at protein level) CC (PubMed:15081113, PubMed:32051257). Expressed in mature germ cells and CC secondary spermatocytes, while it is weakly or not expressed in primary CC spermatocytes (PubMed:15081113). {ECO:0000269|PubMed:15081113, CC ECO:0000269|PubMed:32051257}. CC -!- PTM: Phosphorylation at Ser-226 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. {ECO:0000250|UniProtKB:Q8BMD2}. CC -!- DISEASE: Mitral valve prolapse 3 (MVP3) [MIM:610840]: An autosomal CC dominant form of mitral valve prolapse, a valvular heart disease CC characterized by abnormally elongated and thickened mitral valve CC leaflets, that typically show myxomatous degeneration with increased CC leaflet compliance. It is associated with mitral regurgitation. CC Myxomatous mitral valves have an abnormal layered architecture CC characterized by loose collagen in fibrosa, expanded spongiosa strongly CC positive for proteoglycans, and disrupted elastin in atrialis. In CC classic mitral valve prolapse, leaflets are at least 5 mm thick, CC whereas in the non-classic form, they are less than 5 mm thick. Severe CC classic mitral valve prolapse is strongly associated with arrhythmias, CC endocarditis, heart failure, and need for valve surgery. CC {ECO:0000269|PubMed:31118289}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Spermatogenic failure 47 (SPGF47) [MIM:619102]: An autosomal CC recessive infertility disorder caused by spermatogenesis defects CC resulting in asthenoteratozoospermia. SPGF47 is characterized by CC reduced sperm concentrations and immotile spermatozoa, with short or CC absent flagella as well as centriolar abnormalities. CC {ECO:0000269|PubMed:32051257}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the DZIP C2H2-type zinc-finger protein family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL36978.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA76840.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAB43211.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AF272347; AAL36978.1; ALT_SEQ; mRNA. DR EMBL; AF272348; AAL36979.1; -; mRNA. DR EMBL; AB023213; BAA76840.2; ALT_INIT; mRNA. DR EMBL; AL139376; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC041804; AAH41804.1; -; mRNA. DR EMBL; AL049931; CAB43211.2; ALT_INIT; mRNA. DR CCDS; CCDS9477.1; -. [Q86YF9-2] DR CCDS; CCDS9478.1; -. [Q86YF9-1] DR PIR; T08668; T08668. DR RefSeq; NP_055749.1; NM_014934.4. [Q86YF9-2] DR RefSeq; NP_945319.1; NM_198968.3. [Q86YF9-1] DR AlphaFoldDB; Q86YF9; -. DR SMR; Q86YF9; -. DR BioGRID; 116540; 38. DR CORUM; Q86YF9; -. DR DIP; DIP-35710N; -. DR IntAct; Q86YF9; 26. DR MINT; Q86YF9; -. DR STRING; 9606.ENSP00000257312; -. DR TCDB; 3.A.33.1.1; the bbsome complex (bbsome) family. DR GlyGen; Q86YF9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q86YF9; -. DR PhosphoSitePlus; Q86YF9; -. DR BioMuta; DZIP1; -. DR DMDM; 50400485; -. DR EPD; Q86YF9; -. DR MassIVE; Q86YF9; -. DR PaxDb; 9606-ENSP00000257312; -. DR PeptideAtlas; Q86YF9; -. DR ProteomicsDB; 70410; -. [Q86YF9-1] DR ProteomicsDB; 70411; -. [Q86YF9-2] DR ProteomicsDB; 70412; -. [Q86YF9-3] DR Antibodypedia; 24832; 151 antibodies from 23 providers. DR DNASU; 22873; -. DR Ensembl; ENST00000347108.7; ENSP00000257312.5; ENSG00000134874.18. [Q86YF9-1] DR Ensembl; ENST00000361156.7; ENSP00000355018.3; ENSG00000134874.18. [Q86YF9-2] DR Ensembl; ENST00000361396.6; ENSP00000355175.2; ENSG00000134874.18. [Q86YF9-2] DR Ensembl; ENST00000376829.7; ENSP00000366025.2; ENSG00000134874.18. [Q86YF9-1] DR Ensembl; ENST00000466569.1; ENSP00000431168.1; ENSG00000134874.18. [Q86YF9-3] DR GeneID; 22873; -. DR KEGG; hsa:22873; -. DR MANE-Select; ENST00000376829.7; ENSP00000366025.2; NM_198968.4; NP_945319.1. DR UCSC; uc001vmk.5; human. [Q86YF9-1] DR AGR; HGNC:20908; -. DR CTD; 22873; -. DR DisGeNET; 22873; -. DR GeneCards; DZIP1; -. DR HGNC; HGNC:20908; DZIP1. DR HPA; ENSG00000134874; Tissue enhanced (brain). DR MalaCards; DZIP1; -. DR MIM; 608671; gene. DR MIM; 610840; phenotype. DR MIM; 619102; phenotype. DR neXtProt; NX_Q86YF9; -. DR OpenTargets; ENSG00000134874; -. DR PharmGKB; PA134960194; -. DR VEuPathDB; HostDB:ENSG00000134874; -. DR eggNOG; ENOG502QRAI; Eukaryota. DR GeneTree; ENSGT00940000156862; -. DR HOGENOM; CLU_018051_1_0_1; -. DR InParanoid; Q86YF9; -. DR OMA; TWQAFES; -. DR OrthoDB; 2914439at2759; -. DR PhylomeDB; Q86YF9; -. DR TreeFam; TF330044; -. DR PathwayCommons; Q86YF9; -. DR Reactome; R-HSA-5632684; Hedgehog 'on' state. DR SignaLink; Q86YF9; -. DR BioGRID-ORCS; 22873; 9 hits in 1154 CRISPR screens. DR ChiTaRS; DZIP1; human. DR GeneWiki; DZIP1; -. DR GenomeRNAi; 22873; -. DR Pharos; Q86YF9; Tbio. DR PRO; PR:Q86YF9; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q86YF9; Protein. DR Bgee; ENSG00000134874; Expressed in sperm and 183 other cell types or tissues. DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB. DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL. DR GO; GO:0097546; C:ciliary base; IEA:Ensembl. DR GO; GO:0097539; C:ciliary transition fiber; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. 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; IMP:UniProtKB. DR GO; GO:0032053; P:ciliary basal body organization; IMP:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IMP:BHF-UCL. DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IEA:Ensembl. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl. DR GO; GO:0007281; P:germ cell development; IEP:UniProtKB. DR GO; GO:0007507; P:heart development; IMP:UniProtKB. DR GO; GO:0032507; P:maintenance of protein location in cell; IEA:Ensembl. DR GO; GO:0045724; P:positive regulation of cilium assembly; IEA:Ensembl. DR GO; GO:1903566; P:positive regulation of protein localization to cilium; IEA:Ensembl. DR GO; GO:0061512; P:protein localization to cilium; IEA:Ensembl. DR GO; GO:0140706; P:protein-containing complex localization to centriolar satellite; IDA:UniProtKB. DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl. DR GO; GO:0120316; P:sperm flagellum assembly; IMP:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR InterPro; IPR032714; DZIP1_N. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR21502:SF5; CILIUM ASSEMBLY PROTEIN DZIP1; 1. DR PANTHER; PTHR21502; ZINC FINGER PROTEIN DZIP1; 1. 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. DR Genevisible; Q86YF9; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; Cilium; KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton; KW Developmental protein; Differentiation; Disease variant; Metal-binding; KW Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis; Zinc; KW Zinc-finger. FT CHAIN 1..867 FT /note="Cilium assembly protein DZIP1" FT /id="PRO_0000047106" FT ZN_FING 198..221 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 12..367 FT /note="Mediates interaction with GLI3 and localization to FT the cilium basal body" FT /evidence="ECO:0000250|UniProtKB:Q8BMD2" FT REGION 12..203 FT /note="Mediates interaction with PCM1" FT /evidence="ECO:0000250|UniProtKB:Q8BMD2" FT REGION 154..278 FT /note="Required for interaction with DAZ1" FT /evidence="ECO:0000269|PubMed:15081113" FT REGION 446..617 FT /note="Mediates interaction with GDI2 and RAB8A" FT /evidence="ECO:0000250|UniProtKB:Q8BMD2" FT REGION 643..768 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 796..867 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 230..340 FT /evidence="ECO:0000255" FT COILED 401..445 FT /evidence="ECO:0000255" FT COILED 568..588 FT /evidence="ECO:0000255" FT COMPBIAS 643..657 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 721..737 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 798..819 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 843..867 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 226 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000250|UniProtKB:Q8BMD2" FT VAR_SEQ 12 FT /note="M -> MVRGGRPGRPRRGCRAGENRGFPGPPAPQPARPPSPPPAALSLCPPQ FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12511597" FT /id="VSP_010962" FT VAR_SEQ 229..231 FT /note="EYQ -> GHL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12511597" FT /id="VSP_010963" FT VAR_SEQ 232..867 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12511597" FT /id="VSP_010964" FT VAR_SEQ 455..474 FT /note="GNPLAWQAFESQPAAPAVPM -> V (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10231032" FT /id="VSP_010965" FT VARIANT 24 FT /note="S -> R (in MVP3; decreased protein stability)" FT /evidence="ECO:0000269|PubMed:31118289" FT /id="VAR_085517" FT VARIANT 63 FT /note="R -> Q (in SPGF47; decreased protein abundance; loss FT of sperm flagellum assembly)" FT /evidence="ECO:0000269|PubMed:32051257" FT /id="VAR_085518" FT VARIANT 172 FT /note="T -> M (in dbSNP:rs9561921)" FT /id="VAR_052710" FT VARIANT 230..867 FT /note="Missing (in SPGF47; decreased protein abundance; FT changed ciliary basal body organization; loss of sperm FT flagellum assembly)" FT /evidence="ECO:0000269|PubMed:32051257" FT /id="VAR_085519" FT VARIANT 664 FT /note="M -> L (in dbSNP:rs34303958)" FT /id="VAR_052711" FT VARIANT 736 FT /note="P -> S (in dbSNP:rs11070136)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_019456" FT CONFLICT 615 FT /note="D -> G (in Ref. 5; CAB43211)" FT /evidence="ECO:0000305" FT CONFLICT 818..819 FT /note="KN -> EK (in Ref. 5; CAB43211)" FT /evidence="ECO:0000305" SQ SEQUENCE 867 AA; 98664 MW; 4C5A7B9438D40623 CRC64; MQAEAADWFS SMPFQKHVYY PLASGPEGPD VAVAAAAAGA ASMACAPPSA ASGPLPFFQF RPRLESVDWR RLSAIDVDKV AGAVDVLTLQ ENIMNITFCK LEDEKCPHCQ SGVDPVLLKL IRLAQFTIEY LLHSQEFLTS QLHTLEERLR LSHCDGEQSK KLLTKQAGEI KTLKEECKRR KKMISTQQLM IEAKANYYQC HFCDKAFMNQ AFLQSHIQRR HTEENSHFEY QKNAQIEKLR SEIVVLKEEL QLTRSELEAA HHASAVRFSK EYEMQKTKEE DFLKLFDRWK EEEKEKLVDE MEKVKEMFMK EFKELTSKNS ALEYQLSEIQ KSNMQIKSNI GTLKDAHEFK EDRSPYPQDF HNVMQLLDSQ ESKWTARVQA IHQEHKKEKG RLLSHIEKLR TSMIDDLNAS NVFYKKRIEE LGQRLQEQNE LIITQRQQIK DFTCNPLNSI SEPKGNPLAW QAFESQPAAP AVPMNAPALH TLETKSSLPM VHEQAFSSHI LEPIEELSEE EKGRENEQKL NNNKMHLRKA LKSNSSLTKG LRTMVEQNLM EKLETLGINA DIRGISSDQL HRVLKSVESE RHKQEREIPN FHQIREFLEH QVSCKIEEKA LLSSDQCSVS QMDTLSTGEV PKMIQLPSKN RQLIRQKAVS TDRTSVPKIK KNVMEDPFPR KSSTITTPPF SSEEEQEDDD LIRAYASPGP LPVPPPQNKG SFGKNTVKSD ADGTEGSEIE DTDDSPKPAG VAVKTPTEKV EKMFPHRKNV NKPVGGTNVP EMFIKKEELQ ELKCADVEDE DWDISSLEEE ISLGKKSGKE QKEPPPAKNE PHFAHVLNAW GAFNPKGPKG EGLQENESST LKSSLVTVTD WSDTSDV //