DZIP1_HUMAN
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 03-AUG-2022, entry version 154.
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}; 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};
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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; 30.
DR CORUM; Q86YF9; -.
DR DIP; DIP-35710N; -.
DR IntAct; Q86YF9; 19.
DR MINT; Q86YF9; -.
DR STRING; 9606.ENSP00000257312; -.
DR iPTMnet; Q86YF9; -.
DR PhosphoSitePlus; Q86YF9; -.
DR BioMuta; DZIP1; -.
DR DMDM; 50400485; -.
DR EPD; Q86YF9; -.
DR MassIVE; Q86YF9; -.
DR PaxDb; Q86YF9; -.
DR PeptideAtlas; Q86YF9; -.
DR PRIDE; Q86YF9; -.
DR ProteomicsDB; 70410; -. [Q86YF9-1]
DR ProteomicsDB; 70411; -. [Q86YF9-2]
DR ProteomicsDB; 70412; -. [Q86YF9-3]
DR Antibodypedia; 24832; 130 antibodies from 22 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 CTD; 22873; -.
DR DisGeNET; 22873; -.
DR GeneCards; DZIP1; -.
DR HGNC; HGNC:20908; DZIP1.
DR HPA; ENSG00000134874; Low tissue specificity.
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; DCEQSKE; -.
DR OrthoDB; 1162102at2759; -.
DR PhylomeDB; Q86YF9; -.
DR TreeFam; TF330044; -.
DR PathwayCommons; Q86YF9; -.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR SignaLink; Q86YF9; -.
DR BioGRID-ORCS; 22873; 7 hits in 1076 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 181 other tissues.
DR Genevisible; Q86YF9; HS.
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:0043393; P:regulation of protein binding; IEA:Ensembl.
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 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; 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
