DZIP1_DANRE
ID DZIP1_DANRE Reviewed; 898 AA.
AC Q7T019; Q8QFL8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cilium assembly protein DZIP1 {ECO:0000305};
DE AltName: Full=DAZ-interacting protein 1 homolog {ECO:0000250|UniProtKB:Q86YF9};
DE AltName: Full=DAZ-interacting zinc finger protein 1;
DE AltName: Full=Iguana protein;
GN Name=dzip1; Synonyms=igu; ORFNames=si:dz52i16.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15115751; DOI=10.1242/dev.01059;
RA Sekimizu K., Nishioka N., Sasaki H., Takeda H., Karlstrom R.O.,
RA Kawakami K.;
RT "The zebrafish iguana locus encodes Dzip1, a novel zinc-finger protein
RT required for proper regulation of Hedgehog signaling.";
RL Development 131:2521-2532(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15198976; DOI=10.1101/gad.296004;
RA Wolff C., Roy S., Lewis K.E., Schauerte H., Joerg-Rauch G., Kirn A.,
RA Weiler C., Geisler R., Haffter P., Ingham P.W.;
RT "Iguana encodes a novel zinc-finger protein with coiled-coil domains
RT essential for Hedgehog signal transduction in the zebrafish embryo.";
RL Genes Dev. 18:1565-1576(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Molecular adapter that recruits protein complexes required
CC for cilium assembly and function to the cilium basal body
CC (PubMed:19852954). Required for establishment of left-right asymmetry
CC during embryogenesis (PubMed:19852954). Acts as a permissive factor
CC that is required for the proper regulation of Hedgehog (Hh) target
CC genes in response to Hh signals (PubMed:15115751). Acts downstream of
CC the Smoothened protein to modulate Gli activity in the somites of the
CC developing embryo (PubMed:15198976). {ECO:0000269|PubMed:15115751,
CC ECO:0000269|PubMed:15198976, ECO:0000269|PubMed:19852954}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:19852954}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q86YF9}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q86YF9}. Nucleus {ECO:0000269|PubMed:15115751,
CC ECO:0000269|PubMed:15198976}. Cytoplasm {ECO:0000269|PubMed:15115751,
CC ECO:0000269|PubMed:15198976}. Note=In the cytoplasm, it is localized in
CC large vesicles. These vesicles correspond to lysosomes and/or
CC endosomes. Can shuttle between the cytoplasm and the nucleus in a
CC manner correlated with Hh activity. {ECO:0000269|PubMed:15115751}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7T019-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7T019-2; Sequence=VSP_010970;
CC -!- TISSUE SPECIFICITY: Expressed throughout the embryo starting at 12
CC hours. {ECO:0000269|PubMed:15115751}.
CC -!- DISRUPTION PHENOTYPE: Defects are a cause of reduced expression of Hh
CC target genes in the ventral neural tube, similar to the phenotype seen
CC in zebrafish mutants known to affect Hh signaling (PubMed:15115751,
CC PubMed:15198976). Reduced cilium number in pronephric duct and
CC Kupffer's vesicle (PubMed:19852954). Defects in left/right asymmetry,
CC characterized by abnormal heart location on right or center of body
CC (PubMed:19852954). {ECO:0000269|PubMed:15115751,
CC ECO:0000269|PubMed:15198976, ECO:0000269|PubMed:19852954}.
CC -!- SIMILARITY: Belongs to the DZIP C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE30370.2; Type=Erroneous gene model prediction; 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; AB106357; BAC87859.1; -; mRNA.
DR EMBL; AB106358; BAC87860.1; -; mRNA.
DR EMBL; AY551927; AAS58471.1; -; mRNA.
DR EMBL; AL591370; CAD24437.2; -; Genomic_DNA.
DR EMBL; AL591510; CAE30370.2; ALT_SEQ; Genomic_DNA.
DR EMBL; BX663606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q7T019; -.
DR SMR; Q7T019; -.
DR STRING; 7955.ENSDARP00000105423; -.
DR PaxDb; Q7T019; -.
DR PRIDE; Q7T019; -.
DR ZFIN; ZDB-GENE-040526-1; dzip1.
DR eggNOG; ENOG502QRAI; Eukaryota.
DR InParanoid; Q7T019; -.
DR PhylomeDB; Q7T019; -.
DR Reactome; R-DRE-5632684; Hedgehog 'on' state.
DR PRO; PR:Q7T019; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IDA:ZFIN.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0097730; C:non-motile cilium; IDA:ZFIN.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0062063; F:BBSome binding; ISS: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:0021984; P:adenohypophysis development; IMP:ZFIN.
DR GO; GO:0035082; P:axoneme assembly; IMP:ZFIN.
DR GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
DR GO; GO:0032053; P:ciliary basal body organization; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:ZFIN.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IDA:ZFIN.
DR GO; GO:0140706; P:protein-containing complex localization to centriolar satellite; ISS:UniProtKB.
DR GO; GO:2000223; P:regulation of BMP signaling pathway involved in heart jogging; IMP:ZFIN.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:ZFIN.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:ZFIN.
DR GO; GO:0120316; P:sperm flagellum assembly; ISS:UniProtKB.
DR InterPro; IPR032714; DZIP1_N.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF13815; Dzip-like_N; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Metal-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..898
FT /note="Cilium assembly protein DZIP1"
FT /id="PRO_0000047108"
FT ZN_FING 207..230
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 14..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 145..197
FT /evidence="ECO:0000255"
FT COILED 242..353
FT /evidence="ECO:0000255"
FT COILED 407..447
FT /evidence="ECO:0000255"
FT COILED 573..590
FT /evidence="ECO:0000255"
FT COMPBIAS 19..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..682
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 473..492
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15115751"
FT /id="VSP_010970"
FT CONFLICT 324..325
FT /note="IN -> MH (in Ref. 2; AAS58471)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="T -> A (in Ref. 2; AAS58471)"
FT /evidence="ECO:0000305"
FT CONFLICT 501..504
FT /note="PTEN -> LMES (in Ref. 3; CAD24437)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="S -> P (in Ref. 2; AAS58471 and 3; CAD24437)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="T -> S (in Ref. 2; AAS58471 and 3; CAD24437)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="T -> I (in Ref. 3; CAD24437)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="T -> S (in Ref. 2; AAS58471 and 3; CAD24437)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="V -> I (in Ref. 3; CAD24437)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="Missing (in Ref. 2; AAS58471 and 3; CAD24437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 898 AA; 101728 MW; 13B26E5457EEF1B7 CRC64;
MPFYDNVYYP YPSDPPGTHS SAGIPSLLSS PQSQPSSGSQ SRPAPSTMSG PLTSSGASTS
IPPPFKFRSR RENVDWRRIN AVDVDRVACE MDFQALQEHI NAVTFCSVEG ERCHRCQSPV
DPALIKLFRL AQLTVEYLLH SQDCLSISLQ AAEERLLAEA REREQICVQL QKKTQDAKAL
KEELKQRKKI IASQQAMFSA GISANYHKCQ HCEKAFMNAS FLQSHMQRRH PSEFDMKLMT
DNQKKIQTVK LQDEINKLQE QLTLVTSQME TQQKDYTAKQ EKELIQRQEE FKRQLEIWKE
EEKMRMNSKI DEVKQACQRD MDSINQRNRN LETELLKLQQ KNIQESMQSV QTQPNASTSN
EHWQEVVKLQ QKLHKQEVKW TGKMQKMKED HDREKSLLQE ELCKVSSAVS EGMEESRRQV
QELSHRLQEQ QQIITSQNKQ MKQISSKPPT ITVQREGVST PSPETKAKVV VSEQSNSVHK
LDPIVELSEE DKDSSSISES PTENRSWQKE VQELLKNPGL RRDMRLAAQH NLDDRLQSLG
IKGVSGLSKN LYKSSMTQII SDRRKKLEED PVYRRALKEI SHKLEQRVKE RNTEQPVKSK
LHEQVVQSRP RSSSFPSTVT RVMSGPASKQ QRTPQPVPRS RTNVPHKTST PLQHRRTPPF
SSDEDSSEEE EEEEEEEESS DEESPQMQKK TVLVNSSTAK AQNTAKTQST AQSVRSAVAL
TSAEPTNVTT LSDSDWTDGS EMEEINLSQL HKHTDQNGNL KNVTHSNVKA LGKSLEKQLA
ARGPKKPAGG VNTFLEKPTD VRNTRQNAKK ELKYSDDDDD DDDDWDISSL EDVPAVAKPT
QCPVPVRKSL DKSQDTSTSV WGSSTGKGHK PGLTDAGTAS TLKSSLVTVS DWDDSDEI
