DZIP1_DROME
ID DZIP1_DROME Reviewed; 737 AA.
AC Q9VC70;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cilium assembly protein DZIP1L {ECO:0000305|PubMed:31821146};
DE AltName: Full=DAZ-interacting zinc finger protein 1-like;
DE AltName: Full=Zinc finger protein DZIP1 {ECO:0000303|PubMed:31821146};
GN Name=DZIP1 {ECO:0000303|PubMed:31821146, ECO:0000312|FlyBase:FBgn0039201};
GN ORFNames=CG13617 {ECO:0000312|FlyBase:FBgn0039201};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH FAM92 AND CBY, INTERACTION WITH
RP CBY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 1-MET--GLU-65.
RX PubMed=31821146; DOI=10.7554/elife.49307;
RA Lapart J.A., Gottardo M., Cortier E., Duteyrat J.L., Augiere C., Mange A.,
RA Jerber J., Solassol J., Gopalakrishnan J., Thomas J., Durand B.;
RT "Dzip1 and Fam92 form a ciliary transition zone complex with cell type
RT specific roles in Drosophila.";
RL Elife 8:0-0(2019).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CBY; CEP290 AND RAB8, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 357-LEU--LYS-737.
RX PubMed=33370260; DOI=10.1371/journal.pbio.3001034;
RA Wu Z., Pang N., Zhang Y., Chen H., Peng Y., Fu J., Wei Q.;
RT "CEP290 is essential for the initiation of ciliary transition zone
RT assembly.";
RL PLoS Biol. 18:e3001034-e3001034(2020).
CC -!- FUNCTION: Component of the DZIP1-Fam92-Cby complex which promotes
CC ciliogenesis in sensory neurons and spermatocytes by acting downstream
CC of Cep290 to initiate early ciliary membrane formation and thus
CC transition zone (TZ) assembly (PubMed:31821146, PubMed:33370260).
CC During spermatogenesis, also regulates distal elongation of the basal-
CC body and their docking (anchoring) to the plasma membrane and as a
CC consequence, regulates the initiation and proper elongation of axonemal
CC microtubules (PubMed:31821146). Within the complex, required to recruit
CC or stabilize Rab8, Fam92 and Cby at the distal basal body of cilia to
CC promote early ciliary membrane formation and initiate TZ assembly
CC (PubMed:31821146). Also acts with Fam92 to restrict cep290 localization
CC to the proximal part of the TZ (PubMed:31821146). May also be involved
CC in recruitment or stabilization of Mks1 at the TZ (PubMed:31821146).
CC {ECO:0000269|PubMed:31821146, ECO:0000269|PubMed:33370260}.
CC -!- SUBUNIT: Component of a ciliary transition zone (TZ)-localized complex
CC composed of DZIP1, Fam92 and Cby (PubMed:31821146). Interacts directly
CC with Cby (PubMed:31821146, PubMed:33370260). Interacts with cep290 (via
CC N-terminus) (PubMed:33370260). Interacts (via N-terminus) with Rab8
CC (PubMed:33370260). {ECO:0000269|PubMed:31821146,
CC ECO:0000269|PubMed:33370260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:31821146,
CC ECO:0000269|PubMed:33370260}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:31821146, ECO:0000269|PubMed:33370260}.
CC Note=Localizes at the transition zone (TZ) in type I sensory neurons
CC and spermatocytes (PubMed:31821146, PubMed:33370260). In spermatocytes,
CC localizes along the TZ membranes (PubMed:33370260). Localizes at the
CC centriolar distal ends of early spermatocytes and in elongating
CC spermatids, when the TZ migrates away from the basal body, localizes at
CC the ring centriole (PubMed:31821146, PubMed:33370260). In sensory
CC neurons, localizes between the transition fiber and TZ core components
CC (PubMed:33370260). {ECO:0000269|PubMed:31821146,
CC ECO:0000269|PubMed:33370260}.
CC -!- TISSUE SPECIFICITY: In neurons of the second and third antennal
CC segments, expressed at the tip of the dendrites.
CC {ECO:0000269|PubMed:31821146}.
CC -!- SIMILARITY: Belongs to the DZIP C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF56305.1; -; Genomic_DNA.
DR EMBL; AE014297; AGB96298.1; -; Genomic_DNA.
DR RefSeq; NP_001262918.1; NM_001275989.1.
DR RefSeq; NP_651263.1; NM_143006.2.
DR AlphaFoldDB; Q9VC70; -.
DR SMR; Q9VC70; -.
DR IntAct; Q9VC70; 5.
DR STRING; 7227.FBpp0084025; -.
DR PaxDb; Q9VC70; -.
DR EnsemblMetazoa; FBtr0084641; FBpp0084025; FBgn0039201.
DR EnsemblMetazoa; FBtr0334333; FBpp0306441; FBgn0039201.
DR GeneID; 42921; -.
DR KEGG; dme:Dmel_CG13617; -.
DR UCSC; CG13617-RA; d. melanogaster.
DR FlyBase; FBgn0039201; DZIP1.
DR VEuPathDB; VectorBase:FBgn0039201; -.
DR eggNOG; ENOG502QRAI; Eukaryota.
DR HOGENOM; CLU_380955_0_0_1; -.
DR InParanoid; Q9VC70; -.
DR OMA; VKMPERA; -.
DR OrthoDB; 330097at2759; -.
DR PhylomeDB; Q9VC70; -.
DR Reactome; R-DME-5632684; Hedgehog 'on' state.
DR BioGRID-ORCS; 42921; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42921; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039201; Expressed in testis and 5 other tissues.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..737
FT /note="Cilium assembly protein DZIP1L"
FT /id="PRO_0000452641"
FT ZN_FING 144..167
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..293
FT /note="Interaction with Rab8"
FT /evidence="ECO:0000269|PubMed:33370260"
FT REGION 167..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 98..132
FT /evidence="ECO:0000255"
FT COMPBIAS 214..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..506
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1..65
FT /note="Missing: Viable but displays adherent transition
FT zone (TZ) assembly in sensory neurons and spermatocytes.
FT Consequently, adults display defects associated with
FT ciliary dysfunction and disorganization, such as severe
FT uncoordination and axonemal defects and dispersed nuclei in
FT the testes. Cilia are essentially absent in antennal
FT chordotonal organs, transition zones are disorganized and
FT microtubules fail to elongate."
FT /evidence="ECO:0000269|PubMed:31821146"
FT MUTAGEN 357..737
FT /note="Missing: Adults display adherent transition zone
FT (TZ) assembly and cilia are almost completely lost in
FT auditory neurons. Consequently, adults display defects
FT associated with ciliary dysfunction and disorganization,
FT such as uncoordination, inability to stand, and severely
FT deficient in touch and hearing. In spermatocytes, ciliary
FT axonemes extend aberrantly and the basal body and plasma
FT membrane separate at later stages of spermatogenesis."
FT /evidence="ECO:0000269|PubMed:33370260"
SQ SEQUENCE 737 AA; 83822 MW; 0C67EF41DC4D9652 CRC64;
MGFKGKYPQM VRETGFKLRQ YRDGPLDWRL MGSYETERIL REQNFELVDK ALTHLSEAPL
GTVLETHILD SGIAKYFVMS QYAIQYLMCC RTYLDECVTD LKEAHTTAQE EIATLRKSLS
ESNNEVVQLH KRITQIEAIR EVVYPCHLCT KNFISNEALN VHIGRKHRVA SPPSLTSATG
KEKDRDKATD VHLINTIKME LEIKQLKERL NAAERNIKER STGSKRVSPR QEQRHVGIQS
NLAEPKEKDE DSGEARQSEA SERKEQLTGL AERLSNFEEW QTQLKQSNEQ FIQDINKRLE
GLSHALEQSK QASASTPPLE DRVATPCLED LERILTEKVA EIGKVSAHRL EEVVYHLEEG
YKEKLGALER ELKQLSVQKV QPEPVQTVPV ASKIPKPVVR KEETNIDRIR KQVESEFLKQ
KHDDDTYSIE EAPRKGSEKP FPQLVTQVQV VEKEQPSAGS SDSNPTYTKS PREPAPNKQE
TKEATDVSDS LSQEETENEE ERSLTEEEGT DVPTSGSEAA REDPTPKTIK PSGRIIKSPQ
KPLTRKDARK MVNRKLMSHG FDMKSKGISH NSLKRVNSEL TEHRNKLKLQ HPHFYATRNR
IRKFVEKLCS AKFSERAEML LKHKSPLKPM EVPGKGIPRS AISEKSEEDI ASSQGEEQTD
EQTDSSEQQT RSPSPQRLVS RDFKARLEEI LVKPAATIRG ASKSSLSSRP VPLPRKRVMF
NTTEDGKSFN DSDDNLK
