DZI1L_DANRE
ID DZI1L_DANRE Reviewed; 756 AA.
AC Q32PN7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cilium assembly protein DZIP1L {ECO:0000305|PubMed:28530676};
DE AltName: Full=DAZ-interacting zinc finger protein 1-like;
GN Name=dzip1l; ORFNames=zgc:123017;
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 [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=28530676; DOI=10.1038/ng.3871;
RA Lu H., Galeano M.C.R., Ott E., Kaeslin G., Kausalya P.J., Kramer C.,
RA Ortiz-Bruechle N., Hilger N., Metzis V., Hiersche M., Tay S.Y.,
RA Tunningley R., Vij S., Courtney A.D., Whittle B., Wuehl E., Vester U.,
RA Hartleben B., Neuber S., Frank V., Little M.H., Epting D.,
RA Papathanasiou P., Perkins A.C., Wright G.D., Hunziker W., Gee H.Y.,
RA Otto E.A., Zerres K., Hildebrandt F., Roy S., Wicking C., Bergmann C.;
RT "Mutations in DZIP1L, which encodes a ciliary-transition-zone protein,
RT cause autosomal recessive polycystic kidney disease.";
RL Nat. Genet. 49:1025-1034(2017).
CC -!- FUNCTION: Involved in primary cilium formation (PubMed:28530676).
CC Probably acts as a transition zone protein required for localization of
CC PKD1/PC1 and PKD2/PC2 to the ciliary membrane.
CC {ECO:0000250|UniProtKB:Q8IYY4, ECO:0000305|PubMed:28530676}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q8IYY4}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q8IYY4}. Note=Localizes to centrioles and to the
CC distal ends of basal bodies. {ECO:0000250|UniProtKB:Q8IYY4}.
CC -!- DEVELOPMENTAL STAGE: Maternally expressed. Ubiquitously expressed in
CC embryos at 1 day post-fertilization (dpf), with a more discrete
CC accumulation in the embryonic kidneys. In developing kidney, expressed
CC in the midsections of the pronephric ducts, in a pattern consistent
CC with the multiciliated cells. {ECO:0000269|PubMed:28530676}.
CC -!- DISRUPTION PHENOTYPE: Embryos show defects in otolith formation in the
CC inner ear, but no other overt morphological changes.
CC {ECO:0000269|PubMed:28530676}.
CC -!- SIMILARITY: Belongs to the DZIP C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; BC108046; AAI08047.1; -; mRNA.
DR RefSeq; NP_001032304.1; NM_001037227.1.
DR AlphaFoldDB; Q32PN7; -.
DR SMR; Q32PN7; -.
DR STRING; 7955.ENSDARP00000103743; -.
DR PaxDb; Q32PN7; -.
DR PeptideAtlas; Q32PN7; -.
DR GeneID; 553313; -.
DR KEGG; dre:553313; -.
DR CTD; 199221; -.
DR ZFIN; ZDB-GENE-051113-196; dzip1l.
DR eggNOG; ENOG502QRAI; Eukaryota.
DR InParanoid; Q32PN7; -.
DR OrthoDB; 1162102at2759; -.
DR PhylomeDB; Q32PN7; -.
DR PRO; PR:Q32PN7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0032880; P:regulation of protein localization; 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 2: Evidence at transcript level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..756
FT /note="Cilium assembly protein DZIP1L"
FT /id="PRO_0000331309"
FT ZN_FING 171..194
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..158
FT /evidence="ECO:0000255"
FT COILED 196..283
FT /evidence="ECO:0000255"
FT COILED 321..416
FT /evidence="ECO:0000255"
FT COMPBIAS 236..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 86384 MW; 27FF3BA5E1EBD9ED CRC64;
MLGQFSPGEP YTTSLSSTPP WSPANQFQLF RFRSRTEPID WRRLSTLDVD RVARDMDVSV
LQDFIMTVTF CALEGERCPN CRGPVDPSLV KLLRMSQLST EYLLQCQDFL SSQLAGLEER
LQAATSLVQQ GEGQRAELEK SLQETKQENR RRKQLIATQQ LLLQASANNY HKCQFCEKSF
VNYSYLQAHV QRRHPEVTDA EKQKKRKVEE MEDGIEELKE KLRLTQMQLQ EEQQADNLRR
QQEQEQQRRR EQSEKEALER WKEDERRKFN QEIADLRQLF LQESKEMASK SSSIEAKLLV
LQNKEMAGFN NASLQQDSDP EKEMRENRER ELRERIARKK SEWRRKFQEA QKRHQQENKE
LKSENSRLLK ALSVEKNSTS SVQKLQQQVV SLSSQLSQKD RLIKSQEEKI KKLSATPVPV
SVVSLNDQDS SEEPVEQDRD SQEDSDEPQW KAPKIRKGKP ALMRESKPIL EESLEQKLEN
MGLRKGTKGI SKQTFKSLSS LLAGQRLQKF RQQTNLQSLR DSLTLEVTRR VKSLQKSSGK
PTPNTLKQRG KKTSTPLNEK SLRFRQDSKA SDRREKSQQP KTLLPTPTPR SKAPPPNQTP
KILAKKNSTP PFSSDEESVE DTAYITSSRG NLSSSVRVVQ SGSLLNPTTE PDWTDSELSE
DLDLPKIYKT CNPQGSVVQT LTRSLERQLS TPIKTPVGGT RVLPPSSTTP RPAIVKQQAL
SGEESDSELS SIEELTGRRA GGHKSLEVDR TSGTSA
