DZI1L_MOUSE
ID DZI1L_MOUSE Reviewed; 774 AA.
AC Q499E4; Q8BZI8; Q8C182; Q9CSR1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cilium assembly protein DZIP1L {ECO:0000305|PubMed:28530676};
DE AltName: Full=DAZ-interacting zinc finger protein 1-like {ECO:0000312|MGI:MGI:1919757};
DE AltName: Full=Protein warpy {ECO:0000303|PubMed:28530676};
GN Name=Dzip1l {ECO:0000312|MGI:MGI:1919757};
GN Synonyms=wpy {ECO:0000303|PubMed:28530676};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Embryo, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem cell;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF 375-GLN--TRP-774.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IYY4, ECO:0000305|PubMed:28530676}.
CC -!- SUBUNIT: Interacts with SEPTIN2. {ECO:0000250|UniProtKB:Q8IYY4}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q499E4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q499E4-2; Sequence=VSP_033160;
CC -!- SIMILARITY: Belongs to the DZIP C2H2-type zinc-finger protein family.
CC {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; AK012132; BAB28052.1; -; mRNA.
DR EMBL; AK028787; BAC26121.1; -; mRNA.
DR EMBL; AK034503; BAC28732.1; -; mRNA.
DR EMBL; BC099950; AAH99950.1; -; mRNA.
DR CCDS; CCDS23436.1; -. [Q499E4-1]
DR CCDS; CCDS81060.1; -. [Q499E4-2]
DR RefSeq; NP_001298071.1; NM_001311142.1. [Q499E4-2]
DR RefSeq; NP_082534.2; NM_028258.4. [Q499E4-1]
DR RefSeq; XP_006511537.1; XM_006511474.3. [Q499E4-1]
DR RefSeq; XP_006511538.1; XM_006511475.3. [Q499E4-1]
DR RefSeq; XP_006511539.1; XM_006511476.3. [Q499E4-1]
DR AlphaFoldDB; Q499E4; -.
DR SMR; Q499E4; -.
DR BioGRID; 215407; 1.
DR STRING; 10090.ENSMUSP00000108506; -.
DR iPTMnet; Q499E4; -.
DR PhosphoSitePlus; Q499E4; -.
DR MaxQB; Q499E4; -.
DR PaxDb; Q499E4; -.
DR PRIDE; Q499E4; -.
DR ProteomicsDB; 279595; -. [Q499E4-1]
DR ProteomicsDB; 279596; -. [Q499E4-2]
DR Antibodypedia; 33422; 18 antibodies from 9 providers.
DR DNASU; 72507; -.
DR Ensembl; ENSMUST00000078367; ENSMUSP00000077475; ENSMUSG00000037784. [Q499E4-1]
DR Ensembl; ENSMUST00000112884; ENSMUSP00000108505; ENSMUSG00000037784. [Q499E4-2]
DR Ensembl; ENSMUST00000112885; ENSMUSP00000108506; ENSMUSG00000037784. [Q499E4-1]
DR Ensembl; ENSMUST00000112886; ENSMUSP00000108507; ENSMUSG00000037784. [Q499E4-2]
DR GeneID; 72507; -.
DR KEGG; mmu:72507; -.
DR UCSC; uc009rem.1; mouse. [Q499E4-1]
DR UCSC; uc009reo.1; mouse. [Q499E4-2]
DR CTD; 199221; -.
DR MGI; MGI:1919757; Dzip1l.
DR VEuPathDB; HostDB:ENSMUSG00000037784; -.
DR eggNOG; ENOG502QRAI; Eukaryota.
DR GeneTree; ENSGT00940000160898; -.
DR HOGENOM; CLU_018051_0_1_1; -.
DR InParanoid; Q499E4; -.
DR OMA; LMPHGFD; -.
DR OrthoDB; 1162102at2759; -.
DR PhylomeDB; Q499E4; -.
DR TreeFam; TF330044; -.
DR BioGRID-ORCS; 72507; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q499E4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q499E4; protein.
DR Bgee; ENSMUSG00000037784; Expressed in olfactory epithelium and 179 other tissues.
DR ExpressionAtlas; Q499E4; baseline and differential.
DR Genevisible; Q499E4; MM.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1905349; P:ciliary transition zone assembly; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0033504; P:floor plate development; IGI:MGI.
DR GO; GO:0021532; P:neural tube patterning; IGI:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:0033365; P:protein localization to organelle; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
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 Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..774
FT /note="Cilium assembly protein DZIP1L"
FT /id="PRO_0000331307"
FT ZN_FING 166..189
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 415..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 204..450
FT /evidence="ECO:0000255"
FT COMPBIAS 524..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 610
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033160"
FT MUTAGEN 375..774
FT /note="Missing: In wpy; widespread embryonic
FT dysmorphologies, including highly penetrant polydactyly of
FT all four limbs as well as craniofacial defects. Mice
FT develop cystic kidney disease."
FT /evidence="ECO:0000269|PubMed:28530676"
FT CONFLICT 45
FT /note="R -> H (in Ref. 1; BAB28052)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="I -> V (in Ref. 1; BAC26121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 774 AA; 87594 MW; 940BAC7B5290E35B CRC64;
MQYPAATAEG LSGPLSGAYT LPAFKFQPRR ESIDWRRISA VDVDRVAREL DVATLQENIA
GVTFCNLDGE VCNHCRQPVD PVLLKVLRLA QLIIEYLLHC QDCLSASVAQ LEARLQASLG
QQQRGQQELG RQADELKGVR EESRRRRKMI STLQQLLLQT SAHSYHTCHL CDKTFMNATF
LRGHIQRRHA GMADVGKQKQ EQPLGEVLEE LRAKLKWTQG ELEAQREAER QRQVQELEMA
RQREMEAKKK FDEWKEKERS KLYGEIDKLK QLFWDEFKTV ANQNSTLEEK LKALQSYSMT
ESHLGSLRDE ESEERLKHAQ EVQALQEKME VQKTEWKRKM KALHEERAAE RRQLQEENER
LHVSLSQDQK KAAAQSQRHI NALRAQLQEQ ARLIESQEET IQTLSLRKVE EVQEMPKAVA
TEEDSSEEEL EASLEERQEQ RKVLAALRKN PTWLKQFRPI LEDTLEEKLE GLGIKRDTKG
ISAQTVRRLE PLLRTQREQI ARSFREFPSL REKLNKEVSS RVKQRWESTT QPDGQPPVKS
QRVTLATREV RPKTRTLTVA LPSKPAEPST PTLQGHSSHG PGLTQVSTPI PRPRVHGPSS
TPVSPGSGLS STPPFSSEEE PEGDVVQRVS LQPPKVLPRS AAKPEDNWGW SDSETSEESA
QPPGKGSGGL ASSGTLVQSI VKNLEKQLET PAKKPSGGVN MFLRPNAALQ RASTPARKSQ
LSEDESDVEI SSLEDLSQDL GQKGKPKPLS HSKLPEKFDV SPWSSGSRPR IPGW
