DZI1L_RAT
ID DZI1L_RAT Reviewed; 776 AA.
AC Q5XIA0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cilium assembly protein DZIP1L {ECO:0000305};
DE AltName: Full=DAZ-interacting zinc finger protein 1-like {ECO:0000312|RGD:1311430};
GN Name=Dzip1l {ECO:0000312|RGD:1311430};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in primary cilium formation. Probably acts as a
CC transition zone protein required for localization of PKD1/PC1 and
CC PKD2/PC2 to the ciliary membrane. {ECO:0000250|UniProtKB:Q8IYY4}.
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 -!- SIMILARITY: Belongs to the DZIP C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; BC083786; AAH83786.1; -; mRNA.
DR RefSeq; NP_001014117.1; NM_001014095.1.
DR AlphaFoldDB; Q5XIA0; -.
DR SMR; Q5XIA0; -.
DR STRING; 10116.ENSRNOP00000019902; -.
DR iPTMnet; Q5XIA0; -.
DR PhosphoSitePlus; Q5XIA0; -.
DR jPOST; Q5XIA0; -.
DR PaxDb; Q5XIA0; -.
DR PRIDE; Q5XIA0; -.
DR GeneID; 315952; -.
DR KEGG; rno:315952; -.
DR UCSC; RGD:1311430; rat.
DR CTD; 199221; -.
DR RGD; 1311430; Dzip1l.
DR VEuPathDB; HostDB:ENSRNOG00000014746; -.
DR eggNOG; ENOG502QRAI; Eukaryota.
DR InParanoid; Q5XIA0; -.
DR OMA; LMPHGFD; -.
DR OrthoDB; 1162102at2759; -.
DR PhylomeDB; Q5XIA0; -.
DR PRO; PR:Q5XIA0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000014746; Expressed in skeletal muscle tissue and 18 other tissues.
DR Genevisible; Q5XIA0; RN.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
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:1905349; P:ciliary transition zone assembly; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0033504; P:floor plate development; ISO:RGD.
DR GO; GO:0021532; P:neural tube patterning; ISO:RGD.
DR GO; GO:0061512; P:protein localization to cilium; ISO:RGD.
DR GO; GO:0033365; P:protein localization to organelle; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
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; Coiled coil; Cytoplasm; Cytoskeleton;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..776
FT /note="Cilium assembly protein DZIP1L"
FT /id="PRO_0000331308"
FT ZN_FING 166..189
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 520..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 196..450
FT /evidence="ECO:0000255"
FT COMPBIAS 539..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q499E4"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q499E4"
SQ SEQUENCE 776 AA; 88025 MW; 19C73D88F90808E7 CRC64;
MQYSVATADG LSGPPSGAYT LPTFKFQPRR ESIDWRRISA VDVDRVAREL DVATLQENIA
GVTFCNLDRE VCNHCRQPVD PVLLKVLRLA QLIIEYLLHC QDCLSASVAQ LEARLQASLG
QQQRGQQELG RQADELKGVR EESRRRRKMI STLQQLLLQT GAHSYHTCHL CDKTFMNATF
LRGHIQRRHA GMAEVGKQKQ EQQLGEVLEE LRAKLKWTQG ELEAQREAER QRQAQELEMI
RQREIEAKKK FDEWKEKERS KLYGEIDKLK QLFWDEFKTV ANQNSTLEEK LKVLQSYSMT
ESHLGSLRDE ESEERLKHAQ ELQALREKMD IQKTEWKRKM KALHEERAAE RRQLQEENER
LHVTLSQDQK KAAAQSQRHI NALRAQLQEQ ARLIESQEET IQTLSFRRME EVQEVPKAVV
TEEDSSEEEL EASLEEQQEQ RKVLAALRNN PAWLKQFRPI LEDTLEEKLE GMGIKRGTKG
ISAQTVRRLE PLLRTQREQT ARSFREFLSL REKLNQEVSS RAKKRWEGTA VVPQPDGQPP
VKSQRTTLAT REVRPKTRTL TVALPSKPAE PSTSTPRGHS SHGPGLTQVS TPIPRPRVHG
PSSTPVSPGP GLSTPPFSSE EEPEGDVVQR VSLQPPKVLP RSAPQPEDNW GWSDSETSEE
SAQSPGKGSD GLASSATLVQ SMVKNLEKQL ETPAKKPSGG VNMFLRPNTA LQRSSTPARK
TQLSEDESDL EISSLEDLSH DLGPKGKPTP LSHSKLPEKF DASPWSSGSR PRIPGW
