CP131_DROME
ID CP131_DROME Reviewed; 1134 AA.
AC A1Z7Z9;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Centrosomal protein of 131 kDa;
DE AltName: Full=5-azacytidine-induced protein 1;
DE AltName: Full=Dilatory protein {ECO:0000303|PubMed:21750193, ECO:0000312|FlyBase:FBgn0033447};
GN Name=dila {ECO:0000303|PubMed:21750193, ECO:0000312|FlyBase:FBgn0033447};
GN Synonyms=azi1 {ECO:0000303|PubMed:27646273},
GN cep131 {ECO:0000303|PubMed:21750193}; ORFNames=Dmel_CG1625;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=21750193; DOI=10.1242/jcs.084798;
RA Ma L., Jarman A.P.;
RT "Dilatory is a Drosophila protein related to AZI1 (CEP131) that is located
RT at the ciliary base and required for cilium formation.";
RL J. Cell Sci. 124:2622-2630(2011).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27646273; DOI=10.1083/jcb.201603086;
RA Vieillard J., Paschaki M., Duteyrat J.L., Augiere C., Cortier E.,
RA Lapart J.A., Thomas J., Durand B.;
RT "Transition zone assembly and its contribution to axoneme formation in
RT Drosophila male germ cells.";
RL J. Cell Biol. 214:875-889(2016).
CC -!- FUNCTION: Cilium-specific protein with a role in cilium/flagellum
CC formation (PubMed:21750193, PubMed:27646273). May be involved in
CC transport of components into the growing cilium (PubMed:21750193). In
CC germ cells and sensory neurons, plays a role with Cby in the building
CC of the transition zone necessary for the formation of the ciliary cap
CC and for the correct elongation of the axoneme (PubMed:27646273).
CC {ECO:0000269|PubMed:21750193, ECO:0000269|PubMed:27646273}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:21750193}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:21750193,
CC ECO:0000269|PubMed:27646273}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:27646273}.
CC Note=Co-localizes with the pericentriolar material (PCM) protein cp190
CC at centrosomes in undifferentiated sensory neurons (PubMed:21750193,
CC PubMed:27646273). Localizes to the ciliary base, including the basal
CC body and transition zone in sensory neurons and germ cells
CC (PubMed:21750193, PubMed:27646273). {ECO:0000269|PubMed:21750193,
CC ECO:0000269|PubMed:27646273}.
CC -!- TISSUE SPECIFICITY: Expressed in chordotonal (Ch) neuronal precursors.
CC Expressed in ciliated cells, like sensory neurons and spermatids.
CC {ECO:0000269|PubMed:21750193}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing and differentiating
CC ciliated sensory neurons of both the chordotonal (Ch) mechanosensory
CC neurons and external sensory (ES) cells. {ECO:0000269|PubMed:21750193}.
CC -!- DISRUPTION PHENOTYPE: Displays reduced climbing ability and die very
CC soon after eclosion (PubMed:21750193). Loss of protein expression leads
CC to truncated sensory cilia formation and impaired intraflagellar
CC transport processes (PubMed:21750193). Simultaneous knockout of Cby and
CC dila results in lack of motor coordination and absence of cilia in
CC chordotonal neurons where centrioles fail to build a transition zone
CC and Cep290 and Mks1 are mis-localized. Males are sterile: aberrant
CC microtubule extensions, lack of ciliary cap and mislocalization of Mks1
CC and B9d1 to the basal body result in failure of axoneme formation and
CC lack of mature sperm; sperm cysts fail to elongate whereas the overall
CC size of the testes is not reduced (PubMed:27646273).
CC {ECO:0000269|PubMed:21750193, ECO:0000269|PubMed:27646273}.
CC -!- SIMILARITY: Belongs to the CEP131 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58897.2; -; Genomic_DNA.
DR RefSeq; NP_610519.2; NM_136675.3.
DR AlphaFoldDB; A1Z7Z9; -.
DR SMR; A1Z7Z9; -.
DR BioGRID; 61839; 1.
DR IntAct; A1Z7Z9; 9.
DR STRING; 7227.FBpp0301614; -.
DR PaxDb; A1Z7Z9; -.
DR EnsemblMetazoa; FBtr0309879; FBpp0301613; FBgn0033447.
DR GeneID; 36010; -.
DR KEGG; dme:Dmel_CG1625; -.
DR UCSC; CG1625-RA; d. melanogaster.
DR CTD; 36010; -.
DR FlyBase; FBgn0033447; dila.
DR VEuPathDB; VectorBase:FBgn0033447; -.
DR eggNOG; ENOG502RZME; Eukaryota.
DR GeneTree; ENSGT00390000001758; -.
DR PhylomeDB; A1Z7Z9; -.
DR SignaLink; A1Z7Z9; -.
DR BioGRID-ORCS; 36010; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36010; -.
DR PRO; PR:A1Z7Z9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033447; Expressed in proneural cluster and 18 other tissues.
DR ExpressionAtlas; A1Z7Z9; baseline and differential.
DR Genevisible; A1Z7Z9; DM.
DR GO; GO:0034451; C:centriolar satellite; IBA:GO_Central.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IDA:FlyBase.
DR GO; GO:0061822; C:ciliary cap; IDA:FlyBase.
DR GO; GO:0035869; C:ciliary transition zone; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000242; C:pericentriolar material; IDA:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0035082; P:axoneme assembly; IMP:FlyBase.
DR GO; GO:0097711; P:ciliary basal body-plasma membrane docking; IGI:FlyBase.
DR GO; GO:1905349; P:ciliary transition zone assembly; IGI:FlyBase.
DR GO; GO:0060271; P:cilium assembly; IMP:FlyBase.
DR GO; GO:0042073; P:intraciliary transport; IMP:FlyBase.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IEA:InterPro.
DR GO; GO:1905515; P:non-motile cilium assembly; IGI:FlyBase.
DR GO; GO:0048935; P:peripheral nervous system neuron development; IMP:FlyBase.
DR GO; GO:1904491; P:protein localization to ciliary transition zone; IGI:FlyBase.
DR GO; GO:0010824; P:regulation of centrosome duplication; IBA:GO_Central.
DR GO; GO:0007288; P:sperm axoneme assembly; IGI:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR InterPro; IPR030465; CEP131.
DR PANTHER; PTHR31540; PTHR31540; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Differentiation; Reference proteome.
FT CHAIN 1..1134
FT /note="Centrosomal protein of 131 kDa"
FT /id="PRO_0000429320"
FT REGION 111..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 732..1131
FT /evidence="ECO:0000255"
FT COMPBIAS 494..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 129643 MW; 4195E401ADE20626 CRC64;
MDLCLKGSQI NLATRQKTKP KYTSRSLTTL HNPCPHFRPR SANFLQQRSR SSPFLGRPQS
ADPKFGRRLS NYFVEKELRN GGKRQVSSND LLKSLLEEPI KRSWLCRSTC NSSESDYSLH
KRTPDSSEEG EQFLVNMPVG EKVKSYSSYS GNQGLSNGAL LQRTAKPDLP GRVSFSKPNM
HADLDSSDCD NDKQEVRPSI SAPGPLTLPS FLSKVEQADP VGQKKSVHFG STAAEGEVLA
ETYEYPKCPS ENCTCSTRSS STTSTNEASA SDVKCACDAP SCRFMESSKQ VEPTSPTPTL
PKAPSSELDV IREYKQAVEG VQVVKNHLGT DTLNNIEILP NYLDKYASPT KEKQNNLSET
KNMATNSSAV NNGSVVYRPV GNPRNFGAEN NFLPAVQDDR RSFANGSSDG VINNYLKVAS
TPPFVGKKKE NVKPASADPI ARSSKSKVTK STINPAPLGK MKKAISVGSL REERKLSEYN
LDKVDSWMSM QDQKQYDGKH KPGLEDLDEA QDNDTASQLS LKSNEDSRDS TYDEIVSVIK
EIEEDKKRDN FSEGIPSELN LNLDSRCETA DTVTVSEGKV PESGDKYKDI LAYLNNVESS
CDKTLMETRR SIPDSNRSEV EFVVEPDVTD EVPKLSELLM LPNHQLARRV IALSLRANEL
ANAIHMSKEH VFQLRGEKQK SLRAEKSTAA AKLRDQKKHY EEVVTRHQGF IEQLLKDKGS
LCEKVAALTR RLESQNQAWE HRLETELART KETTMAGEKI RRERWVRENT KKIKELTVKG
LEAEINKMNC DHQREVTELK RTHQMQLLDA LEEARTKHEQ IETSIRESCA QDREAIIEKE
RTAIRERFER QLEEEQRTQA EQRQKLTEEF AAERDRLQSE LRQRENEHQA RRQEALREQE
QELEQAKFEM QERMAKQEEK YQNRVNTIEQ QYQADFELWK TEHENKTKLA QAEKENAIRQ
HYRAERDRQL DELVVRMEAD ALQHKEEHEL KMNRLKEKYE KDLVLAESVE KSLREKYAET
RGKLAEADAQ VRNSQAEVKQ LQLELSHSKK MCGDIIMERD RLRDNLNADI QSELGVLNER
HKQEMDQLQK RVHQTIQRQE ETIEILKGDN DALRQQCLKL NAVIRQQRKD YCVK
