LCA5_MOUSE
ID LCA5_MOUSE Reviewed; 704 AA.
AC Q80ST9; Q9CYM9; Q9D5J9;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lebercilin;
DE AltName: Full=Leber congenital amaurosis 5 protein homolog;
GN Name=Lca5;
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=Testis;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=17546029; DOI=10.1038/ng2066;
RA den Hollander A.I., Koenekoop R.K., Mohamed M.D., Arts H.H., Boldt K.,
RA Towns K.V., Sedmak T., Beer M., Nagel-Wolfrum K., McKibbin M.,
RA Dharmaraj S., Lopez I., Ivings L., Williams G.A., Springell K., Woods C.G.,
RA Jafri H., Rashid Y., Strom T.M., van der Zwaag B., Gosens I.,
RA Kersten F.F.J., van Wijk E., Veltman J.A., Zonneveld M.N.,
RA van Beersum S.E.C., Maumenee I.H., Wolfrum U., Cheetham M.E., Ueffing M.,
RA Cremers F.P.M., Inglehearn C.F., Roepman R.;
RT "Mutations in LCA5, encoding the ciliary protein lebercilin, cause Leber
RT congenital amaurosis.";
RL Nat. Genet. 39:889-895(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [5]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21606596; DOI=10.1172/jci45627;
RA Boldt K., Mans D.A., Won J., van Reeuwijk J., Vogt A., Kinkl N.,
RA Letteboer S.J., Hicks W.L., Hurd R.E., Naggert J.K., Texier Y.,
RA den Hollander A.I., Koenekoop R.K., Bennett J., Cremers F.P.,
RA Gloeckner C.J., Nishina P.M., Roepman R., Ueffing M.;
RT "Disruption of intraflagellar protein transport in photoreceptor cilia
RT causes Leber congenital amaurosis in humans and mice.";
RL J. Clin. Invest. 121:2169-2180(2011).
CC -!- FUNCTION: Involved in intraflagellar protein (IFT) transport in
CC photoreceptor cilia. {ECO:0000269|PubMed:21606596}.
CC -!- SUBUNIT: Interacts with NINL. Interacts with OFD1. Interacts with
CC FAM161A. Interacts with components of the IFT complex B.
CC {ECO:0000250|UniProtKB:Q86VQ0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytoskeleton, cilium axoneme {ECO:0000269|PubMed:17546029}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:17546029}. Cell
CC projection, cilium {ECO:0000269|PubMed:21606596}. Note=Localized to the
CC region between the outer and inner photoreceptor segments,
CC corresponding to the photoreceptor connecting cilium (PubMed:21606596,
CC PubMed:17546029). Colocalizes with IFT complex A and B proteins in the
CC connecting cilium of photoreceptors (PubMed:21606596).
CC {ECO:0000269|PubMed:17546029, ECO:0000269|PubMed:21606596}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80ST9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80ST9-2; Sequence=VSP_014944, VSP_014945;
CC -!- TISSUE SPECIFICITY: Detected in several tissues.
CC {ECO:0000269|PubMed:17546029}.
CC -!- DEVELOPMENTAL STAGE: Almost ubiquitous, low-level staining at 12.5 dpc.
CC At later stages (14.5 dpc, 16.5 dpc and 18.5 dpc), staining of the eye,
CC inner ear, kidney, regions of the central and peripheral neural system,
CC the gut and the ciliated epithelium of the nasopharynx, trachea and
CC lungs is more pronounced. Expression in the mouse eye shifted during
CC development from the ganglion cell layer to the photoreceptors. In
CC adult eyes (P90), expression is limited to the photoreceptor cell
CC layer. {ECO:0000269|PubMed:17546029}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit retinal patches of
CC depigmentation, lack rod and cone ERG responses to light stimuli, and
CC show loss of ciliary intraflagellar transport function in
CC photoreceptors leading to failure of outer segment formation and
CC photoreceptor degeneration. {ECO:0000269|PubMed:21606596}.
CC -!- SIMILARITY: Belongs to the LCA5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK015260; BAB29769.1; -; mRNA.
DR EMBL; AK017509; BAB30781.1; ALT_INIT; mRNA.
DR EMBL; BC049101; AAH49101.1; -; mRNA.
DR EMBL; BC052060; AAH52060.1; -; mRNA.
DR CCDS; CCDS23373.1; -. [Q80ST9-2]
DR CCDS; CCDS23374.1; -. [Q80ST9-1]
DR RefSeq; NP_081724.1; NM_027448.2.
DR RefSeq; NP_083710.2; NM_029434.3.
DR AlphaFoldDB; Q80ST9; -.
DR SMR; Q80ST9; -.
DR STRING; 10090.ENSMUSP00000034791; -.
DR iPTMnet; Q80ST9; -.
DR PhosphoSitePlus; Q80ST9; -.
DR jPOST; Q80ST9; -.
DR MaxQB; Q80ST9; -.
DR PaxDb; Q80ST9; -.
DR PRIDE; Q80ST9; -.
DR ProteomicsDB; 292237; -. [Q80ST9-1]
DR ProteomicsDB; 292238; -. [Q80ST9-2]
DR DNASU; 75782; -.
DR GeneID; 75782; -.
DR KEGG; mmu:75782; -.
DR CTD; 167691; -.
DR MGI; MGI:1923032; Lca5.
DR eggNOG; ENOG502QQG3; Eukaryota.
DR InParanoid; Q80ST9; -.
DR PhylomeDB; Q80ST9; -.
DR BioGRID-ORCS; 75782; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Lca5; mouse.
DR PRO; PR:Q80ST9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80ST9; protein.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0042073; P:intraciliary transport; IMP:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR026684; Lebercilin.
DR InterPro; IPR026188; Lebercilin-like.
DR InterPro; IPR028933; Lebercilin_dom.
DR PANTHER; PTHR16650; PTHR16650; 1.
DR PANTHER; PTHR16650:SF10; PTHR16650:SF10; 1.
DR Pfam; PF15619; Lebercilin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..704
FT /note="Lebercilin"
FT /id="PRO_0000089547"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..300
FT /evidence="ECO:0000255"
FT COILED 448..479
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VQ0"
FT VAR_SEQ 412..419
FT /note="EWAREELD -> GNLLVRIS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014944"
FT VAR_SEQ 420..704
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014945"
FT CONFLICT 28
FT /note="L -> F (in Ref. 1; BAB29769)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="A -> V (in Ref. 1; BAB29769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 80162 MW; C9B5D28C450F8B0E CRC64;
MGERARSPDI EQGKKGGKHP YSHYSSDLGS SPQSSGPSSP VNTTPCASTR EKNPKRHLSD
NQVHHPTVRK VSPKAVPSKK GIRVGFRSQS LNREPLRKDP DIVTKRVLSA RLLKINELQN
EVSELQVKLA QLLKENKALK SLQYRQEKAL NKFEDAENEI SQLIHRHNNE ITALKERLRK
SQEKERATEK RVKETEGELF RTKFSLQKLK KISEARHLPE RDDLAKKLVS AELKLDDTER
KIKELSKNLE LSTNSFQRQL LAERKRAFEA YDENKVLQKE LQRLHHKLKE KEKELDIKNI
YANRLPKSSP KKEKEIERKH VSCQSDFTDQ CTKGVQTAED FELEDFPFTA QTVLCYENRW
DEPEYLSSYL EYQDLNKHGS EMLSSVLGQE GKYDEDEDPC SAKQEARKPE SEWAREELDK
VKGKSALLGR AEKLALEAGR FPTENYQAQS VDKFEDEAER LKTEMLLAKL NEINKELQDP
QNLGRAPLPL LPNFESKLHS PDRSTRPYSF PESLDRSFNG QHLQDLSFLT PRGEGGSPGP
IRSPGQIRSP APLDEFSFGS YVPSFGKTLG KSNPPSQKSS LLDFQSNSSE SPSKDSLDLM
SRKEKKATLM EQLFGPSASN TSVSSKSTDP HFPAASRGDM DPLHFLSGDR NSRVREPGDE
EEDLFLREGR SFNPNRHRLK HASNKPTVTA VDSVDEDIEE VTLR
