CROCC_MOUSE
ID CROCC_MOUSE Reviewed; 2009 AA.
AC Q8CJ40; A2AA81; Q7TQL2; Q80U01; Q8R0B9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Rootletin;
DE AltName: Full=Ciliary rootlet coiled-coil protein;
GN Name=Crocc {ECO:0000312|MGI:MGI:3529431};
GN Synonyms=Kiaa0445 {ECO:0000312|EMBL:BAC65567.3};
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] {ECO:0000305, ECO:0000312|EMBL:AAN73044.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH KLC3.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAN73044.1};
RX PubMed=12427867; DOI=10.1083/jcb.200207153;
RA Yang J., Liu X., Yue G., Adamian M., Bulgakov O., Li T.;
RT "Rootletin, a novel coiled-coil protein, is a structural component of the
RT ciliary rootlet.";
RL J. Cell Biol. 159:431-440(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH54054.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH27090.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH54054.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH54054.1}, and
RC Retina {ECO:0000312|EMBL:AAH27090.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAC65567.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 391-2009 (ISOFORM 3).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC65567.3};
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP PROTEIN SEQUENCE OF 1261-1274, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=15870283; DOI=10.1128/mcb.25.10.4129-4137.2005;
RA Yang J., Gao J., Adamian M., Wen X.-H., Pawlyk B., Zhang L.,
RA Sanderson M.J., Zuo J., Makino C.L., Li T.;
RT "The ciliary rootlet maintains long-term stability of sensory cilia.";
RL Mol. Cell. Biol. 25:4129-4137(2005).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CEP250.
RX PubMed=16339073; DOI=10.1091/mbc.e05-10-0943;
RA Yang J., Adamian M., Li T.;
RT "Rootletin interacts with C-Nap1 and may function as a physical linker
RT between the pair of centrioles/basal bodies in cells.";
RL Mol. Biol. Cell 17:1033-1040(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1463; SER-1469; TYR-1475;
RP SER-1476; SER-1479; SER-1483; SER-1489 AND SER-1568, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and 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).
CC -!- FUNCTION: Major structural component of the ciliary rootlet, a
CC cytoskeletal-like structure in ciliated cells which originates from the
CC basal body at the proximal end of a cilium and extends proximally
CC toward the cell nucleus (PubMed:12427867). Furthermore, is required for
CC the correct positioning of the cilium basal body relative to the cell
CC nucleus, to allow for ciliogenesis (By similarity). Contributes to
CC centrosome cohesion before mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q5TZA2, ECO:0000269|PubMed:12427867}.
CC -!- SUBUNIT: Homomer. Interacts with KLC3, NEK2 and the N-terminus of
CC CEP250 (PubMed:12427867, PubMed:16339073). Interacts with CEP44 (By
CC similarity). {ECO:0000250|UniProtKB:Q5TZA2,
CC ECO:0000269|PubMed:12427867, ECO:0000269|PubMed:16339073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:12427867,
CC ECO:0000269|PubMed:16339073}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q5TZA2}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q5TZA2}. Note=In ciliated cells, associated with
CC ciliary rootlets. In non-ciliated cells, localized between, around and
CC at the proximal ends of the centrioles. Dissociates from the centrioles
CC at the onset of mitosis and reassociates with them at anaphase.
CC {ECO:0000269|PubMed:12427867, ECO:0000269|PubMed:16339073}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:12427867};
CC IsoId=Q8CJ40-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8CJ40-2; Sequence=VSP_052066, VSP_052067;
CC Name=3 {ECO:0000269|PubMed:12693553};
CC IsoId=Q8CJ40-3; Sequence=VSP_052068;
CC -!- TISSUE SPECIFICITY: Highest expression detected in photoreceptor cells
CC of retina. Expressed at lower levels in brain, trachea and kidney.
CC Detected in all major ciliated epithelia. During embryonic development,
CC enriched along the apical domains of neuroepithelium in brain
CC ventricular zone, in primordia of retinal pigment epithelia and in
CC neural retina. {ECO:0000269|PubMed:12427867}.
CC -!- PTM: Phosphorylated by NEK2 which may regulate its association with
CC centrosomes.
CC -!- DISRUPTION PHENOTYPE: Mice have no ciliary rootlets in ciliated cells.
CC {ECO:0000269|PubMed:15870283}.
CC -!- SIMILARITY: Belongs to the rootletin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27090.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF527975; AAN73044.1; -; mRNA.
DR EMBL; AL645625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027090; AAH27090.1; ALT_INIT; mRNA.
DR EMBL; BC054054; AAH54054.1; -; mRNA.
DR EMBL; AK122285; BAC65567.3; -; Transcribed_RNA.
DR CCDS; CCDS18861.1; -. [Q8CJ40-1]
DR CCDS; CCDS51346.1; -. [Q8CJ40-2]
DR RefSeq; NP_001139430.1; NM_001145958.1. [Q8CJ40-2]
DR RefSeq; NP_742120.2; NM_172122.2. [Q8CJ40-1]
DR AlphaFoldDB; Q8CJ40; -.
DR SMR; Q8CJ40; -.
DR BioGRID; 231046; 13.
DR IntAct; Q8CJ40; 6.
DR STRING; 10090.ENSMUSP00000099549; -.
DR iPTMnet; Q8CJ40; -.
DR PhosphoSitePlus; Q8CJ40; -.
DR EPD; Q8CJ40; -.
DR jPOST; Q8CJ40; -.
DR MaxQB; Q8CJ40; -.
DR PaxDb; Q8CJ40; -.
DR PeptideAtlas; Q8CJ40; -.
DR PRIDE; Q8CJ40; -.
DR ProteomicsDB; 277898; -. [Q8CJ40-1]
DR ProteomicsDB; 277899; -. [Q8CJ40-2]
DR ProteomicsDB; 277900; -. [Q8CJ40-3]
DR Antibodypedia; 14565; 35 antibodies from 15 providers.
DR Ensembl; ENSMUST00000040222; ENSMUSP00000037679; ENSMUSG00000040860. [Q8CJ40-2]
DR Ensembl; ENSMUST00000097816; ENSMUSP00000095425; ENSMUSG00000040860. [Q8CJ40-2]
DR Ensembl; ENSMUST00000102491; ENSMUSP00000099549; ENSMUSG00000040860. [Q8CJ40-1]
DR Ensembl; ENSMUST00000168157; ENSMUSP00000126543; ENSMUSG00000040860. [Q8CJ40-2]
DR GeneID; 230872; -.
DR KEGG; mmu:230872; -.
DR UCSC; uc008vns.2; mouse. [Q8CJ40-1]
DR UCSC; uc012dnz.1; mouse. [Q8CJ40-2]
DR CTD; 9696; -.
DR MGI; MGI:3529431; Crocc.
DR VEuPathDB; HostDB:ENSMUSG00000040860; -.
DR eggNOG; ENOG502QQF0; Eukaryota.
DR GeneTree; ENSGT00940000155758; -.
DR HOGENOM; CLU_000920_1_0_1; -.
DR InParanoid; Q8CJ40; -.
DR OMA; RQMKSKM; -.
DR OrthoDB; 76868at2759; -.
DR PhylomeDB; Q8CJ40; -.
DR TreeFam; TF101138; -.
DR BioGRID-ORCS; 230872; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Crocc; mouse.
DR PRO; PR:Q8CJ40; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CJ40; protein.
DR Bgee; ENSMUSG00000040860; Expressed in retinal neural layer and 172 other tissues.
DR ExpressionAtlas; Q8CJ40; baseline and differential.
DR Genevisible; Q8CJ40; MM.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:MGI.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0120219; C:subapical part of cell; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0019894; F:kinesin binding; IPI:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:MGI.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0019725; P:cellular homeostasis; IMP:MGI.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISO:MGI.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; IMP:MGI.
DR GO; GO:0010669; P:epithelial structure maintenance; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0051656; P:establishment of organelle localization; IMP:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISO:MGI.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0033365; P:protein localization to organelle; ISO:MGI.
DR InterPro; IPR026733; Rootletin.
DR PANTHER; PTHR23159:SF17; PTHR23159:SF17; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1..2009
FT /note="Rootletin"
FT /id="PRO_0000239944"
FT REGION 462..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1957..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 74..265
FT /evidence="ECO:0000255"
FT COILED 346..438
FT /evidence="ECO:0000255"
FT COILED 550..1058
FT /evidence="ECO:0000255"
FT COILED 1091..1439
FT /evidence="ECO:0000255"
FT COILED 1498..1697
FT /evidence="ECO:0000255"
FT COILED 1744..1998
FT /evidence="ECO:0000255"
FT COMPBIAS 462..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1957..1976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1977..2003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TZA2"
FT MOD_RES 1463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1475
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052066"
FT VAR_SEQ 120..209
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052067"
FT VAR_SEQ 1136..1156
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_052068"
FT CONFLICT 289
FT /note="T -> A (in Ref. 1; AAN73044 and 3; AAH54054)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="E -> G (in Ref. 3; AAH54054)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="V -> M (in Ref. 3; AAH54054)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041
FT /note="K -> E (in Ref. 3; AAH54054)"
FT /evidence="ECO:0000305"
FT CONFLICT 1346
FT /note="L -> V (in Ref. 3; BAC65567)"
FT /evidence="ECO:0000305"
FT CONFLICT 1864
FT /note="F -> L (in Ref. 3; AAH54054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2009 AA; 226945 MW; 62D942401C1085DA CRC64;
MSLGLAGSLQ AQLALEIVIQ SLENCVLGPN QEKSLSVQNR VQDFQGASLL VCAREVIASN
LSRPETPAPL QVPEMASLLS LQEENQLLQQ ELSRVEDLLA QSRAERDELA IKYNAVNERL
EQAVRLETGE LEAQEPRGLV RQSVELRRQL QEEQSSYRRK LQAYQEGQQR QAQLVQRLQA
KILQYKKQCS ELEKQLMDRS TELEQQRLRD TEHSQDLDSA LLRLEEEQQR SASLAQVNAM
LREQLDQANL ANQALSEDIR KVTSDWTRSC KELEQREAVW RREEESFNTY FSSEHSRLLR
LWRQVMGLRR QASEVKMGTE RDLLQLGGEL VRTSRAVQEL GLGLSASLHR AESKAEAALE
KQKLLQAQLE EQLQAKLLRE KDLAQLQVQS DLDKADLSAR VTELALSVEH LQNQNSEKDQ
VNRTLSDKLE ALESLRLQEQ TTLDTEDGEG LQQTLRDLAQ AALSDTESGV QLSSSERTAD
TSDGSLRGFS GQRTPTPPRH SPGRGRSPRR GLSPACSDSS TLTLIHSALH KRQLQVQDMR
GRYEASQELL GSVRKQLSDS EGERRGLEEQ LQRLRDQTAA SAQAQEDAQR EAQRLRSANE
LLSREKGNLT HSLQVTQQQA KELRQELEKL QAAQEELKRQ HNQLEDAQED SVQEGARARR
ELERSHRQLE QLEVKRSGLT KELVEVREAL SCAILQRDVL QTEKAEVAEA LTKAEAGRAQ
LELSLTKLRA EEASLRDSLS KMSALNESLA QDKLELNRLI AQLEEEKVAL LGRQQQAEHA
TTMAVEKQEL LEQLRLEQEV ERQGLQGSLC VAEQAREALE QQILVLRSER SHLQEQLAQL
SRQLSGRDQE LEQALRESQR QVEALERAAR EKEAMAKERA GLAVKLAAAE REGRTLSEEA
IRLRLEKEAL ESSLFDVQRQ LAQLEARREQ LEADSQALLL AKETLTGELA GLRQQVTSTE
EKAALDKELM TQKLVQAERE AQASLREQRA AHEEDLQRLQ HEKEAAWREL QAERAQLQGQ
LQQEREELLA RMEAEKEELS KEIAALQQER DEGLLLAESE KQQALSLKES EKTALSEKLM
GTRHSLAAIS LEMERQKRDA QSRQEQDRNT LNALTSELRD LRAQLEEATA AHAQTVKELE
ERTGNLGRQR EACMREAEEL RTQLRVLEDT RDGLRRELLE AQRKGRDSQD SSEAHRQEAS
ELRRSLSEGA KEREALRRSN EELRSAVKKA ESERISLKLA NEDKEQKLAL LEEARVSVAK
EAGELRASLQ EVERSRLEAR RELQELRRQM KTLDSDNGRL GRELADLQGR LALGERTEKE
SRREALGLRQ RLLKGESSLE ALKQELQGSQ RKLQEQEAEF RARERGLLGS LEEARGAEKR
LLDSARSLEL RLEAVRAETS ELGLRLSAAE GRAQGLEVEL ARVEAQRRVA EAQLGGLRSA
LRRGLGLGRV SSSPAREAPA GGSGDGLSSP SPLEYSPRSQ PPSPGLIASP APPDLDPEAV
RDALRDFLQE LRSAQRERDE LKVQTSTLSQ QLVEMEAERD HAASRAKQLQ KAVAESEEAW
RSADRRLSGA QAELALQEES VRRSKRECRA TLDQMAVLER SLQATESELR ASQEKVSKMK
ATEAKLESDK RRLKEVLDAS ESRSIKLELQ RRALEGELQR SRLGLGDREA HAQALQDRVD
SLQRQVADSE VKAGTLQLTV ERLSGALAKV EESEGNLRSK VQSLTDALTQ SSASLSSTQD
KNLHLQKALS TCEHDRQVLQ ERLDAARQAL SEARRQSSSL GEQVQTLRGE LASLELQRGD
AEGQLQQLQQ ALRQRQEGEA MALRSVQKLQ EERRLLQERL GSLQRALAQL EAEKRDLERS
ALQFDKDRVA LRKTLDKVER EKLRSHEDTL RLNAERGRLD RTLTGAELDL AEAQQQIQHL
EAQVDVALEG NHNPVQPEAG EQQLELQQEV ERLRSAQVQT ERTLEARERA HRQRVSGLEE
QVSTLKAQLH QELRRSSASV SLPPGTPEK
