CAMP3_MOUSE
ID CAMP3_MOUSE Reviewed; 1252 AA.
AC Q80VC9; E9Q5B0; Q5DTW9; Q8BUZ0; U5LGR7; U5LGS1; U5LGS5; U5LGT0; U5LHT8;
AC U5LHU4; U5LHW1; U5LHW4; U5LHW9; U5LK15; U5LK19; U5LK24; U5LK70; U5LK74;
AC U5LK79;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 3 {ECO:0000305};
DE AltName: Full=Marshalin {ECO:0000303|PubMed:24244856};
DE AltName: Full=Protein Nezha {ECO:0000303|PubMed:23169647};
GN Name=Camsap3 {ECO:0000312|MGI:MGI:1916947};
GN Synonyms=Kiaa1543 {ECO:0000303|Ref.6};
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 [MRNA] (ISOFORMS 1; 3; 4; 5; 6; 7; 8; 9; 10; 11; 12;
RP 13; 14; 15; 16 AND 17), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cochlea;
RX PubMed=24244856; DOI=10.1242/bio.20135603;
RA Zheng J., Furness D., Duan C., Miller K.K., Edge R.M., Chen J., Homma K.,
RA Hackney C.M., Dallos P., Cheatham M.A.;
RT "Marshalin, a microtubule minus-end binding protein, regulates cytoskeletal
RT structure in the organ of Corti.";
RL Biol. Open 2:1192-1202(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-1252 (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 704-713, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-351; THR-797;
RP SER-812 AND SER-881, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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).
RN [9]
RP FUNCTION, AND INTERACTION WITH CAMSAP2.
RX PubMed=23169647; DOI=10.1073/pnas.1218017109;
RA Tanaka N., Meng W., Nagae S., Takeichi M.;
RT "Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific organization of
RT noncentrosomal microtubules.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20029-20034(2012).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24706919; DOI=10.1073/pnas.1404133111;
RA Hendershott M.C., Vale R.D.;
RT "Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5860-5865(2014).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 608-LEU--ARG-612.
RX PubMed=26715742; DOI=10.1073/pnas.1520638113;
RA Toya M., Kobayashi S., Kawasaki M., Shioi G., Kaneko M., Ishiuchi T.,
RA Misaki K., Meng W., Takeichi M.;
RT "CAMSAP3 orients the apical-to-basal polarity of microtubule arrays in
RT epithelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:332-337(2016).
RN [12]
RP INTERACTION WITH CDH23.
RX PubMed=27349180; DOI=10.1038/srep28706;
RA Takahashi S., Mui V.J., Rosenberg S.K., Homma K., Cheatham M.A., Zheng J.;
RT "Cadherin 23-C regulates microtubule networks by modifying CAMSAP3's
RT function.";
RL Sci. Rep. 6:28706-28706(2016).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28860385; DOI=10.1126/science.aam9335;
RA Zenker J., White M.D., Templin R.M., Parton R.G., Thorn-Seshold O.,
RA Bissiere S., Plachta N.;
RT "A microtubule-organizing center directing intracellular transport in the
RT early mouse embryo.";
RL Science 357:925-928(2017).
RN [14]
RP INTERACTION WITH AKNA.
RX PubMed=30787442; DOI=10.1038/s41586-019-0962-4;
RA Camargo Ortega G., Falk S., Johansson P.A., Peyre E., Broix L., Sahu S.K.,
RA Hirst W., Schlichthaerle T., De Juan Romero C., Draganova K., Vinopal S.,
RA Chinnappa K., Gavranovic A., Karakaya T., Steininger T., Merl-Pham J.,
RA Feederle R., Shao W., Shi S.H., Hauck S.M., Jungmann R., Bradke F.,
RA Borrell V., Geerlof A., Reber S., Tiwari V.K., Huttner W.B.,
RA Wilsch-Braeuninger M., Nguyen L., Goetz M.;
RT "The centrosome protein AKNA regulates neurogenesis via microtubule
RT organization.";
RL Nature 567:113-117(2019).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=32482850; DOI=10.1073/pnas.1907335117;
RA Robinson A.M., Takahashi S., Brotslaw E.J., Ahmad A., Ferrer E.,
RA Procissi D., Richter C.P., Cheatham M.A., Mitchell B.J., Zheng J.;
RT "CAMSAP3 facilitates basal body polarity and the formation of the central
RT pair of microtubules in motile cilia.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:13571-13579(2020).
RN [16]
RP STRUCTURE BY NMR OF 1112-1240.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of a murine hypothetical protein from RIKEN cDNA
RT 2310057j16.";
RL Submitted (JUN-2003) to the PDB data bank.
CC -!- FUNCTION: Key microtubule-organizing protein that specifically binds
CC the minus-end of non-centrosomal microtubules and regulates their
CC dynamics and organization (PubMed:23169647, PubMed:24706919,
CC PubMed:26715742). Specifically recognizes growing microtubule minus-
CC ends and autonomously decorates and stabilizes microtubule lattice
CC formed by microtubule minus-end polymerization (PubMed:24706919). Acts
CC on free microtubule minus-ends that are not capped by microtubule-
CC nucleating proteins or other factors and protects microtubule minus-
CC ends from depolymerization (PubMed:24706919). In addition, it also
CC reduces the velocity of microtubule polymerization (PubMed:24706919).
CC Required for the biogenesis and the maintenance of zonula adherens by
CC anchoring the minus-end of microtubules to zonula adherens and by
CC recruiting the kinesin KIFC3 to those junctional sites (By similarity).
CC Required for orienting the apical-to-basal polarity of microtubules in
CC epithelial cells: acts by tethering non-centrosomal microtubules to the
CC apical cortex, leading to their longitudinal orientation
CC (PubMed:26715742). Plays a key role in early embryos, which lack
CC centrosomes: accumulates at the microtubule bridges that connect pairs
CC of cells and enables the formation of a non-centrosomal microtubule-
CC organizing center that directs intracellular transport in the early
CC embryo (PubMed:28860385). Couples non-centrosomal microtubules with
CC actin: interaction with MACF1 at the minus ends of non-centrosomal
CC microtubules, tethers the microtubules to actin filaments, regulating
CC focal adhesion size and cell migration (By similarity). Plays a key
CC role in the generation of non-centrosomal microtubules by accumulating
CC in the pericentrosomal region and cooperating with KATNA1 to release
CC non-centrosomal microtubules from the centrosome (By similarity).
CC Through the microtubule cytoskeleton, also regulates the organization
CC of cellular organelles including the Golgi and the early endosomes (By
CC similarity). Through the microtubule cytoskeleton, also regulates the
CC organization of cellular organelles including the Golgi and the early
CC endosomes (By similarity). Through interaction with AKAP9, involved in
CC translocation of Golgi vesicles in epithelial cells, where microtubules
CC are mainly non-centrosomal (By similarity). Plays an important role in
CC motile cilia function by facilitatating proper orientation of basal
CC bodies and formation of central microtubule pairs in motile cilia
CC (PubMed:32482850). {ECO:0000250|UniProtKB:Q9P1Y5,
CC ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24706919,
CC ECO:0000269|PubMed:26715742, ECO:0000269|PubMed:28860385,
CC ECO:0000269|PubMed:32482850}.
CC -!- SUBUNIT: Interacts with PLEKHA7 (By similarity). Interacts with CAMSAP2
CC (PubMed:23169647). Interacts with KATNA1 and KATNB1; leading to
CC regulate the length of CAMSAP3-decorated microtubule stretches (By
CC similarity). Interacts with AKAP9; regulating Golgi assembly in
CC epithelial cells (By similarity). Interacts with MACF1 (By similarity).
CC Interacts with isoform C of CDH23; leading to inhibit CAMSAP3 ability
CC to induce microtubule bundle formation (PubMed:27349180). Interacts
CC with AKNA (PubMed:30787442). {ECO:0000250|UniProtKB:Q9P1Y5,
CC ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:27349180,
CC ECO:0000269|PubMed:30787442}.
CC -!- INTERACTION:
CC Q80VC9; Q8C1B1: Camsap2; NbExp=2; IntAct=EBI-2125556, EBI-8839434;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24244856, ECO:0000269|PubMed:24706919,
CC ECO:0000269|PubMed:26715742, ECO:0000269|PubMed:28860385}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:Q9P1Y5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9P1Y5}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:32482850}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:32482850}. Note=Scattered in the cytoplasm,
CC associated with the minus-end of microtubules and also detected at the
CC centrosomes (PubMed:24706919, PubMed:26715742). Decorates the minus-end
CC of microtubules by decreasing the rate of tubulin incorporation and
CC remaining bound (By similarity). Localizes along zonula adherens only
CC at mature cell-cell contacts (By similarity). In early embryos,
CC accumulates at the microtubule bridges that connect pairs of cells:
CC this structure is present in early embryos, which lack centrosomes
CC (PubMed:28860385). This cytokinetic bridge does not undergo
CC stereotypical abscission after cell division (PubMed:28860385).
CC Accumulates to the pericentrosomal region following interaction with
CC KATNA1 (By similarity). {ECO:0000250|UniProtKB:Q9P1Y5,
CC ECO:0000269|PubMed:28860385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=17;
CC Name=1; Synonyms=Ld {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80VC9-2; Sequence=VSP_013705;
CC Name=3; Synonyms=Lc variant 2 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-3; Sequence=VSP_059237;
CC Name=4; Synonyms=Lb variant 2 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-4; Sequence=VSP_059238;
CC Name=5; Synonyms=La variant 2 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-5; Sequence=VSP_059239;
CC Name=6; Synonyms=Sc variant 2 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-6; Sequence=VSP_059237, VSP_059241;
CC Name=7; Synonyms=Sb variant 2 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-7; Sequence=VSP_059238, VSP_059241;
CC Name=8; Synonyms=Sa variant 2 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-8; Sequence=VSP_059239, VSP_059241;
CC Name=9; Synonyms=Sd variant 2 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-9; Sequence=VSP_059241;
CC Name=10; Synonyms=Ld variant 1 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-10; Sequence=VSP_059240;
CC Name=11; Synonyms=Lb variant 1 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-11; Sequence=VSP_059238, VSP_059240;
CC Name=12; Synonyms=Lc variant 1 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-12; Sequence=VSP_059237, VSP_059240;
CC Name=13; Synonyms=Sd variant 1 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-13; Sequence=VSP_059240, VSP_059241;
CC Name=14; Synonyms=La variant 1 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-14; Sequence=VSP_059239, VSP_059240;
CC Name=15; Synonyms=Sc variant 1 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-15; Sequence=VSP_059237, VSP_059240, VSP_059241;
CC Name=16; Synonyms=Sb variant 1 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-16; Sequence=VSP_059238, VSP_059240, VSP_059241;
CC Name=17; Synonyms=Sa variant 1 {ECO:0000303|PubMed:24244856};
CC IsoId=Q80VC9-17; Sequence=VSP_059239, VSP_059240, VSP_059241;
CC -!- TISSUE SPECIFICITY: Expressed at the apical surface of respiratory
CC epithelia, as well as in the acini of submucosal glands (at protein
CC level)(PubMed:32482850). In cochlea, restricted to the organ of Corti
CC and increases during development (at protein level) (PubMed:24244856).
CC Highly expressed in both sensory hair cells and supporting cells
CC (PubMed:24244856). {ECO:0000269|PubMed:24244856,
CC ECO:0000269|PubMed:32482850}.
CC -!- DOMAIN: The CKK domain binds microtubules and specifically recognizes
CC the minus-end of microtubules. {ECO:0000250|UniProtKB:Q9P1Y5,
CC ECO:0000255|PROSITE-ProRule:PRU00841}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but show growth defects
CC (PubMed:26715742). Disorganization of epithelial architecture,
CC characterized by impaired apical-to-basal polarity of microtubules in
CC epithelial cells (PubMed:26715742). Defects in the stereotypic
CC positioning of the nucleus and Golgi apparatus (PubMed:26715742). Mice
CC display subfertility in both sexes and severe nasal airway blockage
CC leading to coughing, sneezing, hyposmia and rhinosinusitis
CC (PubMed:32482850). Majority of cilia lack the central microtubule pair
CC in their axoneme and display disorientated basal bodies and defects in
CC ciliary motion, which is no longer synchronized (PubMed:32482850).
CC {ECO:0000269|PubMed:26715742, ECO:0000269|PubMed:32482850}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
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DR EMBL; KC426930; AGX24909.1; -; mRNA.
DR EMBL; KC426931; AGX24910.1; -; mRNA.
DR EMBL; KC426932; AGX24911.1; -; mRNA.
DR EMBL; KC426933; AGX24912.1; -; mRNA.
DR EMBL; KC426934; AGX24913.1; -; mRNA.
DR EMBL; KC426935; AGX24914.1; -; mRNA.
DR EMBL; KC426936; AGX24915.1; -; mRNA.
DR EMBL; KC426937; AGX24916.1; -; mRNA.
DR EMBL; KC426938; AGX24917.1; -; mRNA.
DR EMBL; KC426939; AGX24918.1; -; mRNA.
DR EMBL; KC426940; AGX24919.1; -; mRNA.
DR EMBL; KC426941; AGX24920.1; -; mRNA.
DR EMBL; KC426942; AGX24921.1; -; mRNA.
DR EMBL; KC426943; AGX24922.1; -; mRNA.
DR EMBL; KC426944; AGX24923.1; -; mRNA.
DR EMBL; KC426945; AGX24924.1; -; mRNA.
DR EMBL; AK081728; BAC38313.1; -; mRNA.
DR EMBL; AC170806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466566; EDL21921.1; -; Genomic_DNA.
DR EMBL; BC048787; AAH48787.1; -; mRNA.
DR EMBL; AK220401; BAD90256.1; -; Transcribed_RNA.
DR CCDS; CCDS22064.1; -. [Q80VC9-1]
DR CCDS; CCDS52469.1; -. [Q80VC9-10]
DR CCDS; CCDS85488.1; -. [Q80VC9-5]
DR CCDS; CCDS85489.1; -. [Q80VC9-3]
DR CCDS; CCDS85490.1; -. [Q80VC9-4]
DR CCDS; CCDS90365.1; -. [Q80VC9-15]
DR CCDS; CCDS90366.1; -. [Q80VC9-7]
DR CCDS; CCDS90367.1; -. [Q80VC9-13]
DR RefSeq; NP_001157221.1; NM_001163749.1. [Q80VC9-10]
DR RefSeq; NP_001334040.1; NM_001347111.1. [Q80VC9-5]
DR RefSeq; NP_001334041.1; NM_001347112.1. [Q80VC9-4]
DR RefSeq; NP_001334042.1; NM_001347113.1. [Q80VC9-3]
DR RefSeq; NP_081447.2; NM_027171.3. [Q80VC9-1]
DR RefSeq; XP_006508937.1; XM_006508874.1.
DR RefSeq; XP_006508939.1; XM_006508876.1.
DR RefSeq; XP_006508941.1; XM_006508878.1.
DR PDB; 1UGJ; NMR; -; A=1113-1240.
DR PDB; 5LZN; X-ray; 1.40 A; A=1121-1239.
DR PDB; 5M50; EM; 5.30 A; C=1121-1238.
DR PDB; 5OW5; X-ray; 1.70 A; E/F=461-470.
DR PDBsum; 1UGJ; -.
DR PDBsum; 5LZN; -.
DR PDBsum; 5M50; -.
DR PDBsum; 5OW5; -.
DR AlphaFoldDB; Q80VC9; -.
DR SMR; Q80VC9; -.
DR BioGRID; 213622; 18.
DR DIP; DIP-52404N; -.
DR IntAct; Q80VC9; 5.
DR MINT; Q80VC9; -.
DR STRING; 10090.ENSMUSP00000125993; -.
DR iPTMnet; Q80VC9; -.
DR PhosphoSitePlus; Q80VC9; -.
DR SwissPalm; Q80VC9; -.
DR MaxQB; Q80VC9; -.
DR PaxDb; Q80VC9; -.
DR PeptideAtlas; Q80VC9; -.
DR PRIDE; Q80VC9; -.
DR ProteomicsDB; 265638; -. [Q80VC9-1]
DR ProteomicsDB; 265639; -. [Q80VC9-2]
DR ProteomicsDB; 265640; -. [Q80VC9-3]
DR ProteomicsDB; 265641; -. [Q80VC9-4]
DR ProteomicsDB; 265642; -. [Q80VC9-5]
DR ProteomicsDB; 265643; -. [Q80VC9-6]
DR ProteomicsDB; 265644; -. [Q80VC9-7]
DR ProteomicsDB; 265645; -. [Q80VC9-8]
DR ProteomicsDB; 265646; -. [Q80VC9-9]
DR ProteomicsDB; 265647; -. [Q80VC9-10]
DR ProteomicsDB; 265648; -. [Q80VC9-11]
DR ProteomicsDB; 265649; -. [Q80VC9-12]
DR ProteomicsDB; 265650; -. [Q80VC9-13]
DR ProteomicsDB; 265651; -. [Q80VC9-14]
DR ProteomicsDB; 265652; -. [Q80VC9-15]
DR ProteomicsDB; 265653; -. [Q80VC9-16]
DR ProteomicsDB; 265654; -. [Q80VC9-17]
DR Antibodypedia; 50549; 80 antibodies from 19 providers.
DR DNASU; 69697; -.
DR Ensembl; ENSMUST00000057028; ENSMUSP00000058958; ENSMUSG00000044433. [Q80VC9-1]
DR Ensembl; ENSMUST00000171962; ENSMUSP00000125993; ENSMUSG00000044433. [Q80VC9-10]
DR Ensembl; ENSMUST00000207077; ENSMUSP00000146852; ENSMUSG00000044433. [Q80VC9-4]
DR Ensembl; ENSMUST00000207432; ENSMUSP00000146896; ENSMUSG00000044433. [Q80VC9-5]
DR Ensembl; ENSMUST00000207533; ENSMUSP00000147209; ENSMUSG00000044433. [Q80VC9-7]
DR Ensembl; ENSMUST00000207712; ENSMUSP00000146565; ENSMUSG00000044433. [Q80VC9-13]
DR Ensembl; ENSMUST00000207970; ENSMUSP00000146772; ENSMUSG00000044433. [Q80VC9-3]
DR Ensembl; ENSMUST00000208240; ENSMUSP00000146359; ENSMUSG00000044433. [Q80VC9-15]
DR GeneID; 69697; -.
DR KEGG; mmu:69697; -.
DR UCSC; uc009krw.2; mouse. [Q80VC9-1]
DR UCSC; uc012fym.1; mouse.
DR UCSC; uc033jds.1; mouse.
DR UCSC; uc033jdu.1; mouse.
DR UCSC; uc033jdv.1; mouse.
DR UCSC; uc033jdy.1; mouse.
DR UCSC; uc033jec.1; mouse.
DR UCSC; uc033jed.1; mouse.
DR CTD; 57662; -.
DR MGI; MGI:1916947; Camsap3.
DR VEuPathDB; HostDB:ENSMUSG00000044433; -.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_004833_1_0_1; -.
DR InParanoid; Q80VC9; -.
DR OMA; PERPVCE; -.
DR OrthoDB; 741937at2759; -.
DR PhylomeDB; Q80VC9; -.
DR TreeFam; TF315529; -.
DR BioGRID-ORCS; 69697; 6 hits in 71 CRISPR screens.
DR EvolutionaryTrace; Q80VC9; -.
DR PRO; PR:Q80VC9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q80VC9; protein.
DR Bgee; ENSMUSG00000044433; Expressed in secondary oocyte and 179 other tissues.
DR ExpressionAtlas; Q80VC9; baseline and differential.
DR Genevisible; Q80VC9; MM.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0036449; C:microtubule minus-end; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005915; C:zonula adherens; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0003341; P:cilium movement; IMP:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IDA:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR GO; GO:0098840; P:protein transport along microtubule; IDA:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; ISS:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0033043; P:regulation of organelle organization; IGI:UniProtKB.
DR GO; GO:0045218; P:zonula adherens maintenance; ISS:UniProtKB.
DR Gene3D; 3.10.20.360; -; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595; PTHR21595; 1.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1252
FT /note="Calmodulin-regulated spectrin-associated protein 3"
FT /id="PRO_0000050800"
FT DOMAIN 203..312
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1112..1246
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 183..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 595..629
FT /evidence="ECO:0000255"
FT COILED 696..727
FT /evidence="ECO:0000255"
FT COILED 896..943
FT /evidence="ECO:0000255"
FT COMPBIAS 336..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT MOD_RES 797
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P1Y5"
FT VAR_SEQ 207
FT /note="S -> SCPTRWYWKLVP (in isoform 3, isoform 6, isoform
FT 12 and isoform 15)"
FT /id="VSP_059237"
FT VAR_SEQ 207
FT /note="S -> SHAIAFCLKESGNKPPM (in isoform 4, isoform 7,
FT isoform 11 and isoform 16)"
FT /id="VSP_059238"
FT VAR_SEQ 207
FT /note="S -> SCPTRWYWKLVPHAIAFCLKESGNKPPM (in isoform 5,
FT isoform 8, isoform 14 and isoform 17)"
FT /id="VSP_059239"
FT VAR_SEQ 331
FT /note="H -> HV (in isoform 10, isoform 11, isoform 12,
FT isoform 13, isoform 14, isoform 15, isoform 16 and isoform
FT 17)"
FT /id="VSP_059240"
FT VAR_SEQ 398..813
FT /note="Missing (in isoform 6, isoform 7, isoform 8, isoform
FT 9, isoform 13, isoform 15, isoform 16 and isoform 17)"
FT /id="VSP_059241"
FT VAR_SEQ 1042..1111
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_013705"
FT MUTAGEN 608..612
FT /note="LEEKR->AAAAA: Retains the ability to interact with
FT microtubules but abolishes the apical localization in
FT epithelial cells."
FT /evidence="ECO:0000269|PubMed:26715742"
FT CONFLICT 199..207
FT /note="DGASPAQPS -> LTSLSSCPQ (in Ref. 6; BAD90256)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="K -> E (in Ref. 2; BAC38313)"
FT /evidence="ECO:0000305"
FT HELIX 462..469
FT /evidence="ECO:0007829|PDB:5OW5"
FT HELIX 1125..1134
FT /evidence="ECO:0007829|PDB:5LZN"
FT TURN 1135..1137
FT /evidence="ECO:0007829|PDB:1UGJ"
FT HELIX 1143..1155
FT /evidence="ECO:0007829|PDB:5LZN"
FT STRAND 1161..1167
FT /evidence="ECO:0007829|PDB:5LZN"
FT STRAND 1172..1178
FT /evidence="ECO:0007829|PDB:5LZN"
FT TURN 1180..1182
FT /evidence="ECO:0007829|PDB:5LZN"
FT STRAND 1185..1192
FT /evidence="ECO:0007829|PDB:5LZN"
FT STRAND 1194..1196
FT /evidence="ECO:0007829|PDB:5LZN"
FT HELIX 1198..1200
FT /evidence="ECO:0007829|PDB:5LZN"
FT STRAND 1201..1208
FT /evidence="ECO:0007829|PDB:5LZN"
FT TURN 1209..1212
FT /evidence="ECO:0007829|PDB:5LZN"
FT STRAND 1213..1217
FT /evidence="ECO:0007829|PDB:5LZN"
FT STRAND 1218..1221
FT /evidence="ECO:0007829|PDB:1UGJ"
FT STRAND 1228..1231
FT /evidence="ECO:0007829|PDB:5LZN"
FT HELIX 1233..1235
FT /evidence="ECO:0007829|PDB:5LZN"
SQ SEQUENCE 1252 AA; 135175 MW; 1E14AA8640108CF4 CRC64;
MVEAAPAGSG PLRRTFLVPE IKSLDQYDFS RAKAAASLAW VLRAAFGGAE HVPPELWEPF
YTDQYAQEHV KPPVTRLLLS AELYCRAWRQ ALPQLEPSPS PSALLALLAR RGTVPSLPEH
PVREADLKHQ PILMGAHLAV IDALMVAFSF EWTKTLPGPL ALSSLEHKLL FWVDTTVRRL
QEKTEQEAAQ RASPAAPLDG ASPAQPSIRY RKDRAIARRA PCFPNVTTLQ DLASGAALAA
TIHCYCPQLL RLEEVCLKDP MSVADSLYNL QLVQDFCASH LPRGCPLSLE DLLYVPPPLK
VNLVVLLAEM YMCFEVLKPD FVQAKDLPDG HAVSPRNTET VPSQNNSGSS SPVFNFRHPL
LSPGGPQSPL RGSTGSLKSS PSMSHMEALG KAWNRQLSRP LSQAVSFSTP FGLDSDVDVV
MGDPVLLRSV SSDSLGPPRP VSTSSRNSAQ PAPESGDLPT IEEALQIIHS AEPRLLPDGA
ADGSFYLHSP EGLSKPPLSP YPPEGASKPL SDRLNKAPIY ISHPENPSKS SPCSTGEILK
PPPPSEGSPK AVASSPAANN SEVKMTSFAE RKKQLVKAEA ESGLGSPTST PVAPEALSSE
MSELGARLEE KRRAIEAQKR RIEAIFAKHR QRLGKSAFLQ VQPREAAGEA EEEAELGSVP
GGERPAGEGQ GEPSLRHKSV TFSPDLGPVP PEGLGDYNRA VSKLSAALSS LQRDMQRLTD
QQQRLLAPPE APGPAPPPAA WVIPGPATGP KAASPSPARR APAARRSPGP GPSPTPRSPK
HARPAELKLA PLTRVLTPPH DVDSLPHLRK FSPSQVPVQT RSSILLSEGT PPEEPTTKPA
LIEIPLASLG EPAADEEGDG SPPGAEDSLE EEASSEGEPR SGLGFFYKDE DKPEDEMAQK
RASLLERQQR RVEEARRRKQ WQEAEKEQKR EEAARLAQEA PGLAFTTPVV ASAAPVATLA
PTTRAMAPAE EEVGPRRGDF TRLEYERRAQ LKLMDDLDKV LRPRASGTGG PGRGGRRATR
PRSGCCDDSA LARSPARGLL GSRLSKVYSQ STLSLSTVAN EAPNNLGVKR PTSRAPSPSG
LMSPSRLPGS RERDWENGSN ASSPASVPEY TGPRLYKEPS AKSNKFIIHN ALSHCCLAGK
VNEPQKNRIL EEIEKSKANH FLILFRDSSC QFRALYTLSG ETEELSRLAG YGPRTVTPAM
VEGIYKYNSD RKRFTQIPAK TMSMSVDAFT IQGHLWQSKK PTTPKKGGGT PK
