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Database: UniProt
Entry: CAMP3_MOUSE
LinkDB: CAMP3_MOUSE
Original site: CAMP3_MOUSE 
ID   CAMP3_MOUSE             Reviewed;        1252 AA.
AC   Q80VC9; E9Q5B0; Q5DTW9; Q8BUZ0; U5LGR7; U5LGS1; U5LGS5; U5LGT0;
AC   U5LHT8; U5LHU4; U5LHW1; U5LHW4; U5LHW9; U5LK15; U5LK19; U5LK24;
AC   U5LK70; U5LK74; U5LK79;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   31-JUL-2019, entry version 147.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6; 7; 8; 9; 10; 11;
RP   12; 13; 14; 15; 16 AND 17), SUBCELLULAR LOCATION, AND TISSUE
RP   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.,
RA   Homma K., Hackney C.M., Dallos P., Cheatham M.A.;
RT   "Marshalin, a microtubule minus-end binding protein, regulates
RT   cytoskeletal 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-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
RP   SCALE 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
RT   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
RT   organization of 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
RT   Patronin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:5860-5865(2014).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP   OF 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.,
RA   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
RT   the 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.,
RA   Sahu S.K., Hirst W., Schlichthaerle T., De Juan Romero C.,
RA   Draganova K., Vinopal S., Chinnappa K., Gavranovic A., Karakaya T.,
RA   Steininger T., Merl-Pham J., Feederle R., Shao W., Shi S.H.,
RA   Hauck S.M., Jungmann R., Bradke F., Borrell V., Geerlof A., Reber S.,
RA   Tiwari V.K., Huttner W.B., 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   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
CC       binds the minus-end of non-centrosomal microtubules and regulates
CC       their dynamics and organization (PubMed:23169647, PubMed:24706919,
CC       PubMed:26715742). Specifically recognizes growing microtubule
CC       minus-ends and autonomously decorates and stabilizes microtubule
CC       lattice formed by microtubule minus-end polymerization
CC       (PubMed:24706919). Acts on free microtubule minus-ends that are
CC       not capped by microtubule-nucleating proteins or other factors and
CC       protects microtubule minus-ends from depolymerization
CC       (PubMed:24706919). In addition, it also reduces the velocity of
CC       microtubule polymerization (PubMed:24706919). Required for the
CC       biogenesis and the maintenance of zonula adherens by anchoring the
CC       minus-end of microtubules to zonula adherens and by recruiting the
CC       kinesin KIFC3 to those junctional sites (By similarity). Required
CC       for orienting the apical-to-basal polarity of microtubules in
CC       epithelial cells: acts by tethering non-centrosomal microtubules
CC       to the 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
CC       pairs of cells and enables the formation of a non-centrosomal
CC       microtubule-organizing center that directs intracellular transport
CC       in the early embryo (PubMed:28860385). Couples non-centrosomal
CC       microtubules with actin: interaction with MACF1 at the minus ends
CC       of non-centrosomal microtubules, tethers the microtubules to actin
CC       filaments, regulating focal adhesion size and cell migration (By
CC       similarity). Plays a key role in the generation of non-centrosomal
CC       microtubules by accumulating in the pericentrosomal region and
CC       cooperating with KATNA1 to release non-centrosomal microtubules
CC       from the centrosome (By similarity). Through the microtubule
CC       cytoskeleton, also regulates the organization of cellular
CC       organelles including the Golgi and the early endosomes (By
CC       similarity). Through the microtubule cytoskeleton, also regulates
CC       the organization of cellular organelles including the Golgi and
CC       the early endosomes (By similarity). Through interaction with
CC       AKAP9, involved in translocation of Golgi vesicles in epithelial
CC       cells, where microtubules are mainly non-centrosomal (By
CC       similarity). {ECO:0000250|UniProtKB:Q9P1Y5,
CC       ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24706919,
CC       ECO:0000269|PubMed:26715742, ECO:0000269|PubMed:28860385}.
CC   -!- SUBUNIT: Interacts with PLEKHA7 (By similarity). Interacts with
CC       CAMSAP2 (PubMed:23169647). Interacts with KATNA1 and KATNB1;
CC       leading to regulate the length of CAMSAP3-decorated microtubule
CC       stretches (By similarity). Interacts with AKAP9; regulating Golgi
CC       assembly in epithelial cells (By similarity). Interacts with MACF1
CC       (By similarity). Interacts with isoform C of CDH23; leading to
CC       inhibit CAMSAP3 ability to induce microtubule bundle formation
CC       (PubMed:27349180). Interacts with AKNA (PubMed:30787442).
CC       {ECO:0000250|UniProtKB:Q9P1Y5, ECO:0000269|PubMed:23169647,
CC       ECO:0000269|PubMed:27349180, ECO:0000269|PubMed:30787442}.
CC   -!- INTERACTION:
CC       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}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q9P1Y5}. Note=Scattered in the
CC       cytoplasm, associated with the minus-end of microtubules and also
CC       detected at the centrosomes (PubMed:24706919, PubMed:26715742).
CC       Decorates the minus-end of microtubules by decreasing the rate of
CC       tubulin incorporation and remaining bound (By similarity).
CC       Localizes along zonula adherens only at mature cell-cell contacts
CC       (By similarity). In early embryos, accumulates at the microtubule
CC       bridges that connect pairs of cells: this structure is present in
CC       early embryos, which lack centrosomes (PubMed:28860385). This
CC       cytokinetic bridge does not undergo stereotypical abscission after
CC       cell division (PubMed:28860385). Accumulates to the
CC       pericentrosomal region following interaction with KATNA1 (By
CC       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         Note=No experimental confirmation available.;
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: In cochlea, restricted to the organ of Corti
CC       and increases during development (at protein level)
CC       (PubMed:24244856). Highly expressed in both sensory hair cells and
CC       supporting cells (PubMed:24244856). {ECO:0000269|PubMed:24244856}.
CC   -!- DOMAIN: The CKK domain binds microtubules and specifically
CC       recognizes the minus-end of microtubules.
CC       {ECO:0000250|UniProtKB:Q9P1Y5, ECO:0000255|PROSITE-
CC       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
CC       in epithelial cells (PubMed:26715742). Defects in the stereotypic
CC       positioning of the nucleus and Golgi apparatus (PubMed:26715742).
CC       {ECO:0000269|PubMed:26715742}.
CC   -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00841}.
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   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   SMR; Q80VC9; -.
DR   BioGrid; 213622; 4.
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   PaxDb; Q80VC9; -.
DR   PeptideAtlas; Q80VC9; -.
DR   PRIDE; Q80VC9; -.
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   eggNOG; KOG3654; Eukaryota.
DR   eggNOG; ENOG4111D0B; LUCA.
DR   GeneTree; ENSGT00950000182975; -.
DR   HOGENOM; HOG000059671; -.
DR   InParanoid; Q80VC9; -.
DR   KO; K17493; -.
DR   OMA; LRDPFYC; -.
DR   OrthoDB; 741937at2759; -.
DR   PhylomeDB; Q80VC9; -.
DR   TreeFam; TF315529; -.
DR   EvolutionaryTrace; Q80VC9; -.
DR   PRO; PR:Q80VC9; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000044433; Expressed in 201 organ(s), highest expression level in secondary oocyte.
DR   ExpressionAtlas; Q80VC9; baseline and differential.
DR   Genevisible; Q80VC9; MM.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0036449; C:microtubule minus-end; IDA:UniProtKB.
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: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:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB.
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; IPR031372; CAMSAP_CC1.
DR   InterPro; IPR022613; CAMSAP_CH.
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; 2.
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; Coiled coil;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Microtubule; Phosphoprotein; Reference proteome.
FT   CHAIN         1   1252       Calmodulin-regulated spectrin-associated
FT                                protein 3.
FT                                /FTId=PRO_0000050800.
FT   DOMAIN      203    312       Calponin-homology (CH).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00044}.
FT   DOMAIN     1112   1246       CKK. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00841}.
FT   COILED      595    629       {ECO:0000255}.
FT   COILED      696    727       {ECO:0000255}.
FT   COILED      896    943       {ECO:0000255}.
FT   COMPBIAS    496    549       Pro-rich.
FT   COMPBIAS    728    839       Pro-rich.
FT   MOD_RES     184    184       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     193    193       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     334    334       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     347    347       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     351    351       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     368    368       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     373    373       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     382    382       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     548    548       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     555    555       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     561    561       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     683    683       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     767    767       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   MOD_RES     797    797       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     812    812       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     881    881       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1077   1077       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9P1Y5}.
FT   VAR_SEQ     207    207       S -> SCPTRWYWKLVP (in isoform 3, isoform
FT                                6, isoform 12 and isoform 15).
FT                                /FTId=VSP_059237.
FT   VAR_SEQ     207    207       S -> SHAIAFCLKESGNKPPM (in isoform 4,
FT                                isoform 7, isoform 11 and isoform 16).
FT                                /FTId=VSP_059238.
FT   VAR_SEQ     207    207       S -> SCPTRWYWKLVPHAIAFCLKESGNKPPM (in
FT                                isoform 5, isoform 8, isoform 14 and
FT                                isoform 17).
FT                                /FTId=VSP_059239.
FT   VAR_SEQ     331    331       H -> HV (in isoform 10, isoform 11,
FT                                isoform 12, isoform 13, isoform 14,
FT                                isoform 15, isoform 16 and isoform 17).
FT                                /FTId=VSP_059240.
FT   VAR_SEQ     398    813       Missing (in isoform 6, isoform 7, isoform
FT                                8, isoform 9, isoform 13, isoform 15,
FT                                isoform 16 and isoform 17).
FT                                /FTId=VSP_059241.
FT   VAR_SEQ    1042   1111       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.6}.
FT                                /FTId=VSP_013705.
FT   MUTAGEN     608    612       LEEKR->AAAAA: Retains the ability to
FT                                interact with microtubules but abolishes
FT                                the apical localization in epithelial
FT                                cells. {ECO:0000269|PubMed:26715742}.
FT   CONFLICT    199    207       DGASPAQPS -> LTSLSSCPQ (in Ref. 6;
FT                                BAD90256). {ECO:0000305}.
FT   CONFLICT    892    892       K -> E (in Ref. 2; BAC38313).
FT                                {ECO:0000305}.
FT   HELIX       462    469       {ECO:0000244|PDB:5OW5}.
FT   HELIX      1125   1134       {ECO:0000244|PDB:5LZN}.
FT   TURN       1135   1137       {ECO:0000244|PDB:1UGJ}.
FT   HELIX      1143   1155       {ECO:0000244|PDB:5LZN}.
FT   STRAND     1161   1167       {ECO:0000244|PDB:5LZN}.
FT   STRAND     1172   1178       {ECO:0000244|PDB:5LZN}.
FT   TURN       1180   1182       {ECO:0000244|PDB:5LZN}.
FT   STRAND     1185   1192       {ECO:0000244|PDB:5LZN}.
FT   STRAND     1194   1196       {ECO:0000244|PDB:5LZN}.
FT   HELIX      1198   1200       {ECO:0000244|PDB:5LZN}.
FT   STRAND     1201   1208       {ECO:0000244|PDB:5LZN}.
FT   TURN       1209   1212       {ECO:0000244|PDB:5LZN}.
FT   STRAND     1213   1217       {ECO:0000244|PDB:5LZN}.
FT   STRAND     1218   1221       {ECO:0000244|PDB:1UGJ}.
FT   STRAND     1228   1231       {ECO:0000244|PDB:5LZN}.
FT   HELIX      1233   1235       {ECO:0000244|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
//
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