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Calmodulin-regulated spectrin-associated protein 3 (Marshalin) (Protein Nezha)

 CAMP3_MOUSE             Reviewed;        1252 AA.
Q80VC9; E9Q5B0; Q5DTW9; Q8BUZ0; U5LGR7; U5LGS1; U5LGS5; U5LGT0;
U5LHT8; U5LHU4; U5LHW1; U5LHW4; U5LHW9; U5LK15; U5LK19; U5LK24;
U5LK70; U5LK74; U5LK79;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
18-JUL-2018, entry version 138.
RecName: Full=Calmodulin-regulated spectrin-associated protein 3 {ECO:0000305};
AltName: Full=Marshalin {ECO:0000303|PubMed:24244856};
AltName: Full=Protein Nezha {ECO:0000303|PubMed:23169647};
Name=Camsap3 {ECO:0000312|MGI:MGI:1916947};
Synonyms=Kiaa1543 {ECO:0000303|Ref.6};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6; 7; 8; 9; 10; 11;
12; 13; 14; 15; 16 AND 17), SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Cochlea;
PubMed=24244856; DOI=10.1242/bio.20135603;
Zheng J., Furness D., Duan C., Miller K.K., Edge R.M., Chen J.,
Homma K., Hackney C.M., Dallos P., Cheatham M.A.;
"Marshalin, a microtubule minus-end binding protein, regulates
cytoskeletal structure in the organ of Corti.";
Biol. Open 2:1192-1202(2013).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-1252 (ISOFORM 2).
TISSUE=Fetal brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 704-713, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-351; THR-797;
SER-812 AND SER-881, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, AND INTERACTION WITH CAMSAP2.
PubMed=23169647; DOI=10.1073/pnas.1218017109;
Tanaka N., Meng W., Nagae S., Takeichi M.;
"Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific
organization of noncentrosomal microtubules.";
Proc. Natl. Acad. Sci. U.S.A. 109:20029-20034(2012).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24706919; DOI=10.1073/pnas.1404133111;
Hendershott M.C., Vale R.D.;
"Regulation of microtubule minus-end dynamics by CAMSAPs and
Patronin.";
Proc. Natl. Acad. Sci. U.S.A. 111:5860-5865(2014).
[11]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
OF 608-LEU--ARG-612.
PubMed=26715742; DOI=10.1073/pnas.1520638113;
Toya M., Kobayashi S., Kawasaki M., Shioi G., Kaneko M., Ishiuchi T.,
Misaki K., Meng W., Takeichi M.;
"CAMSAP3 orients the apical-to-basal polarity of microtubule arrays in
epithelial cells.";
Proc. Natl. Acad. Sci. U.S.A. 113:332-337(2016).
[12]
INTERACTION WITH CDH23.
PubMed=27349180; DOI=10.1038/srep28706;
Takahashi S., Mui V.J., Rosenberg S.K., Homma K., Cheatham M.A.,
Zheng J.;
"Cadherin 23-C regulates microtubule networks by modifying CAMSAP3's
function.";
Sci. Rep. 6:28706-28706(2016).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=28860385; DOI=10.1126/science.aam9335;
Zenker J., White M.D., Templin R.M., Parton R.G., Thorn-Seshold O.,
Bissiere S., Plachta N.;
"A microtubule-organizing center directing intracellular transport in
the early mouse embryo.";
Science 357:925-928(2017).
[14]
STRUCTURE BY NMR OF 1112-1240.
RIKEN structural genomics initiative (RSGI);
"Solution structure of a murine hypothetical protein from RIKEN cDNA
2310057j16.";
Submitted (JUN-2003) to the PDB data bank.
-!- FUNCTION: Key microtubule-organizing protein that specifically
binds the minus-end of non-centrosomal microtubules and regulates
their dynamics and organization (PubMed:23169647, PubMed:24706919,
PubMed:26715742). Specifically recognizes growing microtubule
minus-ends and autonomously decorates and stabilizes microtubule
lattice formed by microtubule minus-end polymerization
(PubMed:24706919). Acts on free microtubule minus-ends that are
not capped by microtubule-nucleating proteins or other factors and
protects microtubule minus-ends from depolymerization
(PubMed:24706919). In addition, it also reduces the velocity of
microtubule polymerization (PubMed:24706919). Required for the
biogenesis and the maintenance of zonula adherens by anchoring the
minus-end of microtubules to zonula adherens and by recruiting the
kinesin KIFC3 to those junctional sites (By similarity). Required
for orienting the apical-to-basal polarity of microtubules in
epithelial cells: acts by tethering non-centrosomal microtubules
to the apical cortex, leading to their longitudinal orientation
(PubMed:26715742). Plays a key role in early embryos, which lack
centrosomes: accumulates at the microtubule bridges that connect
pairs of cells and enables the formation of a non-centrosomal
microtubule-organizing center that directs intracellular transport
in the early embryo (PubMed:28860385). Couples non-centrosomal
microtubules with actin: interaction with MACF1 at the minus ends
of non-centrosomal microtubules, tethers the microtubules to actin
filaments, regulating focal adhesion size and cell migration (By
similarity). Plays a key role in the generation of non-centrosomal
microtubules by accumulating in the pericentrosomal region and
cooperating with KATNA1 to release non-centrosomal microtubules
from the centrosome (By similarity). Through the microtubule
cytoskeleton, also regulates the organization of cellular
organelles including the Golgi and the early endosomes (By
similarity). Through the microtubule cytoskeleton, also regulates
the organization of cellular organelles including the Golgi and
the early endosomes (By similarity). Through interaction with
AKAP9, involved in translocation of Golgi vesicles in epithelial
cells, where microtubules are mainly non-centrosomal (By
similarity). {ECO:0000250|UniProtKB:Q9P1Y5,
ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:24706919,
ECO:0000269|PubMed:26715742, ECO:0000269|PubMed:28860385}.
-!- SUBUNIT: Interacts with PLEKHA7 (By similarity). Interacts with
CAMSAP2 (PubMed:23169647). Interacts with KATNA1 and KATNB1;
leading to regulate the length of CAMSAP3-decorated microtubule
stretches (By similarity). Interacts with AKAP9; regulating Golgi
assembly in epithelial cells (By similarity). Interacts with MACF1
(By similarity). Interacts with isoform C of CDH23; leading to
inhibit CAMSAP3 ability to induce microtubule bundle formation
(PubMed:27349180). {ECO:0000250|UniProtKB:Q9P1Y5,
ECO:0000269|PubMed:23169647, ECO:0000269|PubMed:27349180}.
-!- INTERACTION:
Q8C1B1:Camsap2; NbExp=2; IntAct=EBI-2125556, EBI-8839434;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:24244856, ECO:0000269|PubMed:24706919,
ECO:0000269|PubMed:26715742, ECO:0000269|PubMed:28860385}. Cell
junction, adherens junction {ECO:0000250|UniProtKB:Q9P1Y5}.
Cytoplasm {ECO:0000250|UniProtKB:Q9P1Y5}. Note=Scattered in the
cytoplasm, associated with the minus-end of microtubules and also
detected at the centrosomes (PubMed:24706919, PubMed:26715742).
Decorates the minus-end of microtubules by decreasing the rate of
tubulin incorporation and remaining bound (By similarity).
Localizes along zonula adherens only at mature cell-cell contacts
(By similarity). In early embryos, accumulates at the microtubule
bridges that connect pairs of cells: this structure is present in
early embryos, which lack centrosomes (PubMed:28860385). This
cytokinetic bridge does not undergo stereotypical abscission after
cell division (PubMed:28860385). Accumulates to the
pericentrosomal region following interaction with KATNA1 (By
similarity). {ECO:0000250|UniProtKB:Q9P1Y5,
ECO:0000269|PubMed:28860385}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=17;
Name=1; Synonyms=Ld {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-1; Sequence=Displayed;
Name=2;
IsoId=Q80VC9-2; Sequence=VSP_013705;
Note=No experimental confirmation available.;
Name=3; Synonyms=Lc variant 2 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-3; Sequence=VSP_059237;
Name=4; Synonyms=Lb variant 2 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-4; Sequence=VSP_059238;
Name=5; Synonyms=La variant 2 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-5; Sequence=VSP_059239;
Name=6; Synonyms=Sc variant 2 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-6; Sequence=VSP_059237, VSP_059241;
Name=7; Synonyms=Sb variant 2 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-7; Sequence=VSP_059238, VSP_059241;
Name=8; Synonyms=Sa variant 2 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-8; Sequence=VSP_059239, VSP_059241;
Name=9; Synonyms=Sd variant 2 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-9; Sequence=VSP_059241;
Name=10; Synonyms=Ld variant 1 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-10; Sequence=VSP_059240;
Name=11; Synonyms=Lb variant 1 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-11; Sequence=VSP_059238, VSP_059240;
Name=12; Synonyms=Lc variant 1 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-12; Sequence=VSP_059237, VSP_059240;
Name=13; Synonyms=Sd variant 1 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-13; Sequence=VSP_059240, VSP_059241;
Name=14; Synonyms=La variant 1 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-14; Sequence=VSP_059239, VSP_059240;
Name=15; Synonyms=Sc variant 1 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-15; Sequence=VSP_059237, VSP_059240, VSP_059241;
Name=16; Synonyms=Sb variant 1 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-16; Sequence=VSP_059238, VSP_059240, VSP_059241;
Name=17; Synonyms=Sa variant 1 {ECO:0000303|PubMed:24244856};
IsoId=Q80VC9-17; Sequence=VSP_059239, VSP_059240, VSP_059241;
-!- TISSUE SPECIFICITY: In cochlea, restricted to the organ of Corti
and increases during development (at protein level)
(PubMed:24244856). Highly expressed in both sensory hair cells and
supporting cells (PubMed:24244856). {ECO:0000269|PubMed:24244856}.
-!- DOMAIN: The CKK domain binds microtubules and specifically
recognizes the minus-end of microtubules.
{ECO:0000250|UniProtKB:Q9P1Y5, ECO:0000255|PROSITE-
ProRule:PRU00841}.
-!- DISRUPTION PHENOTYPE: Mice are viable but show growth defects
(PubMed:26715742). Disorganization of epithelial architecture,
characterized by impaired apical-to-basal polarity of microtubules
in epithelial cells (PubMed:26715742). Defects in the stereotypic
positioning of the nucleus and Golgi apparatus (PubMed:26715742).
{ECO:0000269|PubMed:26715742}.
-!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
ProRule:PRU00841}.
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EMBL; KC426930; AGX24909.1; -; mRNA.
EMBL; KC426931; AGX24910.1; -; mRNA.
EMBL; KC426932; AGX24911.1; -; mRNA.
EMBL; KC426933; AGX24912.1; -; mRNA.
EMBL; KC426934; AGX24913.1; -; mRNA.
EMBL; KC426935; AGX24914.1; -; mRNA.
EMBL; KC426936; AGX24915.1; -; mRNA.
EMBL; KC426937; AGX24916.1; -; mRNA.
EMBL; KC426938; AGX24917.1; -; mRNA.
EMBL; KC426939; AGX24918.1; -; mRNA.
EMBL; KC426940; AGX24919.1; -; mRNA.
EMBL; KC426941; AGX24920.1; -; mRNA.
EMBL; KC426942; AGX24921.1; -; mRNA.
EMBL; KC426943; AGX24922.1; -; mRNA.
EMBL; KC426944; AGX24923.1; -; mRNA.
EMBL; KC426945; AGX24924.1; -; mRNA.
EMBL; AK081728; BAC38313.1; -; mRNA.
EMBL; AC170806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466566; EDL21921.1; -; Genomic_DNA.
EMBL; BC048787; AAH48787.1; -; mRNA.
EMBL; AK220401; BAD90256.1; -; Transcribed_RNA.
CCDS; CCDS22064.1; -. [Q80VC9-1]
CCDS; CCDS52469.1; -. [Q80VC9-10]
CCDS; CCDS85488.1; -. [Q80VC9-5]
CCDS; CCDS85489.1; -. [Q80VC9-3]
CCDS; CCDS85490.1; -. [Q80VC9-4]
RefSeq; NP_001157221.1; NM_001163749.1. [Q80VC9-10]
RefSeq; NP_001334040.1; NM_001347111.1. [Q80VC9-5]
RefSeq; NP_001334041.1; NM_001347112.1. [Q80VC9-4]
RefSeq; NP_001334042.1; NM_001347113.1. [Q80VC9-3]
RefSeq; NP_081447.2; NM_027171.3. [Q80VC9-1]
RefSeq; XP_006508937.1; XM_006508874.1. [Q80VC9-14]
RefSeq; XP_006508939.1; XM_006508876.1. [Q80VC9-11]
RefSeq; XP_006508941.1; XM_006508878.1. [Q80VC9-12]
UniGene; Mm.390010; -.
PDB; 1UGJ; NMR; -; A=1113-1240.
PDB; 5LZN; X-ray; 1.40 A; A=1121-1239.
PDB; 5M50; EM; 5.30 A; C=1121-1238.
PDBsum; 1UGJ; -.
PDBsum; 5LZN; -.
PDBsum; 5M50; -.
ProteinModelPortal; Q80VC9; -.
SMR; Q80VC9; -.
BioGrid; 213622; 4.
DIP; DIP-52404N; -.
IntAct; Q80VC9; 7.
MINT; Q80VC9; -.
STRING; 10090.ENSMUSP00000125993; -.
iPTMnet; Q80VC9; -.
PhosphoSitePlus; Q80VC9; -.
PaxDb; Q80VC9; -.
PeptideAtlas; Q80VC9; -.
PRIDE; Q80VC9; -.
DNASU; 69697; -.
Ensembl; ENSMUST00000057028; ENSMUSP00000058958; ENSMUSG00000044433. [Q80VC9-1]
Ensembl; ENSMUST00000171962; ENSMUSP00000125993; ENSMUSG00000044433. [Q80VC9-10]
Ensembl; ENSMUST00000207077; ENSMUSP00000146852; ENSMUSG00000044433. [Q80VC9-4]
Ensembl; ENSMUST00000207432; ENSMUSP00000146896; ENSMUSG00000044433. [Q80VC9-5]
Ensembl; ENSMUST00000207533; ENSMUSP00000147209; ENSMUSG00000044433. [Q80VC9-7]
Ensembl; ENSMUST00000207712; ENSMUSP00000146565; ENSMUSG00000044433. [Q80VC9-13]
Ensembl; ENSMUST00000207970; ENSMUSP00000146772; ENSMUSG00000044433. [Q80VC9-3]
Ensembl; ENSMUST00000208240; ENSMUSP00000146359; ENSMUSG00000044433. [Q80VC9-15]
GeneID; 69697; -.
KEGG; mmu:69697; -.
UCSC; uc009krw.2; mouse. [Q80VC9-1]
UCSC; uc012fym.1; mouse.
UCSC; uc033jds.1; mouse.
UCSC; uc033jdu.1; mouse.
UCSC; uc033jdv.1; mouse.
UCSC; uc033jdy.1; mouse.
UCSC; uc033jec.1; mouse.
UCSC; uc033jed.1; mouse.
CTD; 57662; -.
MGI; MGI:1916947; Camsap3.
eggNOG; KOG3654; Eukaryota.
eggNOG; ENOG4111D0B; LUCA.
GeneTree; ENSGT00390000010026; -.
HOGENOM; HOG000059671; -.
InParanoid; Q80VC9; -.
KO; K17493; -.
OMA; RSGCCDD; -.
PhylomeDB; Q80VC9; -.
EvolutionaryTrace; Q80VC9; -.
PRO; PR:Q80VC9; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000044433; -.
CleanEx; MM_2310057J16RIK; -.
ExpressionAtlas; Q80VC9; baseline and differential.
Genevisible; Q80VC9; MM.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0036449; C:microtubule minus-end; IDA:UniProtKB.
GO; GO:0005915; C:zonula adherens; ISS:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB.
GO; GO:0030507; F:spectrin binding; IEA:InterPro.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IDA:UniProtKB.
GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:UniProtKB.
GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
GO; GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB.
GO; GO:0031175; P:neuron projection development; IEA:InterPro.
GO; GO:0098840; P:protein transport along microtubule; IDA:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:1903358; P:regulation of Golgi organization; ISS:UniProtKB.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
GO; GO:0031113; P:regulation of microtubule polymerization; IDA:UniProtKB.
GO; GO:0033043; P:regulation of organelle organization; IGI:UniProtKB.
GO; GO:0045218; P:zonula adherens maintenance; ISS:UniProtKB.
Gene3D; 3.10.20.360; -; 1.
InterPro; IPR032940; CAMSAP.
InterPro; IPR031372; CAMSAP_CC1.
InterPro; IPR022613; CAMSAP_CH.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR038209; CKK_dom_sf.
InterPro; IPR014797; CKK_domain.
InterPro; IPR011033; PRC_barrel-like_sf.
PANTHER; PTHR21595; PTHR21595; 1.
Pfam; PF17095; CAMSAP_CC1; 1.
Pfam; PF11971; CAMSAP_CH; 1.
Pfam; PF08683; CAMSAP_CKK; 1.
SMART; SM01051; CAMSAP_CKK; 1.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF50346; SSF50346; 1.
PROSITE; PS50021; CH; 1.
PROSITE; PS51508; CKK; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Microtubule; Phosphoprotein; Reference proteome.
CHAIN 1 1252 Calmodulin-regulated spectrin-associated
protein 3.
/FTId=PRO_0000050800.
DOMAIN 203 312 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 1112 1246 CKK. {ECO:0000255|PROSITE-
ProRule:PRU00841}.
COILED 595 629 {ECO:0000255}.
COILED 696 727 {ECO:0000255}.
COILED 896 943 {ECO:0000255}.
COMPBIAS 496 549 Pro-rich.
COMPBIAS 728 839 Pro-rich.
MOD_RES 184 184 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 334 334 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 351 351 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 555 555 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 561 561 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 767 767 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
MOD_RES 797 797 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 812 812 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 881 881 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1077 1077 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P1Y5}.
VAR_SEQ 207 207 S -> SCPTRWYWKLVP (in isoform 3, isoform
6, isoform 12 and isoform 15).
/FTId=VSP_059237.
VAR_SEQ 207 207 S -> SHAIAFCLKESGNKPPM (in isoform 4,
isoform 7, isoform 11 and isoform 16).
/FTId=VSP_059238.
VAR_SEQ 207 207 S -> SCPTRWYWKLVPHAIAFCLKESGNKPPM (in
isoform 5, isoform 8, isoform 14 and
isoform 17).
/FTId=VSP_059239.
VAR_SEQ 331 331 H -> HV (in isoform 10, isoform 11,
isoform 12, isoform 13, isoform 14,
isoform 15, isoform 16 and isoform 17).
/FTId=VSP_059240.
VAR_SEQ 398 813 Missing (in isoform 6, isoform 7, isoform
8, isoform 9, isoform 13, isoform 15,
isoform 16 and isoform 17).
/FTId=VSP_059241.
VAR_SEQ 1042 1111 Missing (in isoform 2).
{ECO:0000303|Ref.6}.
/FTId=VSP_013705.
MUTAGEN 608 612 LEEKR->AAAAA: Retains the ability to
interact with microtubules but abolishes
the apical localization in epithelial
cells. {ECO:0000269|PubMed:26715742}.
CONFLICT 199 207 DGASPAQPS -> LTSLSSCPQ (in Ref. 6;
BAD90256). {ECO:0000305}.
CONFLICT 892 892 K -> E (in Ref. 2; BAC38313).
{ECO:0000305}.
HELIX 1125 1134 {ECO:0000244|PDB:5LZN}.
TURN 1135 1137 {ECO:0000244|PDB:1UGJ}.
HELIX 1143 1155 {ECO:0000244|PDB:5LZN}.
STRAND 1161 1167 {ECO:0000244|PDB:5LZN}.
STRAND 1172 1178 {ECO:0000244|PDB:5LZN}.
TURN 1180 1182 {ECO:0000244|PDB:5LZN}.
STRAND 1185 1192 {ECO:0000244|PDB:5LZN}.
STRAND 1194 1196 {ECO:0000244|PDB:5LZN}.
HELIX 1198 1200 {ECO:0000244|PDB:5LZN}.
STRAND 1201 1208 {ECO:0000244|PDB:5LZN}.
TURN 1209 1212 {ECO:0000244|PDB:5LZN}.
STRAND 1213 1217 {ECO:0000244|PDB:5LZN}.
STRAND 1218 1221 {ECO:0000244|PDB:1UGJ}.
STRAND 1228 1231 {ECO:0000244|PDB:5LZN}.
HELIX 1233 1235 {ECO:0000244|PDB:5LZN}.
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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