CAMP3_HUMAN
ID CAMP3_HUMAN Reviewed; 1249 AA.
AC Q9P1Y5; Q8NDF1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 3 {ECO:0000305};
DE AltName: Full=Protein Nezha {ECO:0000303|PubMed:23169647};
GN Name=CAMSAP3 {ECO:0000312|HGNC:HGNC:29307};
GN Synonyms=KIAA1543 {ECO:0000303|PubMed:10819331};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Retinoblastoma;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-1249 (ISOFORMS 1/2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 407-1249 (ISOFORM 1/2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, MICROTUBULE-BINDING, AND INTERACTION WITH
RP PLEKHA7.
RX PubMed=19041755; DOI=10.1016/j.cell.2008.09.040;
RA Meng W., Mushika Y., Ichii T., Takeichi M.;
RT "Anchorage of microtubule minus ends to adherens junctions regulates
RT epithelial cell-cell contacts.";
RL Cell 135:948-959(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184; SER-193; SER-341;
RP SER-347; SER-368; SER-554; SER-560; SER-685 AND THR-799, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334 AND SER-814, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-341; SER-351;
RP SER-368; SER-373; SER-382; SER-769; SER-814 AND SER-1074, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH KATNA1 AND
RP KATNB1.
RX PubMed=24486153; DOI=10.1016/j.devcel.2014.01.001;
RA Jiang K., Hua S., Mohan R., Grigoriev I., Yau K.W., Liu Q., Katrukha E.A.,
RA Altelaar A.F., Heck A.J., Hoogenraad C.C., Akhmanova A.;
RT "Microtubule minus-end stabilization by polymerization-driven CAMSAP
RT deposition.";
RL Dev. Cell 28:295-309(2014).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-334; SER-547 AND
RP THR-799, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MACF1.
RX PubMed=27693509; DOI=10.1016/j.devcel.2016.09.003;
RA Ning W., Yu Y., Xu H., Liu X., Wang D., Wang J., Wang Y., Meng W.;
RT "The CAMSAP3-ACF7 complex couples noncentrosomal microtubules with actin
RT filaments to coordinate their dynamics.";
RL Dev. Cell 39:61-74(2016).
RN [18]
RP FUNCTION, AND INTERACTION WITH MACF1.
RX PubMed=27802168; DOI=10.1242/jcs.194878;
RA Noordstra I., Liu Q., Nijenhuis W., Hua S., Jiang K., Baars M.,
RA Remmelzwaal S., Martin M., Kapitein L.C., Akhmanova A.;
RT "Control of apico-basal epithelial polarity by the microtubule minus-end-
RT binding protein CAMSAP3 and spectraplakin ACF7.";
RL J. Cell Sci. 129:4278-4288(2016).
RN [19]
RP FUNCTION.
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 [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KATNA1.
RX PubMed=28386021; DOI=10.1242/jcs.198010;
RA Dong C., Xu H., Zhang R., Tanaka N., Takeichi M., Meng W.;
RT "CAMSAP3 accumulates in the pericentrosomal area and accompanies
RT microtubule release from the centrosome via katanin.";
RL J. Cell Sci. 130:1709-1715(2017).
RN [21]
RP FUNCTION, AND INTERACTION WITH AKAP9.
RX PubMed=28089391; DOI=10.1016/j.jgg.2016.11.005;
RA Wang J., Xu H., Jiang Y., Takahashi M., Takeichi M., Meng W.;
RT "CAMSAP3-dependent microtubule dynamics regulates Golgi assembly in
RT epithelial cells.";
RL J. Genet. Genomics 44:39-49(2017).
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:19041755, PubMed:23169647).
CC Specifically recognizes growing microtubule minus-ends and autonomously
CC decorates and stabilizes microtubule lattice formed by microtubule
CC minus-end polymerization (PubMed:24486153). Acts on free microtubule
CC minus-ends that are not capped by microtubule-nucleating proteins or
CC other factors and protects microtubule minus-ends from depolymerization
CC (PubMed:24486153). In addition, it also reduces the velocity of
CC microtubule polymerization (PubMed:24486153). 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 (PubMed:19041755). Required for
CC orienting the apical-to-basal polarity of microtubules in epithelial
CC cells: acts by tethering non-centrosomal microtubules to the apical
CC cortex, leading to their longitudinal orientation (PubMed:27802168,
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 (By similarity). 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 (PubMed:27693509). 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 (PubMed:28386021).
CC Through the microtubule cytoskeleton, also regulates the organization
CC of cellular organelles including the Golgi and the early endosomes
CC (PubMed:28089391). Through interaction with AKAP9, involved in
CC translocation of Golgi vesicles in epithelial cells, where microtubules
CC are mainly non-centrosomal (PubMed:28089391). Plays an important role
CC in motile cilia function by facilitatating proper orientation of basal
CC bodies and formation of central microtubule pairs in motile cilia (By
CC similarity). {ECO:0000250|UniProtKB:Q80VC9,
CC ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:23169647,
CC ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:26715742,
CC ECO:0000269|PubMed:27693509, ECO:0000269|PubMed:27802168,
CC ECO:0000269|PubMed:28089391, ECO:0000269|PubMed:28386021}.
CC -!- SUBUNIT: Interacts with PLEKHA7 (PubMed:19041755). Interacts with
CC CAMSAP2 (By similarity). Interacts with KATNA1 and KATNB1; leading to
CC regulate the length of CAMSAP3-decorated microtubule stretches
CC (PubMed:24486153, PubMed:28386021). Interacts with AKAP9; regulating
CC Golgi assembly in epithelial cells (PubMed:28089391). Interacts with
CC MACF1 (PubMed:27693509, PubMed:27802168). Interacts with AKNA (By
CC similarity). {ECO:0000250|UniProtKB:Q80VC9,
CC ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:24486153,
CC ECO:0000269|PubMed:27693509, ECO:0000269|PubMed:27802168,
CC ECO:0000269|PubMed:28089391, ECO:0000269|PubMed:28386021}.
CC -!- INTERACTION:
CC Q9P1Y5-2; O43143: DHX15; NbExp=3; IntAct=EBI-18121830, EBI-1237044;
CC Q9P1Y5-2; A1L4K1: FSD2; NbExp=3; IntAct=EBI-18121830, EBI-5661036;
CC Q9P1Y5-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-18121830, EBI-7116203;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19041755, ECO:0000269|PubMed:23169647,
CC ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:27693509,
CC ECO:0000269|PubMed:28386021}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:19041755}. Cytoplasm {ECO:0000269|PubMed:19041755}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q80VC9}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q80VC9}. Note=Scattered in the cytoplasm,
CC associated with the minus-end of microtubules and also detected at the
CC centrosomes (PubMed:19041755, PubMed:24486153, PubMed:27693509).
CC Decorates the minus-end of microtubules by decreasing the rate of
CC tubulin incorporation and remaining bound (PubMed:24486153). Localizes
CC along zonula adherens only at mature cell-cell contacts
CC (PubMed:19041755). In early embryos, accumulates at the microtubule
CC bridges that connect pairs of cells: this structure is present in early
CC embryos, which lack centrosomes (By similarity). This cytokinetic
CC bridge does not undergo stereotypical abscission after cell division
CC (By similarity). Accumulates to the pericentrosomal region following
CC interaction with KATNA1 (PubMed:28386021).
CC {ECO:0000250|UniProtKB:Q80VC9, ECO:0000269|PubMed:19041755,
CC ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:27693509,
CC ECO:0000269|PubMed:28386021}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P1Y5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P1Y5-2; Sequence=VSP_041473;
CC -!- DOMAIN: The CKK domain binds microtubules and specifically recognizes
CC the minus-end of microtubules. {ECO:0000255|PROSITE-ProRule:PRU00841,
CC ECO:0000269|PubMed:24486153}.
CC -!- MISCELLANEOUS: 'Nezha' is a deity in Chinese mythology.
CC {ECO:0000305|PubMed:23169647}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC008763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW69025.1; -; Genomic_DNA.
DR EMBL; BC020431; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC035808; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB040976; BAA96067.1; -; mRNA.
DR EMBL; AL833927; CAD38783.1; -; mRNA.
DR CCDS; CCDS42489.1; -. [Q9P1Y5-1]
DR CCDS; CCDS45947.1; -. [Q9P1Y5-2]
DR RefSeq; NP_001073898.1; NM_001080429.2. [Q9P1Y5-2]
DR RefSeq; NP_065953.1; NM_020902.1. [Q9P1Y5-1]
DR AlphaFoldDB; Q9P1Y5; -.
DR SMR; Q9P1Y5; -.
DR BioGRID; 121695; 99.
DR DIP; DIP-52405N; -.
DR ELM; Q9P1Y5; -.
DR IntAct; Q9P1Y5; 50.
DR MINT; Q9P1Y5; -.
DR STRING; 9606.ENSP00000416797; -.
DR CarbonylDB; Q9P1Y5; -.
DR GlyGen; Q9P1Y5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P1Y5; -.
DR PhosphoSitePlus; Q9P1Y5; -.
DR BioMuta; CAMSAP3; -.
DR DMDM; 61213747; -.
DR EPD; Q9P1Y5; -.
DR jPOST; Q9P1Y5; -.
DR MassIVE; Q9P1Y5; -.
DR MaxQB; Q9P1Y5; -.
DR PaxDb; Q9P1Y5; -.
DR PeptideAtlas; Q9P1Y5; -.
DR PRIDE; Q9P1Y5; -.
DR ProteomicsDB; 83677; -. [Q9P1Y5-1]
DR ProteomicsDB; 83678; -. [Q9P1Y5-2]
DR ABCD; Q9P1Y5; 8 sequenced antibodies.
DR Antibodypedia; 50549; 80 antibodies from 19 providers.
DR DNASU; 57662; -.
DR Ensembl; ENST00000160298.9; ENSP00000160298.3; ENSG00000076826.10. [Q9P1Y5-1]
DR Ensembl; ENST00000446248.4; ENSP00000416797.1; ENSG00000076826.10. [Q9P1Y5-2]
DR GeneID; 57662; -.
DR KEGG; hsa:57662; -.
DR MANE-Select; ENST00000160298.9; ENSP00000160298.3; NM_020902.2; NP_065953.1.
DR UCSC; uc002mgu.5; human. [Q9P1Y5-1]
DR CTD; 57662; -.
DR DisGeNET; 57662; -.
DR GeneCards; CAMSAP3; -.
DR HGNC; HGNC:29307; CAMSAP3.
DR HPA; ENSG00000076826; Tissue enhanced (skin).
DR MIM; 612685; gene.
DR neXtProt; NX_Q9P1Y5; -.
DR OpenTargets; ENSG00000076826; -.
DR PharmGKB; PA134885087; -.
DR VEuPathDB; HostDB:ENSG00000076826; -.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_004833_1_0_1; -.
DR InParanoid; Q9P1Y5; -.
DR OMA; PERPVCE; -.
DR OrthoDB; 741937at2759; -.
DR PhylomeDB; Q9P1Y5; -.
DR TreeFam; TF315529; -.
DR PathwayCommons; Q9P1Y5; -.
DR SignaLink; Q9P1Y5; -.
DR BioGRID-ORCS; 57662; 18 hits in 1070 CRISPR screens.
DR ChiTaRS; CAMSAP3; human.
DR GenomeRNAi; 57662; -.
DR Pharos; Q9P1Y5; Tbio.
DR PRO; PR:Q9P1Y5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9P1Y5; protein.
DR Bgee; ENSG00000076826; Expressed in lower esophagus mucosa and 94 other tissues.
DR Genevisible; Q9P1Y5; HS.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036449; C:microtubule minus-end; IEA:Ensembl.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005915; C:zonula adherens; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IDA:UniProtKB.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0034453; P:microtubule anchoring; IMP: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; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; IDA:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0033043; P:regulation of organelle organization; IMP:UniProtKB.
DR GO; GO:0045218; P:zonula adherens maintenance; IMP: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 Alternative splicing; Cell junction; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1249
FT /note="Calmodulin-regulated spectrin-associated protein 3"
FT /id="PRO_0000050799"
FT DOMAIN 203..312
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1109..1243
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 328..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 594..628
FT /evidence="ECO:0000255"
FT COILED 696..729
FT /evidence="ECO:0000255"
FT COILED 896..935
FT /evidence="ECO:0000255"
FT COMPBIAS 338..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..746
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 799
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1074
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 207
FT /note="S -> SCPTRWYWKLVPHAIAFCLKESGSKPPM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041473"
FT VARIANT 335
FT /note="P -> S (in dbSNP:rs3745358)"
FT /id="VAR_053991"
FT CONFLICT 824
FT /note="S -> P (in Ref. 3; BC035808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1249 AA; 134750 MW; 5A597E13531443CE CRC64;
MVEAAPPGPG PLRRTFLVPE IKSLDQYDFS RAKAAASLAW VLRAAFGGAE HVPPELWEPF
YTDQYAQEHV KPPVTRLLLS AELYCRAWRQ ALPQLETPPN PSALLALLAR RGTVPALPER
PVREADLRHQ PILMGAHLAV IDALMAAFAF EWTKTLPGPL ALTSLEHKLL FWVDTTVRRL
QEKTEQEAAQ RASPAAPADG AAPAQPSIRY RKDRVVARRA PCFPTVTSLQ DLASGAALAA
TIHCYCPQLL RLEEVCLKDP MSVADSLYNL QLVQDFCASR LPRGCPLSLE DLLYVPPPLK
VNLVVMLAEL FMCFEVLKPD FVQVKDLPDG HAASPRGTEA SPPQNNSGSS SPVFTFRHPL
LSSGGPQSPL RGSTGSLKSS PSMSHMEALG KAWNRQLSRP LSQAVSFSTP FGLDSDVDVV
MGDPVLLRSV SSDSLGPPRP APARTPTQPP PEPGDLPTIE EALQIIHSAE PRLLPDGAAD
GSFYLHSPEG PSKPSLASPY LPEGTSKPLS DRPTKAPVYM PHPETPSKPS PCLVGEASKP
PAPSEGSPKA VASSPAATNS EVKMTSFAER KKQLVKAEAE AGAGSPTSTP APPEALSSEM
SELSARLEEK RRAIEAQKRR IEAIFAKHRQ RLGKSAFLQV QPREASGEAE AEAEEADSGP
VPGGERPAGE GQGEPTSRPK AVTFSPDLGP VPHEGLGEYN RAVSKLSAAL SSLQRDMQRL
TDQQQRLLAP PEAPGSAPPP AAWVIPGPTT GPKAASPSPA RRVPATRRSP GPGPSQSPRS
PKHTRPAELR LAPLTRVLTP PHDVDSLPHL RKFSPSQVPV QTRSSILLAE ETPPEEPAAR
PGLIEIPLGS LADPAAEDEG DGSPAGAEDS LEEEASSEGE PRVGLGFFYK DEDKPEDEMA
QKRASLLERQ QRRAEEARRR KQWQEVEKEQ RREEAARLAQ EEAPGPAPLV SAVPMATPAP
AARAPAEEEV GPRKGDFTRQ EYERRAQLKL MDDLDKVLRP RAAGSGGPGR GGRRATRPRS
GCCDDSALAR SPARGLLGSR LSKIYSQSTL SLSTVANEAH NNLGVKRPTS RAPSPSGLMS
PSRLPGSRER DWENGSNASS PASVPEYTGP RLYKEPSAKS NKFIIHNALS HCCLAGKVNE
PQKNRILEEI EKSKANHFLI LFRDSSCQFR ALYTLSGETE ELSRLAGYGP RTVTPAMVEG
IYKYNSDRKR FTQIPAKTMS MSVDAFTIQG HLWQGKKPTT PKKGGGTPK
