MARE3_RAT
ID MARE3_RAT Reviewed; 281 AA.
AC Q5XIT1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Microtubule-associated protein RP/EB family member 3;
DE AltName: Full=EB1 protein family member 3;
DE Short=EBF3;
DE AltName: Full=End-binding protein 3;
DE Short=EB3;
DE AltName: Full=RP3;
GN Name=Mapre3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP INTERACTION WITH SRCIN1.
RX PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
RA Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
RA Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
RA Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
RT "Dynamic microtubules regulate dendritic spine morphology and synaptic
RT plasticity.";
RL Neuron 61:85-100(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plus-end tracking protein (+TIP) that binds to the plus-end
CC of microtubules and regulates the dynamics of the microtubule
CC cytoskeleton. Promotes microtubule growth. May be involved in spindle
CC function by stabilizing microtubules and anchoring them at centrosomes.
CC Also acts as a regulator of minus-end microtubule organization:
CC interacts with the complex formed by AKAP9 and PDE4DIP, leading to
CC recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-
CC centrosomal minus-end microtubules to the Golgi, an important step for
CC polarized cell movement. Promotes elongation of CAMSAP2-decorated
CC microtubule stretches on the minus-end of microtubules (By similarity).
CC May play a role in cell migration (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9UPY8}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer with MAPRE1 (By
CC similarity). Interacts with DCTN1 (By similarity). Binds to the C-
CC terminal domain of APC (By similarity). Binds monomeric and polymerized
CC tubulin (By similarity). Interacts (via C-terminus) with CLIP1 (By
CC similarity). Interacts with SLAIN2 and SLAIN1 (By similarity).
CC Interacts with APC2 (By similarity). Interacts with SRCIN1
CC (PubMed:19146815). Interacts with AKAP9 (By similarity). Interacts with
CC PDE4DIP; this interaction, which is PDE4DIP isoform-specific, is
CC required for its recruitment to the Golgi apparatus (By similarity).
CC {ECO:0000250|UniProtKB:Q9UPY8, ECO:0000269|PubMed:19146815}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9UPY8}. Note=Associated with the microtubule
CC network. Detected at the plus end of microtubules.
CC {ECO:0000250|UniProtKB:Q9UPY8}.
CC -!- DOMAIN: Composed of two functionally independent domains. The N-
CC terminal domain forms a hydrophobic cleft involved in microtubule
CC binding and the C-terminal is involved in the formation of mutually
CC exclusive complexes with APC and DCTN1. {ECO:0000250|UniProtKB:Q9UPY8}.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR EMBL; BC083589; AAH83589.1; -; mRNA.
DR RefSeq; NP_001007657.1; NM_001007656.1.
DR RefSeq; XP_008762734.1; XM_008764512.2.
DR AlphaFoldDB; Q5XIT1; -.
DR BMRB; Q5XIT1; -.
DR SMR; Q5XIT1; -.
DR BioGRID; 256035; 2.
DR STRING; 10116.ENSRNOP00000011877; -.
DR iPTMnet; Q5XIT1; -.
DR PhosphoSitePlus; Q5XIT1; -.
DR jPOST; Q5XIT1; -.
DR PaxDb; Q5XIT1; -.
DR PRIDE; Q5XIT1; -.
DR Ensembl; ENSRNOT00000011874; ENSRNOP00000011877; ENSRNOG00000008961.
DR GeneID; 298848; -.
DR KEGG; rno:298848; -.
DR CTD; 22924; -.
DR RGD; 1359297; Mapre3.
DR eggNOG; KOG3000; Eukaryota.
DR GeneTree; ENSGT00490000043329; -.
DR HOGENOM; CLU_041744_1_0_1; -.
DR InParanoid; Q5XIT1; -.
DR OMA; VQHAKEM; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q5XIT1; -.
DR TreeFam; TF313620; -.
DR PRO; PR:Q5XIT1; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000008961; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q5XIT1; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; ISO:RGD.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:1905721; C:mitotic spindle astral microtubule end; ISO:RGD.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0051010; F:microtubule plus-end binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:1903033; P:positive regulation of microtubule plus-end binding; ISO:RGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:1904825; P:protein localization to microtubule plus-end; IBA:GO_Central.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR036133; EB1_C_sf.
DR InterPro; IPR027738; EB3.
DR InterPro; IPR027328; MAPRE.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR PANTHER; PTHR10623:SF10; PTHR10623:SF10; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF03271; EB1; 1.
DR SUPFAM; SSF140612; SSF140612; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51230; EB1_C; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..281
FT /note="Microtubule-associated protein RP/EB family member
FT 3"
FT /id="PRO_0000213430"
FT DOMAIN 14..116
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 194..264
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 157..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..281
FT /note="DCTN1-binding"
FT /evidence="ECO:0000250"
FT REGION 217..260
FT /note="APC-binding"
FT /evidence="ECO:0000250"
FT REGION 260..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PER3"
SQ SEQUENCE 281 AA; 31966 MW; 6713427C480838DC CRC64;
MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM LFPGCVHLRK
VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK FQDNFEFIQW FKKFFDANYD
GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP
PCILRKNPPS ARNGGHEADA QILELNQQLL DLKLTVDGLE KERDFYFSKL RDIELICQEH
ESENSPVISG IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y
