MARE2_RAT
ID MARE2_RAT Reviewed; 326 AA.
AC Q3B8Q0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Microtubule-associated protein RP/EB family member 2;
GN Name=Mapre2;
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=Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP 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: May be involved in microtubule polymerization, and spindle
CC function by stabilizing microtubules and anchoring them at centrosomes.
CC May play a role in cell migration (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DCTN1. Interacts with APC (via C-terminal).
CC Interacts with monomeric and polymerized tubulin. Interacts with
CC SLAIN1. {ECO:0000250|UniProtKB:Q15555, ECO:0000250|UniProtKB:Q8R001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Associated with the microtubule network.
CC Accumulates at the plus end of microtubules (By similarity).
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR EMBL; BC105879; AAI05880.1; -; mRNA.
DR RefSeq; NP_001094470.1; NM_001101000.1.
DR AlphaFoldDB; Q3B8Q0; -.
DR SMR; Q3B8Q0; -.
DR BioGRID; 594167; 3.
DR IntAct; Q3B8Q0; 1.
DR STRING; 10116.ENSRNOP00000065460; -.
DR iPTMnet; Q3B8Q0; -.
DR PhosphoSitePlus; Q3B8Q0; -.
DR jPOST; Q3B8Q0; -.
DR PaxDb; Q3B8Q0; -.
DR PRIDE; Q3B8Q0; -.
DR GeneID; 679221; -.
DR KEGG; rno:679221; -.
DR CTD; 10982; -.
DR RGD; 1590736; Mapre2.
DR eggNOG; KOG3000; Eukaryota.
DR InParanoid; Q3B8Q0; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q3B8Q0; -.
DR PRO; PR:Q3B8Q0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
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:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032014; P:positive regulation of ARF protein signal transduction; ISO:RGD.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:RGD.
DR GO; GO:1904825; P:protein localization to microtubule plus-end; IBA:GO_Central.
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; IPR027328; MAPRE.
DR InterPro; IPR027735; RP1/EB2_vertebrate.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR PANTHER; PTHR10623:SF7; PTHR10623:SF7; 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..326
FT /note="Microtubule-associated protein RP/EB family member
FT 2"
FT /id="PRO_0000240312"
FT DOMAIN 56..158
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 235..305
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 170..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..326
FT /note="DCTN1-binding"
FT /evidence="ECO:0000250"
FT REGION 258..301
FT /note="APC-binding"
FT /evidence="ECO:0000250"
FT REGION 297..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 166
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15555"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15555"
SQ SEQUENCE 326 AA; 36988 MW; 86829172C9E75643 CRC64;
MPGPTQTLSP NGENNNDIIQ DNGTIIPFRK HTVRGERSYS WGMAVNVYST SITQETMSRH
DIIAWVNDIV SLNYTKVEQL CSGAAYCQFM DMLFPGCISL KKVKFQAKLE HEYIHNFKLL
QASFKRMNVD KVIPVEKLVK GRFQDNLDFI QWFKKFYDAN YDGKEYDPVE ARQGQDAIPP
PDPGEQIFNL PKKSHHANSP TAGAAKSSPA AKPGSTPSRP SSAKRASSSG SASRSDKDLE
TQVIQLNEQV HSLKLALEGV EKERDFYFGK LREIELLCQE HGQENDDLVQ RLMEVLYASD
EQEGQTEEPE VEEQTHDQQP QQQEEY
