MARE2_BOVIN
ID MARE2_BOVIN Reviewed; 326 AA.
AC Q3SZP2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Microtubule-associated protein RP/EB family member 2;
GN Name=MAPRE2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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}.
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; BC102764; AAI02765.1; -; mRNA.
DR RefSeq; NP_001029546.1; NM_001034374.2.
DR AlphaFoldDB; Q3SZP2; -.
DR SMR; Q3SZP2; -.
DR STRING; 9913.ENSBTAP00000009897; -.
DR iPTMnet; Q3SZP2; -.
DR PaxDb; Q3SZP2; -.
DR PRIDE; Q3SZP2; -.
DR Ensembl; ENSBTAT00000009897; ENSBTAP00000009897; ENSBTAG00000007520.
DR GeneID; 510159; -.
DR KEGG; bta:510159; -.
DR CTD; 10982; -.
DR VEuPathDB; HostDB:ENSBTAG00000007520; -.
DR VGNC; VGNC:31233; MAPRE2.
DR eggNOG; KOG3000; Eukaryota.
DR GeneTree; ENSGT00490000043329; -.
DR HOGENOM; CLU_041744_1_0_1; -.
DR InParanoid; Q3SZP2; -.
DR OMA; EQCGTGG; -.
DR OrthoDB; 1237523at2759; -.
DR TreeFam; TF313620; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000007520; Expressed in prefrontal cortex and 103 other tissues.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032014; P:positive regulation of ARF protein signal transduction; IEA:Ensembl.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
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 2: Evidence at transcript 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_0000240310"
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 298..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 MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15555"
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; 48FB47CDBB7821A1 CRC64;
MPGPTQTLSP NGENNNDIIQ DNGTIIPFRK HTVRGERSYS WGMAVNVYST SITQETMSRH
DIIAWVNDIV SLNYTKVEQL CSGAAYCQFM DMLFPGCISL KKVKFQAKLE HEYIHNFKLL
QASFKRMNVD KVIPVEKLVK GRFQDNLDFI QWFKKFYDAN YDGKEYDPVE ARQGQDAIPP
PDPGEQIFNL PKKSHHANSP TAGAAKSSPA SKPGSTPSRP SSAKRASSSG SASRSDKDLE
TQVIQLNEQV HSLKLALEGV EKERDFYFGK LREIELLCQE HGQENDDLVQ RLMDVLYASD
EHEGHPEEPE AEEQVHEQQP QQQEEY
