MARE2_PONAB
ID MARE2_PONAB Reviewed; 327 AA.
AC Q5R4I6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Microtubule-associated protein RP/EB family member 2;
GN Name=MAPRE2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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}.
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DR EMBL; CR861262; CAH93330.1; -; mRNA.
DR RefSeq; NP_001126960.1; NM_001133488.1.
DR AlphaFoldDB; Q5R4I6; -.
DR SMR; Q5R4I6; -.
DR STRING; 9601.ENSPPYP00000010220; -.
DR Ensembl; ENSPPYT00000010624; ENSPPYP00000010220; ENSPPYG00000009101.
DR GeneID; 100173979; -.
DR KEGG; pon:100173979; -.
DR CTD; 10982; -.
DR eggNOG; KOG3000; Eukaryota.
DR GeneTree; ENSGT00490000043329; -.
DR HOGENOM; CLU_041744_1_0_1; -.
DR InParanoid; Q5R4I6; -.
DR OMA; EQCGTGG; -.
DR OrthoDB; 1237523at2759; -.
DR TreeFam; TF313620; -.
DR Proteomes; UP000001595; Chromosome 18.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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 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..327
FT /note="Microtubule-associated protein RP/EB family member
FT 2"
FT /id="PRO_0000240311"
FT DOMAIN 57..159
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 236..306
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..327
FT /note="DCTN1-binding"
FT /evidence="ECO:0000250"
FT REGION 259..302
FT /note="APC-binding"
FT /evidence="ECO:0000250"
FT REGION 299..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..240
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 167
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15555"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15555"
SQ SEQUENCE 327 AA; 37045 MW; 67F45AAF86739B4C CRC64;
MPGPTQTLSP NGENNNDIIQ DNNGTIIPFR KHTVRGERSY SWGMAVNVYS TSITQETMSR
HDIIAWVNDI VSLNYTKVEQ LCSGAAYCQF MDMLFPGCIS LKKVKFQAKL EHEYIHNFKL
LQASFKRMNV DKVIPVEKLV KGRFQDNLDF IQWFKKFYDA NYDGKEYDPV EARQGQDAIP
PPDPGEQIFN LPKKSHHANS PTAGAAKSSP AAKPGSTPSR PSSAKRASSS GSASRSDKDL
ETQVIQLNEQ VHSLKLALEG VEKERDFYFG KLREIELLCQ EHGQENDDLV QRLMDVLYAS
EEHEGHTEEP EAEEQAHEQQ PPQQEEY
