ID   MARE2_XENLA             Reviewed;         327 AA.
AC   Q7ZXP1;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Microtubule-associated protein RP/EB family member 2;
GN   Name=mapre2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) 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       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Note=Associated with the microtubule network.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal domain may form a hydrophobic cleft involved in
CC       microtubule binding and the C-terminal may be involved in the formation
CC       of mutually exclusive complexes with APC and DCTN1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR   EMBL; BC044671; AAH44671.1; -; mRNA.
DR   RefSeq; NP_001079198.1; NM_001085729.1.
DR   AlphaFoldDB; Q7ZXP1; -.
DR   SMR; Q7ZXP1; -.
DR   BioGRID; 97026; 1.
DR   MaxQB; Q7ZXP1; -.
DR   DNASU; 373805; -.
DR   GeneID; 373805; -.
DR   KEGG; xla:373805; -.
DR   CTD; 373805; -.
DR   Xenbase; XB-GENE-6252421; mapre2.S.
DR   OrthoDB; 1237523at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 373805; Expressed in brain and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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   Reference proteome.
FT   CHAIN           1..327
FT                   /note="Microtubule-associated protein RP/EB family member
FT                   2"
FT                   /id="PRO_0000213426"
FT   DOMAIN          56..158
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          234..304
FT                   /note="EB1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   327 AA;  37264 MW;  F2EB229EEA0DF385 CRC64;
     MPGPTQTLSP NGENNNDVIH DNGTIIPFRK HTVRGERSYS WGMAVNVYST SITQETMSRH
     DIIAWVNDIV CLNYIKVEQL SSGAAYCQFM DMLFPGCISL KKVKFQAKLE HEYIHNFKLL
     QASFKRMNVD KVIPVEKLVK GRFQDNLDFI QWFKKFFDAN YDGKEYDPME ARQGQDALPP
     PDPGEQIFNL PKKPHHANSP TAGAARSSPI AKPGSTSSRP SSAKKAVPCP SVKSDKDLET
     QVSHLNEQVH SLKIALEGVE KERDFYFGKL REIELLCQEH GQEGDDLLQR LMDILYSSEE
     QESHTEQHEG EEEQEHGHEE AEQQEEY