ID   MARE1_COTJA             Reviewed;         263 AA.
AC   Q66T82;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Microtubule-associated protein RP/EB family member 1;
GN   Name=MAPRE1;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Matt T., Bister K.;
RT   "Functional characterization of the EB1 C-terminal domain.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 cytoplasmic microtubule nucleation and
CC       elongation. Involved in mitotic spindle positioning by stabilizing
CC       microtubules and promoting dynamic connection between astral
CC       microtubules and the cortex during mitotic chromosome segregation.
CC       {ECO:0000250|UniProtKB:Q15691}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q15691}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton,
CC       spindle {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton,
CC       spindle pole {ECO:0000250|UniProtKB:Q15691}.
CC   -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR   EMBL; AY704913; AAU12573.1; -; mRNA.
DR   RefSeq; NP_001310145.1; NM_001323216.1.
DR   AlphaFoldDB; Q66T82; -.
DR   SMR; Q66T82; -.
DR   GeneID; 107323220; -.
DR   KEGG; cjo:107323220; -.
DR   CTD; 22919; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0030981; C:cortical microtubule cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR   GO; GO:1902888; P:protein localization to astral microtubule; ISS:UniProtKB.
DR   GO; GO:0035372; P:protein localization to microtubule; ISS:UniProtKB.
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; IPR027739; EB1_Meta.
DR   InterPro; IPR027328; MAPRE.
DR   PANTHER; PTHR10623; PTHR10623; 1.
DR   PANTHER; PTHR10623:SF20; PTHR10623:SF20; 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; Golgi apparatus;
KW   Microtubule; Mitosis; Reference proteome.
FT   CHAIN           1..263
FT                   /note="Microtubule-associated protein RP/EB family member
FT                   1"
FT                   /id="PRO_0000213423"
FT   DOMAIN          14..116
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          180..250
FT                   /note="EB1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT   REGION          150..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   263 AA;  29505 MW;  5372447D56EAB508 CRC64;
     MAVNVYSTSV TSDNLSRHDM LAWINESLQL TLTKIEQLCS GAAYCQFMDM LFPGSVALKK
     VKFQAKLEHE YIQNFKVLQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD
     GKEYDPVAAR QGQETVAPNL VAPVMNKPKK PLGTGSAGPQ RPIVAQRTPA TPKGGTGMVK
     KAAGDDESAG LIEQINVLKL TVEDLEKERD FYFGKLRNIE LICQENEGEN DPVLQRIVEI
     LYATDEGFVI PDEGAPQEEQ EEY