ID   MARE1_COTCO             Reviewed;         263 AA.
AC   Q6V291;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Microtubule-associated protein RP/EB family member 1;
GN   Name=MAPRE1;
OS   Coturnix coturnix (Common quail) (Tetrao coturnix).
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=9091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15384902; DOI=10.1093/ps/83.9.1524;
RA   Mott I.W., Ivarie R.D.;
RT   "cDNA array analysis of Japanese quail lines divergently selected for four-
RT   week body weight.";
RL   Poult. Sci. 83:1524-1529(2004).
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; AY353854; AAQ55812.1; -; mRNA.
DR   AlphaFoldDB; Q6V291; -.
DR   SMR; Q6V291; -.
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.
FT   CHAIN           1..263
FT                   /note="Microtubule-associated protein RP/EB family member
FT                   1"
FT                   /id="PRO_0000213422"
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"
SQ   SEQUENCE   263 AA;  29519 MW;  1A55A404B174CCE8 CRC64;
     MAVNVYSTSV TSDNLSRHDM LAWINESLQL TLTKIEQLCS GAAYCQFMDM LFPGSVALKK
     VKFQAKLEHE YIQNFKVLQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD
     GKEYDPVAAR QGQETVAPNL VAPVMNKPKK PLGTGSAAPQ RPIVAQRTPA TPKGGTGMVK
     KAAGDDESAG LIEQINVLKL TVEDLEKERD FYFGKLRNIE LICQENEGEN DPVLQRIVEI
     LYATDEGFVI PDEGAPQEEQ EEY