MARE1_XENTR
ID MARE1_XENTR Reviewed; 269 AA.
AC Q6P848;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Microtubule-associated protein RP/EB family member 1;
GN Name=mapre1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) 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}.
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; BC061382; AAH61382.1; -; mRNA.
DR RefSeq; NP_989115.1; NM_203784.1.
DR RefSeq; XP_012827058.1; XM_012971604.2.
DR RefSeq; XP_017945588.1; XM_018090099.1.
DR AlphaFoldDB; Q6P848; -.
DR SMR; Q6P848; -.
DR STRING; 8364.ENSXETP00000055099; -.
DR PaxDb; Q6P848; -.
DR DNASU; 394720; -.
DR Ensembl; ENSXETT00000055099; ENSXETP00000055099; ENSXETG00000006620.
DR GeneID; 394720; -.
DR KEGG; xtr:394720; -.
DR CTD; 22919; -.
DR Xenbase; XB-GENE-974542; mapre1.
DR eggNOG; KOG3000; Eukaryota.
DR HOGENOM; CLU_041744_1_1_1; -.
DR InParanoid; Q6P848; -.
DR OMA; ICQEKES; -.
DR OrthoDB; 1237523at2759; -.
DR TreeFam; TF313620; -.
DR Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-XTR-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-XTR-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-XTR-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-XTR-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-XTR-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-XTR-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR Reactome; R-XTR-8854518; AURKA Activation by TPX2.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000006620; Expressed in neurula embryo and 18 other tissues.
DR ExpressionAtlas; Q6P848; baseline.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
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 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; 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..269
FT /note="Microtubule-associated protein RP/EB family member
FT 1"
FT /id="PRO_0000213420"
FT DOMAIN 14..116
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 186..256
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 168..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 30206 MW; E2EF0CDA3D58BDE8 CRC64;
MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GSVYCQFMDM LFPGSVVLKK
VKFQAKLEHE YIQNFKVLQA GFKKMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD
GKDYDPVAAR QGQESAPVPV LAAPVLNKPK KPLGSGNTAP QRTVPVQRTA VSNKPPAQGI
SKKPATVGNG DDESAELIQQ INVLKITVED LEKERDFYFG KLRNIELICQ ENEGESDPVL
QRIIEILYAT DEGFVIPDEG APPEDQEEY