MARE1_PONAB
ID MARE1_PONAB Reviewed; 268 AA.
AC Q5R7Z5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Microtubule-associated protein RP/EB family member 1;
DE AltName: Full=APC-binding protein EB1;
DE AltName: Full=End-binding protein 1;
DE Short=EB1;
GN Name=MAPRE1;
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=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-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. Also
CC acts as a regulator of minus-end microtubule organization: interacts
CC with the complex formed by AKAP9 and PDE4DIP, leading to recruit
CC CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal
CC minus-end microtubules to the Golgi, an important step for polarized
CC cell movement. Promotes elongation of CAMSAP2-decorated microtubule
CC stretches on the minus-end of microtubules. Acts as a regulator of
CC autophagosome transport via interaction with CAMSAP2 (By similarity).
CC May play a role in cell migration (By similarity).
CC {ECO:0000250|UniProtKB:Q15691, ECO:0000250|UniProtKB:Q61166}.
CC -!- SUBUNIT: Homodimer. Heterodimer with MAPRE3. Interacts with DCTN1,
CC DCTN2, TERF1 and dynein intermediate chain (By similarity). Interaction
CC with DIAPH1 and DIAPH2 (By similarity). Interacts with APC (via C-
CC terminal domain), CLASP2, DST, KIF2C and STIM1; probably required for
CC their targeting to the growing microtubule plus ends. Interacts with
CC MTUS2; interaction is direct and probably targets MTUS2 to
CC microtubules. Interacts with APC2. Interacts with CLASP1. Interacts
CC with CDK5RAP2 (By similarity). Interacts with MACF1. Interacts with
CC RABL2/RABL2A; binds preferentially to GTP-bound RABL2. Interacts with
CC KCNAB2 (By similarity). Interacts (via C-terminus) with CLIP1.
CC Interacts with SLAIN2 and SLAIN1. Interacts with KIF18B; this
CC interaction is required for efficient accumulation of KIF18B at
CC microtubule plus ends. Interacts with MISP. Interacts with KNSTRN.
CC Interacts with NCKAP5L. Interacts with CAMSAP2. Interacts with PDE4DIP
CC isoform 13/MMG8/SMYLE; this interaction is required for its recruitment
CC to the Golgi apparatus. Forms a pericentrosomal complex with AKAP9,
CC CDK5RAP2 and PDE4DIP isoform 13/MMG8/SMYLE; within this complex, MAPRE1
CC binding to CDK5RAP2 may be mediated by PDE4DIP (By similarity).
CC Interacts with AKNA (By similarity). Interacts with GAS2L1, GAS2L2, and
CC GAS2L3 (By similarity). Interacts with RARRES1 and AGBL2 (By
CC similarity). {ECO:0000250|UniProtKB:Q15691,
CC ECO:0000250|UniProtKB:Q61166}.
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}. Note=Associated with the
CC microtubule growing distal tips. Recruitment to the Golgi apparatus
CC requires the presence of PDE4DIP isoform 13/MMG8/SMYLE.
CC {ECO:0000250|UniProtKB:Q15691}.
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. {ECO:0000250|UniProtKB:Q15691}.
CC -!- PTM: Acetylation at Lys-220 by KAT2B/PCAF promotes dynamic kinetochore-
CC microtubule interactions in early mitosis.
CC {ECO:0000250|UniProtKB:Q15691}.
CC -!- PTM: Crotonylated by KAT5 during mitosis, promoting astral microtubule
CC plasticity and dynamic connection between astral microtubules and the
CC cortex during mitotic chromosome segregation, thereby ensuring accurate
CC spindle positioning in mitosis. Decrotonylated by HDAC3.
CC {ECO:0000250|UniProtKB:Q15691}.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR EMBL; CR859962; CAH92115.1; -; mRNA.
DR RefSeq; NP_001126236.1; NM_001132764.1.
DR RefSeq; XP_009231764.1; XM_009233489.1.
DR AlphaFoldDB; Q5R7Z5; -.
DR BMRB; Q5R7Z5; -.
DR SMR; Q5R7Z5; -.
DR STRING; 9601.ENSPPYP00000012189; -.
DR GeneID; 100173206; -.
DR KEGG; pon:100173206; -.
DR CTD; 22919; -.
DR eggNOG; KOG3000; Eukaryota.
DR HOGENOM; CLU_041744_1_1_1; -.
DR InParanoid; Q5R7Z5; -.
DR OrthoDB; 1237523at2759; -.
DR Proteomes; UP000001595; 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 Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT CHAIN 2..268
FT /note="Microtubule-associated protein RP/EB family member
FT 1"
FT /id="PRO_0000213418"
FT DOMAIN 14..116
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 185..255
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 124..268
FT /note="Interaction with MTUS2/TIP150"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT REGION 146..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..268
FT /note="Interaction with CDK5RAP2"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT REGION 208..268
FT /note="DCTN1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT REGION 220..242
FT /note="APC-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT COMPBIAS 150..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MOD_RES 66
FT /note="N6-crotonyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MOD_RES 124
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
SQ SEQUENCE 268 AA; 29985 MW; 0FC89BCA15A145ED CRC64;
MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK
VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD
GKDYDPVAAR QGQETAVAPS LVAPALNKPK KPLSSSSAAP QRPISTQRTA AAPKAGPGVV
RKNPGVGNGD DEAAELMQQV NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ
RIVDILYATD EGFVIPDEGG PQEEQEEY
