ID   MARE2_CHICK             Reviewed;         338 AA.
AC   Q5ZKK1;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Microtubule-associated protein RP/EB family member 2;
GN   Name=MAPRE2; ORFNames=RCJMB04_10e21;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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}.
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; AJ720083; CAG31742.1; -; mRNA.
DR   RefSeq; NP_001026188.1; NM_001031017.1.
DR   AlphaFoldDB; Q5ZKK1; -.
DR   SMR; Q5ZKK1; -.
DR   STRING; 9031.ENSGALP00000035995; -.
DR   PaxDb; Q5ZKK1; -.
DR   GeneID; 421105; -.
DR   KEGG; gga:421105; -.
DR   CTD; 10982; -.
DR   VEuPathDB; HostDB:geneid_421105; -.
DR   eggNOG; KOG3000; Eukaryota.
DR   HOGENOM; CLU_041744_1_0_1; -.
DR   InParanoid; Q5ZKK1; -.
DR   OrthoDB; 1237523at2759; -.
DR   PhylomeDB; Q5ZKK1; -.
DR   PRO; PR:Q5ZKK1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
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:0051233; C:spindle midzone; IBA:GO_Central.
DR   GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; 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..338
FT                   /note="Microtubule-associated protein RP/EB family member
FT                   2"
FT                   /id="PRO_0000213427"
FT   DOMAIN          57..159
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          236..306
FT                   /note="EB1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   338 AA;  38140 MW;  54914EC92CA0F3FB CRC64;
     MPGPTQALSP NGENNNDIIQ DNGTTIIPFR KHTVRGERSY SWGMAVNVYS TSITQETMSR
     HDIIAWVNDI LALNYTKVEQ LCSGAAYCQF MDMLFPGCIS LKKVKFQAKL EHEYIHNFKL
     LQASFKRMNV DKVIPVEKLV KGRFQDNLDF IQWFKKFFDA NYDGKEYDPV EARQGQDALP
     PPDPGEQIFN LPKKSHHANS PTAGAAKSSP ASKPGSTPSR PSSAKKAAPS SSASKSDKDL
     ETQVIQLSEQ VHSLKLALEG VEKERDFYFG KLREIELLCQ EHGGENNDLV HRLMEVLYAS
     EEHESHTEEH EGEEQVHEQP SSRRSTDSRS VSDNFHFV