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Database: UniProt
Entry: A0A2Y9SGM3_PHYMC
LinkDB: A0A2Y9SGM3_PHYMC
Original site: A0A2Y9SGM3_PHYMC 
ID   A0A2Y9SGM3_PHYMC        Unreviewed;       326 AA.
AC   A0A2Y9SGM3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Microtubule-associated protein RP/EB family member 2 {ECO:0000256|ARBA:ARBA00019565};
GN   Name=MAPRE2 {ECO:0000313|RefSeq:XP_023976477.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023976477.1};
RN   [1] {ECO:0000313|RefSeq:XP_023976477.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023976477.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May be involved in microtubule polymerization, and spindle
CC       function by stabilizing microtubules and anchoring them at centrosomes.
CC       May play a role in cell migration. {ECO:0000256|ARBA:ARBA00025650}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the MAPRE family.
CC       {ECO:0000256|ARBA:ARBA00010729}.
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DR   RefSeq; XP_023976477.1; XM_024120709.3.
DR   AlphaFoldDB; A0A2Y9SGM3; -.
DR   STRING; 9755.ENSPCTP00005008449; -.
DR   Ensembl; ENSPCTT00005009301; ENSPCTP00005008449; ENSPCTG00005005888.
DR   KEGG; pcad:102982847; -.
DR   InParanoid; A0A2Y9SGM3; -.
DR   OrthoDB; 11676at2759; -.
DR   Proteomes; UP000248484; Chromosome 19.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0051010; F:microtubule plus-end binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0032014; P:positive regulation of ARF protein signal transduction; IEA:Ensembl.
DR   GO; GO:0120183; P:positive regulation of focal adhesion disassembly; IEA:Ensembl.
DR   GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
DR   Gene3D; 1.20.5.1430; -; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR004953; EB1_C.
DR   InterPro; IPR036133; EB1_C_sf.
DR   InterPro; IPR027328; MAPRE.
DR   PANTHER; PTHR10623; MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER; 1.
DR   PANTHER; PTHR10623:SF7; MICROTUBULE-ASSOCIATED PROTEIN RP_EB FAMILY MEMBER 2; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF03271; EB1; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF140612; EB1 dimerisation domain-like; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51230; EB1_C; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Microtubule {ECO:0000256|PROSITE-ProRule:PRU00576};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT   DOMAIN          56..158
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          235..305
FT                   /note="EB1 C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51230"
FT   REGION          170..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  37018 MW;  8177D440732D38F0 CRC64;
     MPGPTQTLSP NGENNNDIIQ DNGTIIPFRK HTVRGERSYS WGMAVNVYST SITQETMSRH
     DIIAWVNDIV SLNYTKVEQL CSGAAYCQFM DMLFPGCISL KKVKFQAKLE HEYIHNFKLL
     QASFKRMNVD KVIPVEKLVK GRFQDNLDFI QWFKKFYDAN YDGKEYDPVE ARQGQDAIPP
     PDPGEQIFNL PKKSHHANSP TAGAAKSSPA SKPGSTPSRP SSAKRASSSS SASKSDKDLE
     TQVIQLNEQV HSLKLALEGV EKERDFYFGK LREIELLCQE HGQENDDLVQ RLMEVLYASE
     EHEGHPEEPE AEEQVHEQQP QQQEEY
//
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