MARE1_MOUSE
ID MARE1_MOUSE Reviewed; 268 AA.
AC Q61166; Q7TN34;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sparks A.B., Kay B.K.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-17; 77-84; 114-150 AND 205-214, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic fibroblast;
RA Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.;
RL Submitted (FEB-2008) to UniProtKB.
RN [4]
RP INTERACTION WITH APC; DCTN1; DIAPH1 AND DIAPH2, MUTAGENESIS OF
RP 211-GLU--GLU-213; 211-GLU--ASP-215 AND 220-LYS--ARG-222, AND FUNCTION.
RX PubMed=15311282; DOI=10.1038/ncb1160;
RA Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S., Chen M.,
RA Wallar B.J., Alberts A.S., Gundersen G.G.;
RT "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and
RT promote cell migration.";
RL Nat. Cell Biol. 6:820-830(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MACF1.
RX PubMed=18854161; DOI=10.1016/j.cell.2008.07.045;
RA Wu X., Kodama A., Fuchs E.;
RT "ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has
RT ATPase activity.";
RL Cell 135:137-148(2008).
RN [6]
RP LACK OF INTERACTION WITH MAPRE1.
RX PubMed=19553473; DOI=10.1091/mbc.e09-01-0009;
RA Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., Qi R.Z.;
RT "Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to
RT regulate microtubule dynamics.";
RL Mol. Biol. Cell 20:3660-3670(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH KCNAB2, AND SUBCELLULAR LOCATION.
RX PubMed=21357749; DOI=10.1083/jcb.201007113;
RA Vacher H., Yang J.W., Cerda O., Autillo-Touati A., Dargent B.,
RA Trimmer J.S.;
RT "Cdk-mediated phosphorylation of the Kvbeta2 auxiliary subunit regulates
RT Kv1 channel axonal targeting.";
RL J. Cell Biol. 192:813-824(2011).
RN [9]
RP INTERACTION WITH SLAIN2 AND SLAIN1.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M.,
RA Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O.,
RA Akhmanova A.;
RT "SLAIN2 links microtubule plus end-tracking proteins and controls
RT microtubule growth in interphase.";
RL J. Cell Biol. 193:1083-1099(2011).
RN [10]
RP INTERACTION WITH RABL2, AND TISSUE SPECIFICITY.
RX PubMed=23055941; DOI=10.1371/journal.pgen.1002969;
RA Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C.,
RA Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C.,
RA Ormandy C.J., O'Bryan M.K.;
RT "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar
RT transport, and tail assembly.";
RL PLoS Genet. 8:E1002969-E1002969(2012).
RN [11]
RP INTERACTION WITH GAS2L1; GAS2L2 AND GAS2L3, AND SUBCELLULAR LOCATION.
RX PubMed=24706950; DOI=10.1242/jcs.140558;
RA Stroud M.J., Nazgiewicz A., McKenzie E.A., Wang Y., Kammerer R.A.,
RA Ballestrem C.;
RT "GAS2-like proteins mediate communication between microtubules and actin
RT through interactions with end-binding proteins.";
RL J. Cell Sci. 127:2672-2682(2014).
RN [12]
RP INTERACTION WITH AKNA.
RX PubMed=30787442; DOI=10.1038/s41586-019-0962-4;
RA Camargo Ortega G., Falk S., Johansson P.A., Peyre E., Broix L., Sahu S.K.,
RA Hirst W., Schlichthaerle T., De Juan Romero C., Draganova K., Vinopal S.,
RA Chinnappa K., Gavranovic A., Karakaya T., Steininger T., Merl-Pham J.,
RA Feederle R., Shao W., Shi S.H., Hauck S.M., Jungmann R., Bradke F.,
RA Borrell V., Geerlof A., Reber S., Tiwari V.K., Huttner W.B.,
RA Wilsch-Braeuninger M., Nguyen L., Goetz M.;
RT "The centrosome protein AKNA regulates neurogenesis via microtubule
RT organization.";
RL Nature 567:113-117(2019).
RN [13]
RP STRUCTURE BY NMR OF 12-117.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CH domain from mouse EB-1.";
RL Submitted (MAY-2004) to the PDB data bank.
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 (PubMed:15311282).
CC {ECO:0000250|UniProtKB:Q15691, ECO:0000269|PubMed:15311282}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer with MAPRE3 (By
CC similarity). Interacts with APC (via C-terminal domain), DCTN1, DIAPH1,
CC DIAPH2 (PubMed:15311282). Interacts with DCTN2, TERF1 and dynein
CC intermediate chain (By similarity). Interacts with CLASP2, DST, KIF2C
CC and STIM1; probably required for their targeting to the growing
CC microtubule plus ends (By similarity). Interacts with MTUS2;
CC interaction is direct and probably targets MTUS2 to microtubules (By
CC similarity). Interacts with APC2 (By similarity). Interacts with CLASP1
CC (By similarity). Interacts (via C-terminus) with CLIP1 (By similarity).
CC Interacts with SLAIN2 and SLAIN1 (PubMed:21646404). Interacts with
CC MACF1 (PubMed:18854161). Interacts with KIF18B; this interaction is
CC required for efficient accumulation of KIF18B at microtubule plus ends
CC (By similarity). Interacts with MISP (By similarity). Interacts with
CC RABL2/RABL2A; binds preferentially to GTP-bound RABL2
CC (PubMed:23055941). Interacts with KCNAB2 (PubMed:21357749). Interacts
CC with KNSTRN (By similarity). Interacts with NCKAP5L (By similarity).
CC Interacts with AKAP9 (By similarity). Interacts with PDE4DIP isoform
CC 2/MMG8/SMYLE; this interaction is required for its recruitment to the
CC Golgi apparatus. May form a pericentrosomal complex with AKAP9,
CC CDK5RAP2 and PDE4DIP isoform 2/MMG8/SMYLE; within this complex, MAPRE1
CC binding to CDK5RAP2 may be mediated by PDE4DIP (By similarity).
CC Contrary to other mammalian species, does not interact with CDK5RAP2,
CC possibly due to the lack of conservation of the MAPRE1-binding motif in
CC mouse CDK5RAP2 (PubMed:19553473). Interacts with AKNA
CC (PubMed:30787442). Interacts with GAS2L1, GAS2L2, and GAS2L3
CC (PubMed:24706950). Interacts with RARRES1 and AGBL2 (By similarity).
CC {ECO:0000250|UniProtKB:Q15691, ECO:0000269|PubMed:15311282,
CC ECO:0000269|PubMed:18854161, ECO:0000269|PubMed:19553473,
CC ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:21646404,
CC ECO:0000269|PubMed:23055941, ECO:0000269|PubMed:24706950,
CC ECO:0000269|PubMed:30787442}.
CC -!- INTERACTION:
CC Q61166; P14873: Map1b; NbExp=5; IntAct=EBI-2027055, EBI-764653;
CC Q61166; Q03001: DST; Xeno; NbExp=4; IntAct=EBI-2027055, EBI-310758;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:24706950}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q15691}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q15691}. Note=Associated with the microtubule
CC network at the growing distal tip of microtubules (PubMed:21357749).
CC Also enriched at the centrosome (By similarity).
CC {ECO:0000250|UniProtKB:Q15691, ECO:0000269|PubMed:21357749}.
CC -!- TISSUE SPECIFICITY: Expressed within the midpiece of sperm tail (at
CC protein level). {ECO:0000269|PubMed:23055941}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52405.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; U51196; AAA96320.1; -; mRNA.
DR EMBL; BC052405; AAH52405.1; ALT_INIT; mRNA.
DR EMBL; BC064444; AAH64444.1; -; mRNA.
DR CCDS; CCDS16917.1; -.
DR RefSeq; NP_031922.1; NM_007896.3.
DR PDB; 1V5K; NMR; -; A=15-116.
DR PDB; 6EVI; NMR; -; A/B=191-260.
DR PDB; 6EVQ; NMR; -; A/B=191-260.
DR PDBsum; 1V5K; -.
DR PDBsum; 6EVI; -.
DR PDBsum; 6EVQ; -.
DR AlphaFoldDB; Q61166; -.
DR BMRB; Q61166; -.
DR SMR; Q61166; -.
DR BioGRID; 199356; 42.
DR CORUM; Q61166; -.
DR DIP; DIP-46795N; -.
DR IntAct; Q61166; 29.
DR MINT; Q61166; -.
DR STRING; 10090.ENSMUSP00000028981; -.
DR iPTMnet; Q61166; -.
DR PhosphoSitePlus; Q61166; -.
DR SwissPalm; Q61166; -.
DR REPRODUCTION-2DPAGE; Q61166; -.
DR EPD; Q61166; -.
DR jPOST; Q61166; -.
DR MaxQB; Q61166; -.
DR PaxDb; Q61166; -.
DR PRIDE; Q61166; -.
DR ProteomicsDB; 295783; -.
DR Antibodypedia; 1211; 289 antibodies from 32 providers.
DR DNASU; 13589; -.
DR Ensembl; ENSMUST00000028981; ENSMUSP00000028981; ENSMUSG00000027479.
DR GeneID; 13589; -.
DR KEGG; mmu:13589; -.
DR UCSC; uc008nik.1; mouse.
DR CTD; 22919; -.
DR MGI; MGI:891995; Mapre1.
DR VEuPathDB; HostDB:ENSMUSG00000027479; -.
DR eggNOG; KOG3000; Eukaryota.
DR GeneTree; ENSGT00490000043329; -.
DR HOGENOM; CLU_041744_1_1_1; -.
DR InParanoid; Q61166; -.
DR OMA; HEYIQNY; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q61166; -.
DR TreeFam; TF313620; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 13589; 8 hits in 70 CRISPR screens.
DR ChiTaRS; Mapre1; mouse.
DR EvolutionaryTrace; Q61166; -.
DR PRO; PR:Q61166; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61166; protein.
DR Bgee; ENSMUSG00000027479; Expressed in medial ganglionic eminence and 252 other tissues.
DR ExpressionAtlas; Q61166; baseline and differential.
DR Genevisible; Q61166; MM.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:1905721; C:mitotic spindle astral microtubule end; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
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:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; IDA:UniProtKB.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:1903033; P:positive regulation of microtubule plus-end binding; IDA:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:1902888; P:protein localization to astral microtubule; ISS:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:MGI.
DR GO; GO:0035372; P:protein localization to microtubule; IMP:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Microtubule; Mitosis;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..268
FT /note="Microtubule-associated protein RP/EB family member
FT 1"
FT /id="PRO_0000213417"
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..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3"
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 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15691"
FT MUTAGEN 211..215
FT /note="EKERD->KKERK: Loss of interaction with APC and
FT DCTN1."
FT /evidence="ECO:0000269|PubMed:15311282"
FT MUTAGEN 211..213
FT /note="EKE->AKA: Partial loss of interaction with APC."
FT /evidence="ECO:0000269|PubMed:15311282"
FT MUTAGEN 220..222
FT /note="KLR->ALA: Loss of interaction with APC and DCTN1."
FT /evidence="ECO:0000269|PubMed:15311282"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1V5K"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:1V5K"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1V5K"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1V5K"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1V5K"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:1V5K"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1V5K"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:1V5K"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:1V5K"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:1V5K"
FT HELIX 192..231
FT /evidence="ECO:0007829|PDB:6EVI"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6EVI"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:6EVI"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6EVQ"
SQ SEQUENCE 268 AA; 30016 MW; 8FE3AFB7A5AE7762 CRC64;
MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK
VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD
GKEYDPVAAR QGQETAVAPS LVAPALSKPK KPLGSSTAAP QRPIATQRTT AAPKAGPGMV
RKNPGVGNGD DEAAELMQQV KVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ
RIVDILYATD EGFVIPDEGG PQEEQEEY
