ID A0A1I7VST1_LOALO Unreviewed; 337 AA.
AC A0A1I7VST1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=EBF3-S protein {ECO:0000313|WBParaSite:EN70_5838};
OS Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_5838};
RN [1] {ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_5838}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MAPRE family.
CC {ECO:0000256|ARBA:ARBA00010729}.
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DR AlphaFoldDB; A0A1I7VST1; -.
DR STRING; 7209.A0A1I7VST1; -.
DR WBParaSite; EN70_5838; EN70_5838; EN70_5838.
DR eggNOG; KOG3000; Eukaryota.
DR Proteomes; UP000095285; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:SF6; EB1, ISOFORM F-RELATED; 1.
DR PANTHER; PTHR10623; MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|PROSITE-ProRule:PRU00576};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000095285}.
FT DOMAIN 55..157
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 254..324
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51230"
FT REGION 169..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 255..282
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 196..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 37793 MW; 2927A2E36C3C8CDA CRC64;
MERSFPILVL IYSDSIIDLT AKSRHWASLL VAEVAGLSSE MSVVNVYATS ATTENLSRHE
MLMWVNDCLQ SNFAKIEEMH TGAAYCQFTD FLFPGSIQLR RVKWNSRLEL DWLSNWKLLQ
TSWKTLGVDK IVPVEKLIKG KFQDNFEFLQ WFKKFFDANF DGHEYDPLEA RGGEPLPSDV
KINPPSRMPA KSSAPPVRKS TLSTSNASVN KGEMRKAPAV GGKVNPTRTA AQPAAASTAR
TAANPVQPAV DPQIMANLKR ELEEAKEQIA EGDNVIVSLE KERDFYFSKL RQIEVICQDN
EQIGTVDVGR VLTILYETEE GFAPPDENEV ENGDEVY
//
