GenomeNet

Database: UniProt
Entry: G3TLT9_LOXAF
LinkDB: G3TLT9_LOXAF
Original site: G3TLT9_LOXAF 
ID   G3TLT9_LOXAF            Unreviewed;      1910 AA.
AC   G3TLT9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=EMAP like 6 {ECO:0000313|Ensembl:ENSLAFP00000015938.3};
GN   Name=EML6 {ECO:0000313|Ensembl:ENSLAFP00000015938.3};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000015938.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000015938.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015938.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000015938.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000015938.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May modify the assembly dynamics of microtubules, such that
CC       microtubules are slightly longer, but more dynamic.
CC       {ECO:0000256|ARBA:ARBA00003210}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the WD repeat EMAP family.
CC       {ECO:0000256|ARBA:ARBA00006489}.
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DR   Ensembl; ENSLAFT00000020496.3; ENSLAFP00000015938.3; ENSLAFG00000020864.3.
DR   GeneTree; ENSGT00940000155564; -.
DR   HOGENOM; CLU_001930_0_0_1; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 6.
DR   InterPro; IPR024977; Apc4-like_WD40_dom.
DR   InterPro; IPR011048; Haem_d1_sf.
DR   InterPro; IPR005108; HELP.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR13720:SF52; ECHINODERM MICROTUBULE-ASSOCIATED PROTEIN-LIKE 6; 1.
DR   PANTHER; PTHR13720; WD-40 REPEAT PROTEIN; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   Pfam; PF03451; HELP; 2.
DR   Pfam; PF00400; WD40; 10.
DR   SMART; SM00320; WD40; 29.
DR   SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 2.
DR   SUPFAM; SSF50978; WD40 repeat-like; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 7.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          266..298
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          495..527
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          604..651
FT                   /note="HELP"
FT                   /evidence="ECO:0000259|Pfam:PF03451"
FT   REPEAT          950..971
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1170..1202
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          1285..1345
FT                   /note="HELP"
FT                   /evidence="ECO:0000259|Pfam:PF03451"
FT   REPEAT          1642..1676
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          1687..1764
FT                   /note="Anaphase-promoting complex subunit 4-like WD40"
FT                   /evidence="ECO:0000259|Pfam:PF12894"
FT   REPEAT          1718..1759
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1875..1910
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          533..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..567
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1910 AA;  212002 MW;  F0DD07A8037E5BF4 CRC64;
     FSLALHPDKT LVATGQVGKE PYICVWDSYN VQTVSILKDV HTHGVACLAF DSDGQRLASV
     GLDAKNTVCI WDWRKGKLLA SATGHSDRIF DISWDPYQPN RAVSCGVKHI KFWTLCGNAL
     TAKRGIFGKT GDLQTILCLA CAKEDITYSG ALNGDIYVWK GLNLVRTIQG AHSAGIFSLY
     ACEEGFATGG RDGCIRLWDT DFKPITKIDL RETEQGYKGL SIRSVCWKAD RLLAGTQDSE
     IFEVIVRERD KPMLILQGHC EGELWALALH PKKPLAVTGS DDRSVRLWSL ADHALIARCN
     MEEAVRSVAF SPDGSQLALG MKDGSFIVLR VRDMTEVVHI KDRKEVIHEM KFAPDGSYLA
     VGSNDGPVDV YAVAQRYKKI GECSRSVSFI THIDWSLDSK YLQTNDGAGA RLFYRMPSGK
     PLTSKEEIKG IPWASWTCVK GPEVSGIWPK YTDVTDINSV DANYDSSVLV SGDDFGLVKL
     FKFPCLKKGA KFRKYVGHSA HVTNVRWSHD FQWVLSTGGA DHSVFQWRFI PEGVTNGTPE
     TTPQEGGTDS YSEESDSDLS DVPELDSDIE QETQINYDRQ VYKEDLPQLK QQSKEKNQAV
     PFLKREKAPE DSLRLQFIHG YRGYDCRNNL LYTQAGEVVY HIAAAAVVYD RQQHTQRLYL
     GHDDDILSLT IHPVKDYVAT GQVGRDAAVH VWDTQTLKCL SLLKGQHQRG VCALDFSADG
     KCLVSVGLDD FHSIVFWDWK KGEKIATTRG HKDKIFVIKC NPHHVDKLVT VGMKHIKFWQ
     QAGGGFTSKR GIFGSVGKLE TMMCVSYGRM EDLVFSGAAT GDIFIWKDIL LLKTVKAHDG
     PVFAMYALDK GFVTGGKDGI VELWDDMFER CLKTYAIKRA ALSTSSKGLL LEDNPSIRAI
     TLGHGHILVG TKNGEILEID KSGPMTLLVQ GHMEGEVWGL AAHPLLPICA TVSDDKTLRI
     WDLSSQHRML AVRKLKKGGR CCAFSPDGKA LAVGLNDGSF LVVNADTVED MVSFHHRKEM
     ISDIKFSKDT GKYLAVASHD NFVDIYNVLT SKRVGICRGA SSYITHIDWD SRGKLLQVNS
     GAKEQLFFEA PRGKRHIIRP SEIEKIEWDT WTCVLGPTCE GIWPAHSHVT DVNAASLTKD
     CSLLATGDDF GFVKLFSYPV KGQHARFKKY VGHSAHVTNV RWLHNDSVLL TVGGADTALM
     IWTREFVGTQ ESKLVDSEES DTDVEEDGGY DSDVAREKAI DYTTKIYAVS IREMEGTKPH
     QQLKEVSMEE RYGVASGLQP PVSRAAPQPE KLQKNNVTKK KKLVEELALD HVFGYRGFDC
     RNNLHYLNDG ADIIFHTAAA GVVQNLSTGS QSFYLEHTDD ILCLTVNQHP KYRNVVATSQ
     IGRSCLPHPG TTPSIHIWDA MTKHTLSMLR CFHSKGVNYI NFSATGKLLV SVGVDPEHTI
     TVWRWQEGAK VASRGGHLER IFVVEFRPDS DTQFVSVGVK HMKFWTLAGS ALLYKKGVTG
     SMEAAKMQTM LSVAFGANNL TFTGAINGDV YVWKDHFLVR LVAKAHTGPV FTMYTTLRDG
     LIVTGGKERP TKEGGAVKLW DQEMKRCRAF QLETGQLVEC VRSVCRGKGK ILVGTKDGEI
     IEVGEKNAAS NILIDGHMEG EIWGLATHPS KDIFISASND GTARIWDLAD KKLLNKVNLG
     HAARCAAYSP DGEMVAIGMK NGEFVILLVN SLKVWGKKRD RKSAIQDIRI SPDNRFLAVG
     SSEHTVDFYD LTQGTSLNRT GYCKDIPSFV IQMDFSADSK YIQVSTGAYK RQVHEVPLGK
     QVTDATVVEK ITWASWTSIL GDEVIGIWPR NADKADVNCA CVTHAGLNIV TGDDFGLVKL
     FDFPCTEKFA KHKRYFGHSA HVTNIRFSHD DKYVVSTGGD DCSVFVWRCL
//
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