EMAL4_XENTR
ID EMAL4_XENTR Reviewed; 928 AA.
AC Q6DIP5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Echinoderm microtubule-associated protein-like 4;
DE Short=EMAP-4;
GN Name=eml4;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for the formation and stability of microtubules
CC (MTs) (By similarity). Required for the organization of the mitotic
CC spindle and for the proper attachment of kinetochores to MTs (By
CC similarity). Promotes the recruitment of NUDC to the mitotic spindle
CC for mitotic progression (By similarity).
CC {ECO:0000250|UniProtKB:Q9HC35}.
CC -!- SUBUNIT: Homotrimer; self-association is mediated by the N-terminal
CC coiled coil. {ECO:0000250|UniProtKB:Q9HC35}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9HC35}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9HC35}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000250|UniProtKB:Q9HC35}. Midbody
CC {ECO:0000250|UniProtKB:Q9HC35}. Note=Localizes to microtubules (MTs)
CC during interphase with a significantly reduced affinity for MTs during
CC mitosis. {ECO:0000250|UniProtKB:Q9HC35}.
CC -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}.
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DR EMBL; BC075490; AAH75490.1; -; mRNA.
DR RefSeq; NP_001006917.1; NM_001006916.1.
DR AlphaFoldDB; Q6DIP5; -.
DR SMR; Q6DIP5; -.
DR STRING; 8364.ENSXETP00000058702; -.
DR DNASU; 448764; -.
DR GeneID; 448764; -.
DR KEGG; xtr:448764; -.
DR CTD; 27436; -.
DR Xenbase; XB-GENE-971027; eml4.
DR eggNOG; KOG2106; Eukaryota.
DR HOGENOM; CLU_011754_0_1_1; -.
DR InParanoid; Q6DIP5; -.
DR OrthoDB; 271572at2759; -.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR005108; HELP.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 9.
DR SUPFAM; SSF50998; SSF50998; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..928
FT /note="Echinoderm microtubule-associated protein-like 4"
FT /id="PRO_0000284394"
FT REPEAT 199..237
FT /note="WD 1"
FT REPEAT 241..288
FT /note="WD 2"
FT REPEAT 296..336
FT /note="WD 3"
FT REPEAT 343..378
FT /note="WD 4"
FT REPEAT 385..424
FT /note="WD 5"
FT REPEAT 442..480
FT /note="WD 6"
FT REPEAT 485..521
FT /note="WD 7"
FT REPEAT 524..563
FT /note="WD 8"
FT REPEAT 567..604
FT /note="WD 9"
FT REPEAT 610..646
FT /note="WD 10"
FT REPEAT 653..692
FT /note="WD 11"
FT REPEAT 702..760
FT /note="WD 12"
FT REPEAT 767..806
FT /note="WD 13"
FT REGION 1..189
FT /note="Microtubule-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT REGION 107..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..63
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT COMPBIAS 115..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 102611 MW; C27953BAFD1E22DE CRC64;
MDGFAGSLDD SVSAASTSDV QDRLSALELR VQQQEDEITV LKAALADVLR RLAISEDQVA
TVRKAVPSKG PATMREALSM SCITNGGAGT RKPSHITSVA KKDTLSSAAK SVKRSSTIEK
SHNSWDASEE SRNKLMRAAS TSKLTSKVAK ATDKHKDIVI SPEGEYIKMF MRGRPITMFI
PSDVENYDDI RTELPPEKLK LEWVFGYRGR DCRANVYLLP TGEIVYFIAS VVVLFNYEER
TQRHYLGHTD CVKCIAVHPD KIRIATGQIA GVDKDGRPLQ PHVRVWDSVS LSTLQVIGLG
TFERGVGCLA FSKADSGVHL SVIDDSNEHM LTVWDWQKKS KIAEIKTTNE VVLTVEFHPT
DACTIVTCGK SHIFFWTWSG NSLARKQGIF GKYEKPKFVQ CLAFLANGDV LAGDSGGVML
IWSKTTVEST ASKGAKVLGV YQISRQIKAH DGSVFTLCQM RNGMLLTGGG KDRKVIMWDH
DLNPEREIEV PDQYGTIRAV AEGKGDQFLI GTSRNFILRG TFNDGFQVEV QGHTDELWGL
ATHPFKDLLL TCAQDKQVCL WNSVDHSLEW TRVLDEPGHC ADFHPTGTVV AIGTHSGRWF
VLDAETRDLV SIHTDGNEQL SVMRYSVDGA LLAVGSHDNF IYLYNVSENG RKYSRYGKCT
GHSSYITHLD WSPDNQYIMS NSGDYEILYW DIPSGCKLIR NRSDCKDINW ATYTCVLGFQ
VFGVWPEGSD GTDINALVRS HNRKVIALAD DFCKVHLFQY PCSKPKAPSH KYSAHSSHVT
NVSFTHKDSH LISTGGKDMS IMQWRLIEKV SHSQNDNIVE SSSAVNSPVV TEKPLQPNTP
TNLPQAVNEV PKEDDKTPAE SPVPAEDALE QPEELNEVQS EKCSSQPEGA NGQEPSNEVS
EDPTDSAAIN NTPEDAQDEN QDDSSPLS
