EMAL4_XENLA
ID EMAL4_XENLA Reviewed; 927 AA.
AC Q2TAF3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Echinoderm microtubule-associated protein-like 4;
DE Short=EMAP-4;
GN Name=eml4;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) 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; BC110954; AAI10955.1; -; mRNA.
DR RefSeq; NP_001089952.1; NM_001096483.1.
DR AlphaFoldDB; Q2TAF3; -.
DR SMR; Q2TAF3; -.
DR BioGRID; 592803; 1.
DR IntAct; Q2TAF3; 2.
DR PRIDE; Q2TAF3; -.
DR DNASU; 735022; -.
DR GeneID; 735022; -.
DR KEGG; xla:735022; -.
DR CTD; 735022; -.
DR Xenbase; XB-GENE-971033; eml4.S.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 735022; Expressed in egg cell and 19 other tissues.
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: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: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 InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 9.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
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..927
FT /note="Echinoderm microtubule-associated protein-like 4"
FT /id="PRO_0000284393"
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 85..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..63
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT COMPBIAS 99..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 102332 MW; 9CA058ABF54A7332 CRC64;
MDGFAGSLDD SVSAASTSDV QDRLSALELR VQQQEDEITV LKAALADVLR RLAISEDQVA
TVRKAVPSKG PATLREALSM SCITNGGAGT RKPSHASSVA KKDTLSSAAK SVKRSSTLEK
SHNSWDASEE SRNKLMRAAS TSKLTSKVSK ATDKHKDIVI SPEGEYIKMF MRGRPITMFI
PSDVENYDDV RTELPPEKLK LEWVFGYRGR DCRANVYLLP TGEIVYFIAS VVVLFNYEER
TQRHYLGHTD CVKCIAVHPD KIRIATGQIA GVDKDGRPLQ PHVRVWDSVS LSTLQVIGLG
TFERGVGCLA FSKADSGVHL SVIDDSNEHM LTVWDWQKKS KIAEIKTTNE VVLAVEFHPT
DAGTIVTCGK SHIFFWTWSG NSLARKQGIF GKYEKPKFVQ CLAFLANGDV LAGDSGGIML
IWSKTNVEST ASKGAKVLGV YQISKQIKAH DGSVFTLCQM RNGMLLTGGG KDRKVIMWDH
DLNPEREIEV PDQYGTIRAV AEGKGDQFLV GTSRNFILRG TFNDGFQVEV QGHTDELWGL
ATHPFKDLLL TCAQDKQVCL WNSVDHSLEW TRVLDEPGHC ADFHPTGTVV AIGTHSGRWF
VLDAETRDLV SIHTDGNEQL SVMRYSVDGA LLAVGSHDNF IYLYNVSENG RKYSRYGKCT
GHSSYITHLD WSPDNQYIMS NSGDYEILYW DIPSGCKLIR NRSECKDINW TTYTCVLGFQ
VFGVWPEGSD GTDINALVRS HNRKVIALAD DFCKVHLFQY PCSKPKAPSH KYSAHSSHVT
NVSFTHNDGH LISTGGKDMS IMQWRLIEKV SHSQNDNIAE SSSAVNSPVV SEKVLQPDTP
TTLPQAVNKA TEVEQTPAES MAPPEDALEL EAQQPQDLDD VQSGKSSPLP EEANGQEPSD
EVIEEPANSQ IVDAQDENQD DDDAPLS
