SPDLY_XENTR
ID SPDLY_XENTR Reviewed; 611 AA.
AC B3DLE8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041};
DE AltName: Full=Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041};
DE AltName: Full=Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041};
GN Name=spdl1; Synonyms=ccdc99;
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-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for the localization of dynein and dynactin to the
CC mitotic kintochore. Dynein is believed to control the initial lateral
CC interaction between the kinetochore and spindle microtubules and to
CC facilitate the subsequent formation of end-on kinetochore-microtubule
CC attachments mediated by the NDC80 complex. May act as an adapter
CC protein linking the dynein motor complex to various cargos (By
CC similarity). {ECO:0000250|UniProtKB:Q96EA4, ECO:0000255|HAMAP-
CC Rule:MF_03041}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000255|HAMAP-Rule:MF_03041}.
CC -!- SIMILARITY: Belongs to the Spindly family. {ECO:0000255|HAMAP-
CC Rule:MF_03041}.
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DR EMBL; BC167418; AAI67418.1; -; mRNA.
DR RefSeq; NP_001123745.1; NM_001130273.1.
DR AlphaFoldDB; B3DLE8; -.
DR SMR; B3DLE8; -.
DR STRING; 8364.ENSXETP00000043089; -.
DR PaxDb; B3DLE8; -.
DR GeneID; 100170491; -.
DR KEGG; xtr:100170491; -.
DR CTD; 54908; -.
DR Xenbase; XB-GENE-5754925; spdl1.
DR eggNOG; ENOG502S27G; Eukaryota.
DR InParanoid; B3DLE8; -.
DR OrthoDB; 1595638at2759; -.
DR Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000940; C:outer kinetochore; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0043515; F:kinetochore binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR GO; GO:0034501; P:protein localization to kinetochore; ISS:UniProtKB.
DR HAMAP; MF_03041; SPDLY; 1.
DR InterPro; IPR028593; SPDLY_chordates.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil;
KW Kinetochore; Mitosis; Reference proteome.
FT CHAIN 1..611
FT /note="Protein Spindly"
FT /id="PRO_0000383345"
FT REGION 499..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..288
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03041"
FT COMPBIAS 525..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 70708 MW; AC1318511998B376 CRC64;
MEESETVLKL RLQLKEAEEE RIKAAQYGLE LLESQSDLQN QLEEQRNEMT STIENLEQEK
YSLQREVELK NRMLESLTSE CENIRQQQKL CLEQLQEQLE RNHHRELSEI KDKLEKLKAE
LDEARLSEKQ LKHKLEYQSE VLANKSEELR MMSERVHETM SSEMLTLQLE KTELESAKAN
LEQEVNELQY REQQLLLTNG TQSRQLERLQ DEKEDREKEA VGYFKALEKA REANQDLQAQ
LDIALQQAQD PNSKGNSLFA EVEDRRAEME RQLISMKVQF QSLQKQHAFS RQQMHRMKVQ
IATLLQLKGS QSDPEQLERL QAMVAQKNSE FETLVMKVRQ LEKSQQICEN GPVANSSDGL
GQGDETYYVD LLKMKLVNSS KEIEKIKDEL SLQRMKALAE SQRVLDLERK LFANDRHLKL
SQGENMKLRV NLDEMKMKYE PDEIAKIRTQ KRRKEQLPLD CAIDNTSATV TSGSQAHGLS
DAIPEDMCPA ESTVHRNLLK EDSSLSTKEQ DLSSVAVKPI EPANGQPPKE RKRVRIVENE
NDNQDINKRN TNNCSVTSTS PRSASEESTS ESKRFDEEQE KRKQERKSRL RAPPVLHVPS
KPAATTQCPQ Q