ID   SPDLA_XENLA             Reviewed;         611 AA.
AC   Q5BIX7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Protein Spindly-A {ECO:0000255|HAMAP-Rule:MF_03041};
DE   AltName: Full=Coiled-coil domain-containing protein 99-A {ECO:0000255|HAMAP-Rule:MF_03041};
DE   AltName: Full=Spindle apparatus coiled-coil domain-containing protein 1-A {ECO:0000255|HAMAP-Rule:MF_03041};
GN   Name=spdl1-a; Synonyms=ccdc99-a;
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=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2005) 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. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC091716; AAH91716.1; -; mRNA.
DR   RefSeq; NP_001089308.1; NM_001095839.1.
DR   AlphaFoldDB; Q5BIX7; -.
DR   SMR; Q5BIX7; -.
DR   DNASU; 734358; -.
DR   GeneID; 734358; -.
DR   KEGG; xla:734358; -.
DR   CTD; 734358; -.
DR   Xenbase; XB-GENE-5754977; spdl1.L.
DR   OrthoDB; 1595638at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 734358; Expressed in egg cell and 19 other tissues.
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-A"
FT                   /id="PRO_0000383343"
FT   REGION          487..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..390
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03041"
FT   COMPBIAS        493..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..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;  70573 MW;  111B7C4BF64140AE CRC64;
     MEESETVLKL RRQLKEAEEE RVKAAHYGLE LLESQSDLQN QLEEQRNEMT GTIENLEQEK
     YSLQREVELK NRMLESVTSE CENIRQQQKL ILEQLQEQLE RNHHRELGEI KDKLEKLKAE
     LDEARLSEKQ LKHKLEYQTE VLANKSEELR MMSERVHETM SSEMLTLQLE KTELESAKAN
     LEQEVNELQY REQQLLLTNG TQSRKLEHLQ TEKEEREKES VGYFSALEKA REANQDLQAQ
     LDIALQQAQD PNSKGNSLFS EVEDRRAEME RQLISMKVQF QSLQKQHAFS RQQMHRMKVQ
     IATLLQMKGS QSDPEQLERL QAMVAQKNSE IEALVMKVRQ LEKSQQVSEN GPAVGSSDNL
     GQGDETYYVD LLKMKLLNSS KENEKIKDEL SLQRMKALAE SQRVLELERK LFANDRHLKL
     SQGENMKLRV SLDEIKMKYE PDEMGKIHTQ KRRKEQLPLD FPMDNTSAAV TSGTEAQGLY
     DATAGETCTA ESTDGRIHSK EDLSLSTKEQ DPSSVAVKPK ELPNGPPPKE RKRVRIMEDE
     NNAQDLNKRN THNCSVTSAS PRSTSEDATS ESKRFDEEQE KRKQERKSRL RAPPVLHVPS
     KPNATTQCPQ Q