ID   SPDLY_DANRE             Reviewed;         590 AA.
AC   A7MD70; A4IGD1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
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; ORFNames=zgc:171223;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2007) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI35039.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; BC135038; AAI35039.1; ALT_SEQ; mRNA.
DR   EMBL; BC152508; AAI52509.1; -; mRNA.
DR   RefSeq; NP_001098412.1; NM_001104942.1.
DR   AlphaFoldDB; A7MD70; -.
DR   SMR; A7MD70; -.
DR   STRING; 7955.ENSDARP00000098483; -.
DR   PaxDb; A7MD70; -.
DR   PeptideAtlas; A7MD70; -.
DR   GeneID; 568360; -.
DR   KEGG; dre:568360; -.
DR   CTD; 54908; -.
DR   ZFIN; ZDB-GENE-070928-7; spdl1.
DR   eggNOG; ENOG502S27G; Eukaryota.
DR   InParanoid; A7MD70; -.
DR   OrthoDB; 1595638at2759; -.
DR   PhylomeDB; A7MD70; -.
DR   Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR   PRO; PR:A7MD70; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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..590
FT                   /note="Protein Spindly"
FT                   /id="PRO_0000383342"
FT   REGION          446..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..401
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03041"
FT   COMPBIAS        448..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..572
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  68964 MW;  62839127050CD908 CRC64;
     MSDLEDEIKV LRRKVQDGEE ALQRAGQYGL QLLDEKMELH NRLEEQRTEM SNVIEALEQD
     KYTLQREVEL KIRMLESLRS EFDLVRTQQK HQMEQQQTLL ERNHAVEISD LKNKVVKMKT
     DLEEAQLAEK QMRHKLDQQA EALNSKTEEL RALTERAHET MSSEILELQV QKMELESAMA
     TLEQELQEAQ YKDEQLHLAN TTLQRQLERL TEEKEEREKE AVSCYNALEK AREANQDLQI
     QLEQVLQQAQ DPNSKGNSLF SEVEDKRAAM ERQLNSMKRN YDSLQKQHVL TKQHMHHMKM
     QIATLMQLQG NRADPAQLER LQFMLSDKNK EIESLMMKVR ELEKEKMAVK DHHPHPPSNE
     GELKDETYYT DLLKMQLANS KKDAEKLKEE LSMARMKALS ESQRVLELER KLYGTEQALK
     LRHSDNMKLQ VKLEELKIKY TPNEVNKAQV QKRRREKFPV PEENSASVKD ETTTQDTELS
     KNSNEKAEEK TPSHPVEKPV VIPLQSEHPT EPNPVLSRES KSVRICEDPP VCIPDAPRSP
     VNDSNSKNVD QTHQSSEEEE NWRTEKKRKK YQQPTHVSSQ KTMANECAQQ