SPDL1_CAEEL
ID SPDL1_CAEEL Reviewed; 479 AA.
AC Q17695;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Spindly-like protein spdl-1 {ECO:0000305};
GN Name=spdl-1 {ECO:0000303|PubMed:18765790, ECO:0000303|PubMed:18936247,
GN ECO:0000312|WormBase:C06A8.5};
GN ORFNames=C06A8.5 {ECO:0000312|WormBase:C06A8.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ZWL-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18765790; DOI=10.1101/gad.1687508;
RA Gassmann R., Essex A., Hu J.-S., Maddox P.S., Motegi F., Sugimoto A.,
RA O'Rourke S.M., Bowerman B., McLeod I., Yates J.R. III, Oegema K.,
RA Cheeseman I.M., Desai A.;
RT "A new mechanism controlling kinetochore-microtubule interactions revealed
RT by comparison of two dynein-targeting components: SPDL-1 and the
RT Rod/Zwilch/Zw10 complex.";
RL Genes Dev. 22:2385-2399(2008).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MDF-1 AND MDF-2, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18936247; DOI=10.1083/jcb.200805185;
RA Yamamoto T.G., Watanabe S., Essex A., Kitagawa R.;
RT "SPDL-1 functions as a kinetochore receptor for MDF-1 in Caenorhabditis
RT elegans.";
RL J. Cell Biol. 183:187-194(2008).
RN [4] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PHE-199.
RX PubMed=24231804; DOI=10.1126/science.1246232;
RA Cheerambathur D.K., Gassmann R., Cook B., Oegema K., Desai A.;
RT "Crosstalk between microtubule attachment complexes ensures accurate
RT chromosome segregation.";
RL Science 342:1239-1242(2013).
CC -!- FUNCTION: Transient kinetochore component required for chromosome and
CC spindle pole alignment and chromosome segregation during mitosis
CC (PubMed:18765790, PubMed:18936247). Functions downstream of the RZZ
CC complex to mediate kinetochore-microtubule attachments and nuclear
CC envelope breakdown during cell division (PubMed:18765790,
CC PubMed:18936247, PubMed:24231804). Required for kinetochore assembly
CC and localizes the checkpoint proteins mdf-1 and mdf-2, dynein and
CC dynactin to unattached kinetochores (PubMed:18765790, PubMed:18936247,
CC PubMed:24231804). 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 (PubMed:24231804). Required
CC for embryonic development (PubMed:18765790, PubMed:18936247).
CC {ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:18936247,
CC ECO:0000269|PubMed:24231804}.
CC -!- SUBUNIT: Interacts with Zwilch homolog zwl-1, a component of the RZZ
CC complex (PubMed:18765790). Interacts with mdf-1 and mdf-2
CC (PubMed:18936247). {ECO:0000269|PubMed:18765790,
CC ECO:0000269|PubMed:18936247}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:18936247}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:18765790}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:18936247}. Note=Localizes to
CC microtubules during mitosis (PubMed:18936247). Recruited to the
CC kinetochore by the RZZ complex (PubMed:18765790, PubMed:18936247).
CC Localization to the kinetochore is also dependent on the NDC80 complex
CC and bub-1 (PubMed:18765790). Localizes to the kinetochore during
CC nuclear envelope breakdown and remains there until the metaphase-
CC anaphase transition (PubMed:18765790, PubMed:18936247).
CC {ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:18936247}.
CC -!- DISRUPTION PHENOTYPE: Recessive embryonic lethality (PubMed:18936247).
CC Hemizygous mutants are viable and survive through embryogenesis, but
CC are either lethal at the larval stage of development or sterile
CC (PubMed:18936247). The oocytes of sterile mutants have extra
CC chromosomes and prematurely exit the prophase stage of meiosis which
CC results in endomitosis (PubMed:18936247). RNAi-mediated knockdown
CC results in embryonic lethality (PubMed:18765790, PubMed:18936247). RNA-
CC mediated knockdown results in defective cell division characterized by
CC irregular chromosome alignment and segregation, longer spindles during
CC chromatid separation, premature spindle pole separation, defective
CC formation of kinetochore-microtubule attachments and chromatin bridge
CC formation during the anaphase stage of mitosis (PubMed:18765790,
CC PubMed:18936247, PubMed:24231804). {ECO:0000269|PubMed:18765790,
CC ECO:0000269|PubMed:18936247, ECO:0000269|PubMed:24231804}.
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DR EMBL; BX284602; CCD61463.1; -; Genomic_DNA.
DR PIR; T15425; T15425.
DR RefSeq; NP_495637.1; NM_063236.5.
DR AlphaFoldDB; Q17695; -.
DR SMR; Q17695; -.
DR DIP; DIP-27271N; -.
DR IntAct; Q17695; 12.
DR MINT; Q17695; -.
DR STRING; 6239.C06A8.5; -.
DR EPD; Q17695; -.
DR PaxDb; Q17695; -.
DR PeptideAtlas; Q17695; -.
DR EnsemblMetazoa; C06A8.5.1; C06A8.5.1; WBGene00015515.
DR GeneID; 174256; -.
DR KEGG; cel:CELE_C06A8.5; -.
DR UCSC; C06A8.5; c. elegans.
DR CTD; 174256; -.
DR WormBase; C06A8.5; CE02456; WBGene00015515; spdl-1.
DR eggNOG; ENOG502TFNV; Eukaryota.
DR HOGENOM; CLU_565283_0_0_1; -.
DR InParanoid; Q17695; -.
DR OMA; DIDVKEM; -.
DR OrthoDB; 1181530at2759; -.
DR PhylomeDB; Q17695; -.
DR SignaLink; Q17695; -.
DR PRO; PR:Q17695; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00015515; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:WormBase.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0090268; P:activation of mitotic cell cycle spindle assembly checkpoint; IGI:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IGI:WormBase.
DR GO; GO:1905561; P:positive regulation of kinetochore assembly; IGI:UniProtKB.
DR GO; GO:1905824; P:positive regulation of mitotic sister chromatid arm separation; IMP:UniProtKB.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IMP:UniProtKB.
DR GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IMP:UniProtKB.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IGI:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:WormBase.
DR GO; GO:1902423; P:regulation of attachment of mitotic spindle microtubules to kinetochore; IMP:WormBase.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis;
KW Reference proteome.
FT CHAIN 1..479
FT /note="Spindly-like protein spdl-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438728"
FT COILED 4..180
FT /evidence="ECO:0000255"
FT COILED 210..250
FT /evidence="ECO:0000255"
FT COILED 321..357
FT /evidence="ECO:0000255"
FT MUTAGEN 199
FT /note="F->A: Abolishes dynein recruitment to kinetochores."
FT /evidence="ECO:0000269|PubMed:24231804"
SQ SEQUENCE 479 AA; 55285 MW; 5F5A9E8C26C28766 CRC64;
MPDDEEKLQL LADVERLKKI LRQKDEMLEE MEDDLKNQGK PCSSKLSLEE RAQELSEQLR
DLHVEMDGKN ATILDRDALI DSLRSEIDKL EKINKEFANG SVIPEHDDSN SFGESEMLRI
SEDCQKYKET ATALYERNAE LEKEAVNLKD EIESMMDHIR DLKNHMETRD EEIARLEGEL
FDERNSHEGK LAARGNSMFS EVIDAERKVE EDLKVLHGEN RALKGMVKRL RMEVEEVEER
LRSSTKRFNV TRMTTSDIDV KEMRRLRDRV CHLETERVHL WERMFIKMRS IPKREVGALI
TGYFKSFELS IASVKGGFDG LMKDNEKYVT IIRGLQQEVE NLKADIVQLQ FDNKCAHRKA
APVVNKDFEH PLLAAPLKTL NNGRPSFFIK PKNVEPMPQL GHSLSSIAVT PQKPAAKFTT
RSSIKDDTSE WAERRMKAQA EKKLATPTPR YNYIKLSEPV PKFKPAVLQM PSTSETKEN
