SPDLY_RAT
ID SPDLY_RAT Reviewed; 597 AA.
AC Q3KR99;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. Also required for correct
CC spindle orientation. Does not appear to be required for the removal of
CC spindle assembly checkpoint (SAC) proteins from the kinetochore upon
CC bipolar spindle attachment. Acts as an adapter protein linking the
CC dynein motor complex to various cargos and converts dynein from a non-
CC processive to a highly processive motor in the presence of dynactin.
CC Facilitates the interaction between dynein and dynactin and activates
CC dynein processivity (the ability to move along a microtubule for a long
CC distance without falling off the track) (By similarity). Plays a role
CC in cell migration (By similarity). {ECO:0000250|UniProtKB:Q96EA4,
CC ECO:0000255|HAMAP-Rule:MF_03041}.
CC -!- SUBUNIT: Interacts with KNTC1 and ZW10. These interactions appear weak
CC and may be transient or indirect. Interacts with dynein intermediate
CC chain and dynactin (DCTN1) (By similarity). Interacts with the
CC catalytically active form of USP45 (By similarity).
CC {ECO:0000250|UniProtKB:Q96EA4, ECO:0000255|HAMAP-Rule:MF_03041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000255|HAMAP-Rule:MF_03041}. Chromosome,
CC centromere, kinetochore {ECO:0000255|HAMAP-Rule:MF_03041}. Nucleus
CC {ECO:0000255|HAMAP-Rule:MF_03041}. Cytoplasm, cytoskeleton, spindle
CC pole {ECO:0000255|HAMAP-Rule:MF_03041}. Note=Localizes to the nucleus
CC in interphase and to the kinetochore in early prometaphase. Relocalizes
CC to the mitotic spindle pole before metaphase and is subsequently lost
CC from the spindle poles after chromosome congression is completed.
CC Removal of this protein from the kinetochore requires the
CC dynein/dynactin complex. {ECO:0000255|HAMAP-Rule:MF_03041}.
CC -!- PTM: Monoubiquitinated with'Lys-48' linkage (By similarity).
CC Deubiquitinated by USP45 (By similarity).
CC {ECO:0000250|UniProtKB:Q96EA4}.
CC -!- SIMILARITY: Belongs to the Spindly family. {ECO:0000255|HAMAP-
CC Rule:MF_03041}.
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DR EMBL; BC105812; AAI05813.1; -; mRNA.
DR RefSeq; NP_001029310.1; NM_001034138.1.
DR RefSeq; XP_006246166.1; XM_006246104.1.
DR AlphaFoldDB; Q3KR99; -.
DR SMR; Q3KR99; -.
DR STRING; 10116.ENSRNOP00000009648; -.
DR iPTMnet; Q3KR99; -.
DR PhosphoSitePlus; Q3KR99; -.
DR PaxDb; Q3KR99; -.
DR Ensembl; ENSRNOT00000009648; ENSRNOP00000009648; ENSRNOG00000007292.
DR GeneID; 303037; -.
DR KEGG; rno:303037; -.
DR UCSC; RGD:1306908; rat.
DR CTD; 54908; -.
DR RGD; 1306908; Spdl1.
DR eggNOG; ENOG502S27G; Eukaryota.
DR GeneTree; ENSGT00510000047951; -.
DR HOGENOM; CLU_031713_0_0_1; -.
DR InParanoid; Q3KR99; -.
DR OMA; SCPNNLE; -.
DR OrthoDB; 1595638at2759; -.
DR PhylomeDB; Q3KR99; -.
DR TreeFam; TF332470; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q3KR99; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000007292; Expressed in thymus and 19 other tissues.
DR Genevisible; Q3KR99; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0043515; F:kinetochore binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
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 Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..597
FT /note="Protein Spindly"
FT /id="PRO_0000274519"
FT REGION 531..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..445
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03041"
FT COMPBIAS 533..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96EA4"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EA4"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923A2"
SQ SEQUENCE 597 AA; 69112 MW; 8405161BE73F7235 CRC64;
MEADITNLRN KLKECEDERL KAAQYGLQLL ERQTELQSQL DKCHEEMMTT AENYNQEKYA
LQREVELKSR MLESLSCECE ALRQQQKAQL EQLEMQLHRS HRQEVHGLRN KLENLKVELD
EARLSEKQLK QKLDHQGELL SHKSEELRLL SEQRALSSVS SELLSLQTEL TEAEGVKNAL
REEVNELQCK QEQLECLNAS LLHQVDRLKE EKEEREKEAV SYYNALEKAR VENQDLQVQL
GHALQQAADP NSKGNSLFAE VEDRRVAMER RLNLMKDKYQ SLKKQNAFTR DQMNKMKLQI
STLLRMRGSQ TEFEQQERLF AMLEQKNGEI KHLLGEINKL EKFKNLYENM ESKSSTSDSA
CALEDSTYYT DLLQLKLDKL NKENESTKGE LSIQRMKALF ESQRTLDIER KLFANERHLQ
LSESENLKLR AKLDELKLKY EPEERIEVPV LKRRREVLPL NINTPEETAA ASATGEDVSR
LPLERKEESC LDNLKDNTVQ WKQPASLSPH KSLPLDTQPK KEKCVTLVAS PASTEVLHEQ
SGNTPSSPRL TEESRLPTKV KERKEATSKL EKGASKKSHT IMYVSSKSTP EMQCPQQ
