SPDLY_MACFA
ID SPDLY_MACFA Reviewed; 605 AA.
AC Q4R7H3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 57.
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 {ECO:0000255|HAMAP-Rule:MF_03041};
GN Synonyms=CCDC99 {ECO:0000255|HAMAP-Rule:MF_03041}; ORFNames=QtsA-15340;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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. 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; AB168845; BAE00949.1; -; mRNA.
DR RefSeq; NP_001271899.1; NM_001284970.1.
DR RefSeq; XP_005558540.1; XM_005558483.1.
DR RefSeq; XP_005558541.1; XM_005558484.1.
DR AlphaFoldDB; Q4R7H3; -.
DR SMR; Q4R7H3; -.
DR STRING; 9541.XP_005558540.1; -.
DR GeneID; 101926343; -.
DR KEGG; mcf:101926343; -.
DR CTD; 54908; -.
DR VEuPathDB; HostDB:ENSMFAG00000026820; -.
DR eggNOG; ENOG502S27G; Eukaryota.
DR OMA; SCPNNLE; -.
DR Proteomes; UP000233100; Chromosome 6.
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: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..605
FT /note="Protein Spindly"
FT /id="PRO_0000274517"
FT REGION 545..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..442
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03041"
FT COMPBIAS 547..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..581
FT /note="Basic and acidic 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 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EA4"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EA4"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923A2"
SQ SEQUENCE 605 AA; 70138 MW; A521F4000A403DAF CRC64;
METDIVINLR CKLKEAEEER LKAAQYGLQL VESQNELQNQ LDKCRNEMMT MTESYEQEKY
TLQREVELKS RMLESLSCEC EAIKQQQKMH LEKLEEQLSR SHGQEVNELK SKIEKLKVEL
DEARLSEKQL KHQVDHQKEL LSCKSEELRV MSERVQESMS SEMLALQIEL TEMESMKTTL
KEEVNELQYR QEQLELLITN LMRQVDRLKE EKEEREKEAV SYYNALEKAR VANQDLQVQL
DQALQQALDP NSKGNSLFAE VEDRRAAMER QLISMKVKYQ SLKKQNVFNR EQMQRMKLQI
ATLLQMKGSQ TEFEQQERLL AMLEQKNGEI KHLLGEIRNL EKFKNLYESM ESKPSVDSGA
LEDNTYYTDL LQMKLDNLNK EIESTKGELS IQRMKALFES QRALDIERKL FANERCLQLS
ESENMKLRAK LDELKLKYEP EETVEVPVLK KRREVLPVDI TTSKDTCVNN SAVGGEVYRL
PPQKEETQCC PNSLEDNNLQ LEKSVSIHTP IVSLSPHKNL PVDMQLKKEK KCVKLVGVPA
DAEALSERSG NTLNSPRLAA ESKLQTEVKE GKETASKLEK ETCKKSHPIL YVSSKSTPET
QCPQQ
