ID   SKA3_DANRE              Reviewed;         495 AA.
AC   Q58EL7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Spindle and kinetochore-associated protein 3;
GN   Name=ska3; Synonyms=rama1;
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: Component of the SKA1 complex, a microtubule-binding
CC       subcomplex of the outer kinetochore that is essential for proper
CC       chromosome segregation. The SKA1 complex is a direct component of the
CC       kinetochore-microtubule interface and directly associates with
CC       microtubules as oligomeric assemblies. The complex facilitates the
CC       processive movement of microspheres along a microtubule in a
CC       depolymerization-coupled manner. In the complex, it mediates the
CC       microtubule-stimulated oligomerization. Affinity for microtubules is
CC       synergistically enhanced in the presence of the ndc-80 complex and may
CC       allow the ndc-80 complex to track depolymerizing microtubules.
CC       {ECO:0000250|UniProtKB:Q8IX90}.
CC   -!- SUBUNIT: Component of the SKA1 complex, composed of ska1, ska2 and
CC       ska3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:Q8IX90}. Chromosome, centromere, kinetochore
CC       {ECO:0000250|UniProtKB:Q8IX90}. Note=Localizes to the outer kinetochore
CC       and spindle microtubules during mitosis in a NDC80 complex-dependent
CC       manner. {ECO:0000250|UniProtKB:Q8IX90}.
CC   -!- SIMILARITY: Belongs to the SKA3 family. {ECO:0000305}.
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DR   EMBL; BC091849; AAH91849.1; -; mRNA.
DR   EMBL; CK675017; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; Q58EL7; -.
DR   SMR; Q58EL7; -.
DR   STRING; 7955.ENSDARP00000116579; -.
DR   iPTMnet; Q58EL7; -.
DR   PaxDb; Q58EL7; -.
DR   ZFIN; ZDB-GENE-030131-2997; ska3.
DR   eggNOG; ENOG502QSTX; Eukaryota.
DR   InParanoid; Q58EL7; -.
DR   PhylomeDB; Q58EL7; -.
DR   PRO; PR:Q58EL7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR   GO; GO:0000940; C:outer kinetochore; ISS:UniProtKB.
DR   GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISS:UniProtKB.
DR   InterPro; IPR033341; SKA3.
DR   PANTHER; PTHR48118; PTHR48118; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Kinetochore; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..495
FT                   /note="Spindle and kinetochore-associated protein 3"
FT                   /id="PRO_0000373898"
FT   REGION          119..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
FT   CONFLICT        37
FT                   /note="E -> G (in Ref. 1; AAH91849)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   495 AA;  55834 MW;  3DA6865A6880B7B2 CRC64;
     MNPSERFFSK LRKLTVYLET ESSSLLHTSQ NLKEDEEDEE TGAQALYQLH SEVRALKRQV
     RDQVATHDTS SADLRSFIRR CLVLKQRTTE DIDSLKKHYE KYGYRPRISR LGSTEVNCTK
     EAEERAERDA EKLDAAEEDE ETERGDCDKV DQSVTPEKMP PPVDQLQTPK LSDFGLSALQ
     FQRVLGEAEV PLSAAPESAI ALSSPPILMN LQPPQPKTPK CSLSMEEDAL TPRLEDFGIS
     EYTMCWNNDF TMDLFNKKPP KNRSERNENV LKPHNVFSNT SSVLNKDVAN KSLESPEPPE
     FCTPGFKIAK NHVPSTPLFN GKNDLNSPPR LNNNCPSTPE LPAFETPFVS KLIKKEDREE
     ESKIHSESQE NSLRLPDLST TNGTSWNDAP EMPKMLRYEE EALPEMPILQ SNFGSSLAFK
     NTSGESLSRM KTGAGHMLEM KQTSVPVPED GFNQDWCLST PKVRVKFPAE PCTPEMPDMS
     SVTQDILKLV AQCKY