ID   SKA1_CAEEL              Reviewed;         243 AA.
AC   Q9XWS0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Spindle and kinetochore-associated protein 1 {ECO:0000312|WormBase:Y106G6H.15};
GN   Name=ska-1 {ECO:0000312|WormBase:Y106G6H.15};
GN   ORFNames=Y106G6H.15 {ECO:0000312|WormBase:Y106G6H.15};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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]
RP   STRUCTURE BY NMR OF 118-243, FUNCTION, INTERACTION WITH SKA-3 AND
RP   MICROTUBULES, AND SUBCELLULAR LOCATION.
RX   PubMed=23085020; DOI=10.1016/j.devcel.2012.09.012;
RA   Schmidt J.C., Arthanari H., Boeszoermenyi A., Dashkevich N.M.,
RA   Wilson-Kubalek E.M., Monnier N., Markus M., Oberer M., Milligan R.A.,
RA   Bathe M., Wagner G., Grishchuk E.L., Cheeseman I.M.;
RT   "The kinetochore-bound Ska1 complex tracks depolymerizing microtubules and
RT   binds to curved protofilaments.";
RL   Dev. Cell 23:968-980(2012).
CC   -!- FUNCTION: Component of the ska-1 complex, a microtubule-binding
CC       subcomplex of the outer kinetochore that is essential for proper
CC       chromosome segregation (PubMed:23085020). Required for timely anaphase
CC       onset during mitosis, when chromosomes undergo bipolar attachment on
CC       spindle microtubules leading to silencing of the spindle checkpoint (By
CC       similarity). The ska-1 complex is a direct component of the
CC       kinetochore-microtubule interface and directly associates with
CC       microtubules as oligomeric assemblies (By similarity). The complex
CC       facilitates the processive movement of microspheres along a microtubule
CC       in a depolymerization-coupled manner (By similarity). Affinity for
CC       microtubules is synergistically enhanced in the presence of the ndc-80
CC       complex and may allow the ndc-80 complex to track depolymerizing
CC       microtubules (PubMed:23085020). In the complex, it mediates the
CC       interaction with microtubules (PubMed:23085020).
CC       {ECO:0000250|UniProtKB:Q96BD8, ECO:0000269|PubMed:23085020}.
CC   -!- SUBUNIT: Component of the ska-1 complex, composed of two copies of ska-
CC       1 and a single copy of ska-3. The core complex associates with
CC       microtubules and may form dimeric assemblies. Interacts with ska-3 and
CC       microtubules. {ECO:0000269|PubMed:23085020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:23085020}. Chromosome, centromere, kinetochore
CC       {ECO:0000269|PubMed:23085020}.
CC   -!- SIMILARITY: Belongs to the SKA1 family. {ECO:0000305}.
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DR   EMBL; AL032631; CAA21578.1; -; Genomic_DNA.
DR   PIR; T26432; T26432.
DR   RefSeq; NP_492739.1; NM_060338.3.
DR   PDB; 2LYC; NMR; -; A=118-243.
DR   PDBsum; 2LYC; -.
DR   AlphaFoldDB; Q9XWS0; -.
DR   BMRB; Q9XWS0; -.
DR   SMR; Q9XWS0; -.
DR   BioGRID; 55492; 3.
DR   ComplexPortal; CPX-811; Ska1 complex.
DR   DIP; DIP-25794N; -.
DR   IntAct; Q9XWS0; 2.
DR   STRING; 6239.Y106G6H.15; -.
DR   EPD; Q9XWS0; -.
DR   PaxDb; Q9XWS0; -.
DR   PeptideAtlas; Q9XWS0; -.
DR   EnsemblMetazoa; Y106G6H.15.1; Y106G6H.15.1; WBGene00013725.
DR   GeneID; 190930; -.
DR   KEGG; cel:CELE_Y106G6H.15; -.
DR   UCSC; Y106G6H.15; c. elegans.
DR   CTD; 190930; -.
DR   WormBase; Y106G6H.15; CE20424; WBGene00013725; ska-1.
DR   eggNOG; KOG4832; Eukaryota.
DR   HOGENOM; CLU_1143437_0_0_1; -.
DR   InParanoid; Q9XWS0; -.
DR   OMA; NWRELEI; -.
DR   OrthoDB; 1435835at2759; -.
DR   PhylomeDB; Q9XWS0; -.
DR   PRO; PR:Q9XWS0; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00013725; 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:WormBase.
DR   GO; GO:0005874; C:microtubule; IDA:ComplexPortal.
DR   GO; GO:0072686; C:mitotic spindle; IDA:WormBase.
DR   GO; GO:0000940; C:outer kinetochore; IBA:GO_Central.
DR   GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IDA:WormBase.
DR   GO; GO:0051301; P:cell division; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IC:ComplexPortal.
DR   GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR   Gene3D; 1.10.10.1890; -; 1.
DR   InterPro; IPR009829; SKA1.
DR   InterPro; IPR042031; SKA1-MBD.
DR   PANTHER; PTHR28573; PTHR28573; 1.
DR   Pfam; PF07160; SKA1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW   Cytoskeleton; Kinetochore; Microtubule; Mitosis; Reference proteome.
FT   CHAIN           1..243
FT                   /note="Spindle and kinetochore-associated protein 1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000373890"
FT   REGION          95..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..243
FT                   /note="Microtubule binding"
FT                   /evidence="ECO:0000269|PubMed:23085020"
FT   COMPBIAS        95..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           128..131
FT                   /evidence="ECO:0007829|PDB:2LYC"
FT   HELIX           136..139
FT                   /evidence="ECO:0007829|PDB:2LYC"
FT   HELIX           144..164
FT                   /evidence="ECO:0007829|PDB:2LYC"
FT   TURN            169..171
FT                   /evidence="ECO:0007829|PDB:2LYC"
FT   HELIX           174..189
FT                   /evidence="ECO:0007829|PDB:2LYC"
FT   HELIX           202..205
FT                   /evidence="ECO:0007829|PDB:2LYC"
FT   HELIX           206..208
FT                   /evidence="ECO:0007829|PDB:2LYC"
FT   HELIX           217..225
FT                   /evidence="ECO:0007829|PDB:2LYC"
FT   TURN            226..228
FT                   /evidence="ECO:0007829|PDB:2LYC"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:2LYC"
SQ   SEQUENCE   243 AA;  28428 MW;  3E16F0E75AB4511A CRC64;
     MESFIDRITE ETDENFRICR ENIPNFETTI SPLLNTMKNI KLLLDDAAFD QQKLENNCEE
     TCMNCTKSQL NDFLGIKVEA STIVDVKSQL VPQSKESSAL VETNEPNEQG LSSKPKENDI
     RIVPQITDEE FKTIPKYQLG RLTLEMMNEI VSKMDDFLMK KSKILGKTNK QLTRSDREVL
     DNWRELEMKA RKRLPTTLFF IETDIRPMLQ DRLRPSFAKA IPCLRHIRRI REERCGPLTF
     YYP