SKA3_BOVIN
ID SKA3_BOVIN Reviewed; 403 AA.
AC A8PUI7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Spindle and kinetochore-associated protein 3;
GN Name=SKA3; Synonyms=RAMA1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-403 (ISOFORM 1).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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. The core SKA1 complex is composed of 2 SKA1-SKA2 heterodimers,
CC each heterodimer interacting with a molecule of the SKA3 homodimer. The
CC core SKA1 complex associates with microtubules and forms oligomeric
CC assemblies. Interacts with SKA1; the interaction is direct.
CC {ECO:0000250|UniProtKB:Q8IX90}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A8PUI7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8PUI7-2; Sequence=VSP_037279, VSP_037280;
CC -!- SIMILARITY: Belongs to the SKA3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC112513; AAI12514.1; -; mRNA.
DR EMBL; CK947368; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001103537.2; NM_001110067.2. [A8PUI7-1]
DR AlphaFoldDB; A8PUI7; -.
DR SMR; A8PUI7; -.
DR STRING; 9913.ENSBTAP00000004289; -.
DR PaxDb; A8PUI7; -.
DR PRIDE; A8PUI7; -.
DR Ensembl; ENSBTAT00000004289; ENSBTAP00000004289; ENSBTAG00000003314. [A8PUI7-1]
DR GeneID; 509921; -.
DR KEGG; bta:509921; -.
DR CTD; 221150; -.
DR VEuPathDB; HostDB:ENSBTAG00000003314; -.
DR eggNOG; ENOG502QSTX; Eukaryota.
DR GeneTree; ENSGT00500000045005; -.
DR HOGENOM; CLU_033334_1_0_1; -.
DR InParanoid; A8PUI7; -.
DR OMA; ERYMIPQ; -.
DR OrthoDB; 1070468at2759; -.
DR TreeFam; TF332721; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000003314; Expressed in spermatid and 103 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..403
FT /note="Spindle and kinetochore-associated protein 3"
FT /id="PRO_0000373897"
FT REGION 107..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT VAR_SEQ 244..245
FT /note="SE -> RN (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037279"
FT VAR_SEQ 246..403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037280"
SQ SEQUENCE 403 AA; 44762 MW; FE3FF86B2B105EBE CRC64;
MDPIRGFCGK LRSLAVTLDS ETARLQRALD GEDSDFEDCP MRVLHDLNSE VRILKDDVNI
LLDKANLESQ ENIGFIKATK ILMRKNSMDI MKIKEFFQKY GYTPRAKKNS VDEQEVTDSK
PESSECERPE KPDLKDDLLD SAAASTSVSE KSPRSPQLSD FGLERYIVSQ VLPNPPQAVN
NQKEEPKILT PFSKHSLLKT PKCALKMDDF ECVTPKLEHF GISEYTMCLN DDYTIGLKNV
KTNSETIETE PVPNDNVFAT PGLITQPLGK NNAEHTHSPL APTFCTPGLK VPSTKTSTAM
VSTNSSSNDL ETKESTSLVS NSDECFENFA DPSSPTISSY ENLLKTPTPP EVTTIPEDIR
QILSKYNSNL ASPVAVRAVS PINVFLPRHG GQNMRDASNK ENW