SKA3_RAT
ID SKA3_RAT Reviewed; 419 AA.
AC B2GUZ2;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Spindle and kinetochore-associated protein 3;
GN Name=Ska3; Synonyms=Rama1;
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=Lung;
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: 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 -!- SIMILARITY: Belongs to the SKA3 family. {ECO:0000305}.
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DR EMBL; BC166461; AAI66461.1; -; mRNA.
DR RefSeq; XP_006252136.1; XM_006252074.1.
DR RefSeq; XP_006252137.1; XM_006252075.1.
DR AlphaFoldDB; B2GUZ2; -.
DR SMR; B2GUZ2; -.
DR STRING; 10116.ENSRNOP00000033626; -.
DR PaxDb; B2GUZ2; -.
DR PRIDE; B2GUZ2; -.
DR GeneID; 361047; -.
DR UCSC; RGD:1307201; rat.
DR CTD; 221150; -.
DR RGD; 1307201; Ska3.
DR VEuPathDB; HostDB:ENSRNOG00000021847; -.
DR eggNOG; ENOG502QSTX; Eukaryota.
DR HOGENOM; CLU_033334_1_0_1; -.
DR InParanoid; B2GUZ2; -.
DR OMA; ERYMIPQ; -.
DR OrthoDB; 1070468at2759; -.
DR PhylomeDB; B2GUZ2; -.
DR TreeFam; TF332721; -.
DR PRO; PR:B2GUZ2; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000021847; Expressed in thymus and 18 other tissues.
DR Genevisible; B2GUZ2; RN.
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 Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Kinetochore; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..419
FT /note="Spindle and kinetochore-associated protein 3"
FT /id="PRO_0000350565"
FT REGION 112..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IX90"
SQ SEQUENCE 419 AA; 46352 MW; E88F4DA252CF69A7 CRC64;
MNPIQSFHCK LRSLATVLDG ETARLLRALD GEDSEDFEDS SARILCDLYS EVQTLKDDVN
AHLDKARLES RESTHFIKAA KVLMKKNSAD IIKLREFFQK YGYQARDKED SACEHRVSNS
SPGLAVCKDT QEPGVKQELS EPRVPRGSAP EEPLRSPQLS DFGLQRYMVS QGPANPRQET
VSLKEDRASE TTPAKDPSVQ VLKTPRCALK MDDFECVTPK LEHFGISEYT MCLNEDYTMG
LKNMKSIKSS PLSGVGGEAV ETGPVTSDNS FAIPGPMIQQ LEKNDVEYIN SPLPPKFCTP
GLKIPSSMDS TDLVSIDYPL SKPNSSPTDL EDKDCAPLIL NSDECYQSFA DPHSPTITSY
ENFTTPSPPK VTAIPEDILQ MLKYNSNLAS PIDVKAMPLR RGFTSKGQST RGAANKENW
