SPICE_BOVIN
ID SPICE_BOVIN Reviewed; 860 AA.
AC Q2T9X8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Spindle and centriole-associated protein 1;
DE AltName: Full=Coiled-coil domain-containing protein 52;
GN Name=SPICE1; Synonyms=CCDC52;
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].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator required for centriole duplication. for proper
CC bipolar spindle formation and chromosome congression in mitosis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CEP120. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}.
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DR EMBL; BC111217; AAI11218.1; -; mRNA.
DR RefSeq; NP_001033206.1; NM_001038117.2.
DR AlphaFoldDB; Q2T9X8; -.
DR SMR; Q2T9X8; -.
DR STRING; 9913.ENSBTAP00000049245; -.
DR PaxDb; Q2T9X8; -.
DR PRIDE; Q2T9X8; -.
DR GeneID; 515350; -.
DR KEGG; bta:515350; -.
DR CTD; 152185; -.
DR eggNOG; ENOG502QQ0H; Eukaryota.
DR InParanoid; Q2T9X8; -.
DR OrthoDB; 351032at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
DR InterPro; IPR031387; SPICE1.
DR PANTHER; PTHR31167; PTHR31167; 1.
DR Pfam; PF15678; SPICE; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..860
FT /note="Spindle and centriole-associated protein 1"
FT /id="PRO_0000282412"
FT REGION 160..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 383..437
FT /evidence="ECO:0000255"
FT COILED 729..755
FT /evidence="ECO:0000255"
FT COMPBIAS 167..181
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C804"
SQ SEQUENCE 860 AA; 95713 MW; 7AD87FE7C8D6A9FD CRC64;
MSFVRVNRYG PRGGGRKTLK VKKKTSVKQE WDNTVTDLTV HRATPEDLIR RHEIHKSKNR
ALVHWELQEK ALKRRWKKQK PEISNLEKRR LSIMKEILSD QYQLQDVLEK SDHLMATAKG
LFVDFPRRRT GFPNVTMAPE SSQSPTVVSK DPVTQAIRSE SVIEPQALNE VDDDEQEGTV
NSQSEESENE LDNSLSSQSN ANAGTFLHQI KEENSELINK LWTDIQQKVA TQSQMTASSG
TPSSASPSGE QKAALNATNA VKRIHTRLQP EESTETLDSS YVVGQVLNSR KQKQLLNKVK
RKPDSRAPSK QKSSMLSAST ASTDLPSSSN PSLDVLKHMI HEVEHEIEEY ERWTGREVQG
LQNSQGLTGF TLSLVSSLCR LVRYLKESEL QLRKEVETRQ RLEEALGDHR ELIDALTAEV
LFLREENTAT QARLQQYMIT TDEQLISLTH AIKNCPVISN KESQALERGA TSQRHIDNPE
DPAVNASVSM PLMFRGEDVV EFPQEDLPVK LSQVPNPPES GDLASSLPGH IFEPAVLLTP
PRQKSNSEFS PLQDVLRRTV QTRPAPRIPP TVEIIEKEQN WEKKTLPVGA DIQNSSDESH
LFTQRWRASH MGEDSQSKTQ APFVSLSQPL CSSQSSMQQS RNPTLSEEPL VLGDGQQLRT
NETLIQRKDI MARIAELTLQ NSDIRAHLNN IIGPGGEQGD GLREFNRQET SHASDTMATF
PAVQPLTPSS MEERIAELNR QSMEARGKLL QLIEQQKLLG LNPSSPPVSP VQSPLRAWAE
GGKRTIEVSI PGAEAPESSK CSTDSPTSGL NSRRSSGAAS NSCSPLNATS GSGRLTPLNP
RAKIEKQNEE GWFALSTHVS