ID   SPICE_RAT               Reviewed;         868 AA.
AC   Q5RKG1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Spindle and centriole-associated protein 1;
DE   AltName: Full=Coiled-coil domain-containing protein 52;
GN   Name=Spice1; Synonyms=Ccdc52;
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=Testis;
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773 AND SER-776, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Regulator required for centriole duplication, for proper
CC       bipolar spindle formation and chromosome congression in mitosis.
CC       {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}.
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; BC085954; AAH85954.1; -; mRNA.
DR   RefSeq; NP_001008286.1; NM_001008285.1.
DR   RefSeq; XP_006248394.1; XM_006248332.3.
DR   RefSeq; XP_017453413.1; XM_017597924.1.
DR   AlphaFoldDB; Q5RKG1; -.
DR   SMR; Q5RKG1; -.
DR   STRING; 10116.ENSRNOP00000061013; -.
DR   iPTMnet; Q5RKG1; -.
DR   PhosphoSitePlus; Q5RKG1; -.
DR   PaxDb; Q5RKG1; -.
DR   PRIDE; Q5RKG1; -.
DR   Ensembl; ENSRNOT00000064385; ENSRNOP00000061013; ENSRNOG00000039024.
DR   GeneID; 288111; -.
DR   KEGG; rno:288111; -.
DR   UCSC; RGD:1310729; rat.
DR   CTD; 152185; -.
DR   RGD; 1310729; Spice1.
DR   eggNOG; ENOG502QQ0H; Eukaryota.
DR   GeneTree; ENSGT00390000006207; -.
DR   HOGENOM; CLU_016571_0_0_1; -.
DR   InParanoid; Q5RKG1; -.
DR   OMA; RHEMHKS; -.
DR   OrthoDB; 351032at2759; -.
DR   PhylomeDB; Q5RKG1; -.
DR   TreeFam; TF333301; -.
DR   PRO; PR:Q5RKG1; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000039024; Expressed in testis and 19 other tissues.
DR   ExpressionAtlas; Q5RKG1; baseline and differential.
DR   Genevisible; Q5RKG1; RN.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
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:0051310; P:metaphase plate congression; ISO:RGD.
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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Mitosis;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..868
FT                   /note="Spindle and centriole-associated protein 1"
FT                   /id="PRO_0000282416"
FT   REGION          129..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          381..434
FT                   /evidence="ECO:0000255"
FT   COILED          736..764
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        135..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..850
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         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C804"
FT   MOD_RES         655
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT   MOD_RES         772
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT   MOD_RES         773
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         776
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         831
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C804"
SQ   SEQUENCE   868 AA;  96322 MW;  4F9FA73B406E3B4A CRC64;
     MSLIRVNRFG PRGGARKTLK VKKKAAVRQE WDNTVNDLTV HRATPEDLVR RHEMHKSKNR
     ALVHWELQEK ALKRKWKKQK PETSSIEKRK LSIMKEILSD QYQTQDVLEK SDHLLTAAKG
     LFVDVPRKRT GFPNVTMAPG SSRSPAGINQ DPGTQSILNE SIIEPQALNE VDDGGAESTA
     HSQSEDSESE LPNSLSPHSN RNTERFLHQL KEENSELINQ LWTDIQQKIA AQSQRTPPGS
     PSSELSAEDQ KGALNATDAV KRIQAGLQPE ESAEPVDSSY VGQVLNTRKP KPLLSKVKRK
     QDMRALSKQK KNMLSSSTTS ADLASSNNSS LDVLKHMIHE VEHEMEEYER WTGREVKGLQ
     GGQGLTGFTL SLVSSLCRLV RYLKESETQL RKEVETRQQL EQMLGDHREL IDALTAEILL
     LREENGAVQA RLQQYMVTTD EQLISLTHAI KSCPVINNSR QESQAPERAA MGRRLVDNVG
     APVVNSNVSM PLMLKGEEMV DFPQEELPVK LSQGPPPTEN LNLASNFPTH IFEPAVMLTP
     PRQKSNSEFS PLQDVLRRTV QTRPAPRIPP TVEVIEKEQT WEKKNLPIDP DIQNSSEESR
     LFTQRWRVSH MGDDLENKSQ PQFVSLSQPP QFVSLSQPPC SSPPSTQQSR NPVFSEEPTV
     LGDGQQLGTA DALMHRKDIM ARIAELTLQN SAMKAHLNNI TSSGGEHGDG LREPSRQGNA
     SEVPANFPAV QSLMPSSMEE RIAELNRQSM EARSKLLQLI EQQKLVGLTL SSSPVSPVES
     PLRAWTEEGK RTIEVSVPGV EASESSKCNT VSPVSGVSSR RSSGAISNSC SPLNATSGSG
     KFTPVNPRTK QTEKQSEEGW FALSAHLP