ID   SPICE_PONAB             Reviewed;         855 AA.
AC   Q5RBY6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Spindle and centriole-associated protein 1;
DE   AltName: Full=Coiled-coil domain-containing protein 52;
GN   Name=SPICE1; Synonyms=CCDC52;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CR858496; CAH90724.1; -; mRNA.
DR   RefSeq; NP_001125403.1; NM_001131931.1.
DR   AlphaFoldDB; Q5RBY6; -.
DR   SMR; Q5RBY6; -.
DR   STRING; 9601.ENSPPYP00000015139; -.
DR   GeneID; 100172308; -.
DR   KEGG; pon:100172308; -.
DR   CTD; 152185; -.
DR   eggNOG; ENOG502QQ0H; Eukaryota.
DR   InParanoid; Q5RBY6; -.
DR   Proteomes; UP000001595; 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..855
FT                   /note="Spindle and centriole-associated protein 1"
FT                   /id="PRO_0000282415"
FT   REGION          164..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          325..437
FT                   /evidence="ECO:0000255"
FT   COILED          725..751
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        173..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..831
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         235
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT   MOD_RES         644
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT   MOD_RES         760
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT   MOD_RES         764
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N0Z3"
FT   MOD_RES         819
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C804"
SQ   SEQUENCE   855 AA;  96235 MW;  CB498F8CD273AC16 CRC64;
     MSFVRVNRCG PRVGVRKTPK VKKKKTSVKQ EWDNTVTDLT VHRATPEDLV RRHEIHKSKN
     RALVHWELQE KALKRKWRKQ KPETLNLEKR RLSIMKEILS DQYQMQDVLE KSDHLIAAAK
     ELFPRRRTGF PNITVAPDSS QGPIVVNQDP ITQSIFNESV IEPQALNDVD GEEEGTVTSQ
     SGESENENEL DNSLNSQSNT NTDRFLQQLT EENSELISKL WTDIQQKIVT QSQITPPGTP
     SSALSSGEQR AALNATNAVN RFQTRLQPEE STETLDSSYV VGHVLNSRKQ KQLLNKVKRK
     PNLHALSKPK KNMLSGSTTS ADLPNRTNSN LDVLKHMIHE VEHEMEEYER WTGREVKGLQ
     SSQGLTGFTL SLVSSLCRLV RYLKESEIQL RKEVETRQQL EQVLGDHREL IDALTAEILR
     LREENAATQA RLRQYMVTTD EQLISLTHAI KNCPVINNRQ EIQASESGAT GTRVMDSPEG
     PVVNANVSVP LMFREEVAEF PQEQLPVKLS QVPDPPDKMN LAKNFPAHIF EPAVLLTPPR
     QKSNLKFSPL QDVLRRTVQT RPAPRLLPTV EIIEKEQNWE EKTLPIDTDS QNSSEENRLF
     TQRWRVSHMG EDLENKTQAP FVNLSQPLCS SHSNTQQSRS PTFSEELPVL GDGQQLRTNE
     SLIQRKDIMT RIADLTLQNS AIKAHMNNII DPRGEQGDGL RELNKQESAS DMTSTFPVAQ
     SLTPGSMEER IAELNRQSME ARGKLLQLIE QQKLVGLNLS PPMSPVQLPL RAWTEGAKRT
     IEVSIPGAEA PESSKCSTVS PVSEINTRRS SGATSNSCSP LNATSGSGRF TPLNPRAKIE
     KQNEEGWFAL STHVS