CE120_BOVIN
ID CE120_BOVIN Reviewed; 987 AA.
AC A0JN62;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Centrosomal protein of 120 kDa;
DE Short=Cep120;
DE AltName: Full=Coiled-coil domain-containing protein 100;
GN Name=CEP120; Synonyms=CCDC100;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the microtubule-dependent coupling of the
CC nucleus and the centrosome. Involved in the processes that regulate
CC centrosome-mediated interkinetic nuclear migration (INM) of neural
CC progenitors and for proper positioning of neurons during brain
CC development. Also implicated in the migration and selfrenewal of neural
CC progenitors. May play a role in centriole duplication during mitosis
CC (By similarity). Required for the recruitment of CEP295 to the proximal
CC end of new-born centrioles at the centriolar microtubule wall during
CC early S phase in a PLK4-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q7TSG1, ECO:0000250|UniProtKB:Q8N960}.
CC -!- SUBUNIT: Interacts with TACC2 and TACC3. Interacts with CCDC52.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Note=Regulates the localization of
CC TACC3 to the centrosome in neural progenitors in vivo. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0JN62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0JN62-2; Sequence=VSP_035122;
CC -!- SIMILARITY: Belongs to the CEP120 family. {ECO:0000305}.
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DR EMBL; AAFC03099167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03125893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03125142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03099169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03131164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03126660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126531; AAI26532.1; -; mRNA.
DR RefSeq; NP_001071468.1; NM_001078000.2. [A0JN62-2]
DR RefSeq; XP_005209165.1; XM_005209108.3. [A0JN62-1]
DR RefSeq; XP_005209166.1; XM_005209109.3.
DR RefSeq; XP_010805402.1; XM_010807100.2.
DR RefSeq; XP_010805403.1; XM_010807101.2.
DR AlphaFoldDB; A0JN62; -.
DR SMR; A0JN62; -.
DR STRING; 9913.ENSBTAP00000041320; -.
DR PaxDb; A0JN62; -.
DR PRIDE; A0JN62; -.
DR Ensembl; ENSBTAT00000017545; ENSBTAP00000017545; ENSBTAG00000013184. [A0JN62-2]
DR Ensembl; ENSBTAT00000043775; ENSBTAP00000041320; ENSBTAG00000013184. [A0JN62-1]
DR GeneID; 534400; -.
DR KEGG; bta:534400; -.
DR CTD; 153241; -.
DR VEuPathDB; HostDB:ENSBTAG00000013184; -.
DR eggNOG; ENOG502QPT0; Eukaryota.
DR GeneTree; ENSGT00390000009378; -.
DR HOGENOM; CLU_012372_0_0_1; -.
DR InParanoid; A0JN62; -.
DR OMA; DELETWK; -.
DR OrthoDB; 277001at2759; -.
DR TreeFam; TF329430; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000013184; Expressed in spermatid and 108 other tissues.
DR ExpressionAtlas; A0JN62; baseline and differential.
DR GO; GO:0005814; C:centriole; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0030953; P:astral microtubule organization; IEA:Ensembl.
DR GO; GO:0007098; P:centrosome cycle; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0022027; P:interkinetic nuclear migration; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:1903724; P:positive regulation of centriole elongation; ISS:UniProtKB.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:Ensembl.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IEA:Ensembl.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039893; CEP120-like.
DR InterPro; IPR022136; DUF3668.
DR PANTHER; PTHR21574; PTHR21574; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF12416; DUF3668; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..987
FT /note="Centrosomal protein of 120 kDa"
FT /id="PRO_0000348261"
FT DOMAIN 1..112
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 438..567
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 352..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 670..919
FT /evidence="ECO:0000255"
FT COMPBIAS 352..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TSG1"
FT VAR_SEQ 621..671
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_035122"
SQ SEQUENCE 987 AA; 112913 MW; 4723C6D958F13E8B CRC64;
MVSKSDQLLI VVSILEGRHF PKRPKHMLIV EAKFDGEQLA TDPVDHTDQP EFATELAWEI
DRKALHQHRL QRTPIKLQCF ALDPSTSARE TIGYIVLDLR TAQETKQAPK WYQLLSNKYT
KFKSEIQISI ALETDTKAPV DSFKAKGAPP RDGKVPASLS GLDPKDIVAV LNEEGGYHQI
GPAGYCTDFF IMSVTIAFAT QLEQLIPCTM KLPERQPEFF FYYSLLGNDV TNEPFSDLIN
PNFEPERASV RIRSSIEILR VYLTLHSKLQ IHLCCGDQSL GSTEIPLTGL LKKGSTEINH
RPVTVEGAFT LDPPNRAKQK LAPIPVELAP TVGVSVALQR EGMDVQSLIE LKTQNEHEPH
HSKKRVLTPI KENTHTGPQS PSESPVPPHN QSPPTKDDAT ESEVESLLYD KDTKLNPKAI
SSSVPALLAK PVTTSIASEA ASGQKIAVPA TSHHFCFSID LRSIHDLEVG FPINCILRYS
YPFFGSAAPI MTNPPVEVRK NMEVFLPQSY CAFDFATLPH QLQDTFLRIP LLVELWHKDK
MSKDLLLGIA RIQLSNILSS EKTRFLGSNG EQCWRQTFSE SVPIVATQGS NNRIVDLSYT
VTLEDYGLVK MREIFVSDSS QGLSAVQQKP SSVPPAPCPS EIQTEPRETL EYKAALELEM
WKEMQEDIFE NQLKQKELAH MQALAEEWKK RDRERESLVK KKVAEYNILE GKLQKTLIDL
EKREQQLAIA ESELQRERRE LKSERERNLQ ELQDSIRRAK EDCVHQVELE RLKMKQLEED
KHRLQQQLND AENKYKTLEK EFHQFKDQQS SKPEIRLQSE INLLTLEKVE LERKLESATK
SKLHYKQQWG RALKELARLK QREQESQMAR LKKQQEELEQ MRLRYLAAEE KDTVKTERQE
LLDIRNELNR LRQQEQKQYP DSREIASGKM DGPHGSALEE GLDDYLTRLI EERDTLMRTG
VYNHEDRIIS ELDRQIREVL AKNNASN
