CEP19_BOVIN
ID CEP19_BOVIN Reviewed; 163 AA.
AC A6H7C9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Centrosomal protein of 19 kDa;
DE Short=Cep19;
GN Name=CEP19;
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=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for ciliation. Recruits the RABL2B GTPase to the
CC ciliary base to initiate ciliation. After specifically capturing the
CC activated GTP-bound RABL2B, the CEP19-RABL2B complex binds
CC intraflagellar transport (IFT) complex B from the large pool pre-docked
CC at the base of the cilium and thus triggers its entry into the cilia.
CC Involved in the early steps in cilia formation by recruiting the
CC ciliary vesicles (CVs) to the distal end of the mother centriole where
CC they fuse to initiate cilium assembly. Involved in microtubule (MT)
CC anchoring at centrosomes. {ECO:0000250|UniProtKB:Q96LK0}.
CC -!- SUBUNIT: Interacts with CEP43; this interaction is required for its
CC localization to the mother centriole. Interacts (via residues 121-150)
CC with RABL2B. Interacts (via C-terminus) with CEP350; this interaction
CC is required for its localization to the mother centriole.
CC {ECO:0000250|UniProtKB:Q96LK0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q96LK0}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q96LK0}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q96LK0}. Note=Associates with the mother
CC centriole in early interphase. Localizes to spindle poles during
CC mitosis, and to distinct foci oriented towards the midbody at
CC telophase. Localizes slightly apical to the subdistal appendage on the
CC mother centriole, but below the distal appendage.
CC {ECO:0000250|UniProtKB:Q96LK0}.
CC -!- SIMILARITY: Belongs to the CEP19 family. {ECO:0000305}.
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DR EMBL; BC146199; AAI46200.1; -; mRNA.
DR RefSeq; NP_001092599.1; NM_001099129.1.
DR RefSeq; XP_005201596.1; XM_005201539.3.
DR RefSeq; XP_005201597.1; XM_005201540.3.
DR AlphaFoldDB; A6H7C9; -.
DR STRING; 9913.ENSBTAP00000017558; -.
DR PaxDb; A6H7C9; -.
DR PRIDE; A6H7C9; -.
DR Ensembl; ENSBTAT00000017558; ENSBTAP00000017558; ENSBTAG00000013192.
DR GeneID; 613916; -.
DR KEGG; bta:613916; -.
DR CTD; 84984; -.
DR VEuPathDB; HostDB:ENSBTAG00000013192; -.
DR VGNC; VGNC:27198; CEP19.
DR eggNOG; ENOG502RZP1; Eukaryota.
DR GeneTree; ENSGT00390000016356; -.
DR HOGENOM; CLU_113348_0_0_1; -.
DR InParanoid; A6H7C9; -.
DR OMA; QEKCSWD; -.
DR OrthoDB; 1594443at2759; -.
DR TreeFam; TF328425; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000013192; Expressed in occipital lobe and 103 other tissues.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; ISS:UniProtKB.
DR GO; GO:0097712; P:vesicle targeting, trans-Golgi to periciliary membrane compartment; ISS:UniProtKB.
DR InterPro; IPR029412; CEP19.
DR PANTHER; PTHR31539; PTHR31539; 2.
DR Pfam; PF14933; CEP19; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Reference proteome.
FT CHAIN 1..163
FT /note="Centrosomal protein of 19 kDa"
FT /id="PRO_0000360405"
SQ SEQUENCE 163 AA; 19189 MW; F12BA1DA7380BDC9 CRC64;
MMCTAKKCGI RFQPPAIILI YENEIKGKSR QRIMPVRNFS KYSDCSRAAE QLKNNPRHKG
YLEQVSLKQL EKLFSFLRGN LWGQSLAETM EQIQRETTID PEEDLNKLDD KELAKRKSIM
DELFEKNQKK KDDPNFVYDI EVEFPQDEQL QSCGWDTESA EEF