ID   CEP19_RAT               Reviewed;         163 AA.
AC   Q9QZX9;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Centrosomal protein of 19 kDa;
DE            Short=Cep19;
GN   Name=Cep19;
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   STRAIN=Wistar; TISSUE=Testis;
RA   Wang L.F., Miao S.Y., Yang J., Zhang X.D., Li M., Zhao M.;
RL   Submitted (APR-1999) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD53055.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF146738; AAD53055.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q9QZX9; -.
DR   SMR; Q9QZX9; -.
DR   STRING; 10116.ENSRNOP00000038182; -.
DR   PaxDb; Q9QZX9; -.
DR   UCSC; RGD:621352; rat.
DR   RGD; 621352; Cep19.
DR   eggNOG; ENOG502RZP1; Eukaryota.
DR   InParanoid; Q9QZX9; -.
DR   PhylomeDB; Q9QZX9; -.
DR   PRO; PR:Q9QZX9; -.
DR   Proteomes; UP000002494; Unplaced.
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:0005929; C:cilium; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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_0000251962"
SQ   SEQUENCE   163 AA;  19149 MW;  0AB7790CA421F0C8 CRC64;
     MKYIAKKCGV RFQPPAMILI YENEAEGKSR QRIMPVRNFS KFSDCTRAAE QLKNNPRHKS
     YLEQVSLKQL EKLFVFLRGS LQGQSLAETM EQIQRETTID PEEDLNKLDD KELAKRKSIM
     DELFEKNQKR KDDPSFVYDV EVEFPQDEQL QSCSWDTASV DEF