POC5_XENLA
ID POC5_XENLA Reviewed; 572 AA.
AC Q6DFB7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Centrosomal protein POC5;
DE AltName: Full=Protein of centriole 5;
GN Name=poc5;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for the assembly of the distal half of centrioles,
CC required for centriole elongation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Note=Localized to the
CC distal portion of centrioles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the POC5 family. {ECO:0000305}.
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DR EMBL; BC076822; AAH76822.1; -; mRNA.
DR RefSeq; NP_001086572.1; NM_001093103.1.
DR AlphaFoldDB; Q6DFB7; -.
DR SMR; Q6DFB7; -.
DR DNASU; 446407; -.
DR GeneID; 446407; -.
DR KEGG; xla:446407; -.
DR CTD; 446407; -.
DR Xenbase; XB-GENE-5850643; poc5.L.
DR OrthoDB; 1217267at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 446407; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR033351; POC5.
DR PANTHER; PTHR28618; PTHR28618; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome;
KW Repeat.
FT CHAIN 1..572
FT /note="Centrosomal protein POC5"
FT /id="PRO_0000281912"
FT REPEAT 143..174
FT /note="Centrin-binding (CBR) 1"
FT REPEAT 232..263
FT /note="Centrin-binding (CBR) 2"
FT REPEAT 264..296
FT /note="Centrin-binding (CBR) 3"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..251
FT /evidence="ECO:0000255"
FT COILED 317..353
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 63872 MW; 78FA4020E67059C8 CRC64;
MSSDEEYRES PILPKDSDHG SSVSSDLQDE YDELLRYAVV TPRFGPHFPE QNQLFTEQIK
SDRFSSPKDP VQEQSLARNY SEENIPECSA TSTSQRRSPP TANEEERAMS EKKSFLSGLE
AFSPLHSEDL SLGGSTSSGS QVQQVRVKEL PVPAENMDKV EDVLDLWSGT LKTNVMAELS
KWRLTVIEQH KLEIKNQNEK HAEQISQLSS QIDKLQDHLQ TYETSIQRKD EVISNLTHAL
EKHKEKMELM RTFTHWRLQL TEAREEDYAR SLADRHYRNT LMKNAWKAWH SVIQSNWKDK
IEQACRARAE EVCIELSNDY ESKLTQLNSA LGEARAEVQR LLAERGQFEG SMKKAFMRGV
CALNMEAMSM FQGRESRMEY DPPPRREERD PSPSVTFQNP PVTSTHTSST QHELQSALHS
PVTCEPNYIH AFGPSTVSQS KEEAGAPAVI SAATSASSVL STQKLPMPRV VTSCQQKAGK
IITARISARP DVSQRSSKIG SNITSMAVSP PISSIVVEKH HPVTQQTISQ AAAAKYPRSA
LQSANSVGGR STGQSGRVSQ SHAGIHSIKV VD