PPR35_DANRE
ID PPR35_DANRE Reviewed; 251 AA.
AC Q0P427;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 35 {ECO:0000250|UniProtKB:Q8TAP8};
GN Name=ppp1r35 {ECO:0000250|UniProtKB:Q8TAP8}; ORFNames=zgc:153512;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: During centriole duplication, may play a role in the
CC centriole elongation by promoting the recruitment of the microtubule-
CC binding elongation machinery, leading to the centriole to centrosome
CC conversion (By similarity). In addition may play a role in the primary
CC cilia assembly (By similarity). {ECO:0000250|UniProtKB:Q8TAP8,
CC ECO:0000250|UniProtKB:Q9D8C8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q8TAP8}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q8TAP8}. Note=Recruited to the nascent daughter
CC centriole early in the duplication cycle and localizes to the proximal
CC centriolar lumen just above the cartwheel.
CC {ECO:0000250|UniProtKB:Q8TAP8}.
CC -!- SIMILARITY: Belongs to the PPP1R35 family. {ECO:0000305}.
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DR EMBL; BC122312; AAI22313.1; -; mRNA.
DR RefSeq; NP_001038856.1; NM_001045391.1.
DR AlphaFoldDB; Q0P427; -.
DR SMR; Q0P427; -.
DR STRING; 7955.ENSDARP00000059871; -.
DR PaxDb; Q0P427; -.
DR GeneID; 751676; -.
DR KEGG; dre:751676; -.
DR CTD; 221908; -.
DR ZFIN; ZDB-GENE-060825-232; ppp1r35.
DR eggNOG; ENOG502S5MS; Eukaryota.
DR InParanoid; Q0P427; -.
DR OrthoDB; 1156029at2759; -.
DR PhylomeDB; Q0P427; -.
DR PRO; PR:Q0P427; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; IEA:InterPro.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IEA:InterPro.
DR GO; GO:0048570; P:notochord morphogenesis; ISS:UniProtKB.
DR GO; GO:1903724; P:positive regulation of centriole elongation; ISS:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
DR InterPro; IPR033590; PPP1R35.
DR InterPro; IPR029135; PPP1R35_C.
DR PANTHER; PTHR28625; PTHR28625; 1.
DR Pfam; PF15503; PPP1R35_C; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..251
FT /note="Protein phosphatase 1 regulatory subunit 35"
FT /id="PRO_0000358930"
FT REGION 58..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 28415 MW; 9B61A674DE192283 CRC64;
MEVCGEPLIR AAPEPLRDER IQTAELLCAD LDLSVSLTPE RPADRRRRQV RFNVDPVLIT
VNPEPRNNQP TARKPPNKDE HGVETDREQS RECDGQQTHE AELNTTLALR AELEEEAEQT
FDAEKAVREK LQSSTLTKNH VNSKAAEGLN FPRSQQLYRA LVSVSLSRDQ LISQALQDRP
ALAPPTASQN NKFSSPPPEG PDILQFYSPD KMLRETPLLP GDHIPLPRPR PVPRPAHTTF
HLHRLHKLWE S