ID   PPR35_BOVIN             Reviewed;         266 AA.
AC   A6QPM6; F1MCE9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 35 {ECO:0000305};
GN   Name=PPP1R35 {ECO:0000250|UniProtKB:Q8TAP8};
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=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: During centriole duplication, plays a role in the centriole
CC       elongation by promoting the recruitment of the microtubule-binding
CC       elongation machinery through its interaction with RTTN, leading to the
CC       centriole to centrosome conversion (By similarity). In addition may
CC       play a role in the primary cilia assembly (By similarity).
CC       {ECO:0000250|UniProtKB:Q8TAP8, ECO:0000250|UniProtKB:Q9D8C8}.
CC   -!- SUBUNIT: Interacts with PPP1CA; this interaction mediates the PPP1CA
CC       phosphatase activity inhibition. Interacts with RTTN; this interaction
CC       allows the mutual recruitment to the centriole.
CC       {ECO:0000250|UniProtKB:Q8TAP8}.
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. Co-localizes with RTTN at
CC       the centriole. {ECO:0000250|UniProtKB:Q8TAP8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A6QPM6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A6QPM6-2; Sequence=VSP_042174;
CC   -!- SIMILARITY: Belongs to the PPP1R35 family. {ECO:0000305}.
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DR   EMBL; DAAA02058281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC149391; AAI49392.1; -; mRNA.
DR   RefSeq; NP_001095785.2; NM_001102315.2. [A6QPM6-1]
DR   AlphaFoldDB; A6QPM6; -.
DR   STRING; 9913.ENSBTAP00000012252; -.
DR   PaxDb; A6QPM6; -.
DR   PRIDE; A6QPM6; -.
DR   GeneID; 617968; -.
DR   KEGG; bta:617968; -.
DR   CTD; 221908; -.
DR   eggNOG; ENOG502S5MS; Eukaryota.
DR   HOGENOM; CLU_096528_0_0_1; -.
DR   InParanoid; A6QPM6; -.
DR   OrthoDB; 1390072at2759; -.
DR   TreeFam; TF337101; -.
DR   Proteomes; UP000009136; 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   Alternative splicing; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Protein phosphatase inhibitor; Reference proteome.
FT   CHAIN           1..266
FT                   /note="Protein phosphatase 1 regulatory subunit 35"
FT                   /id="PRO_0000358928"
FT   REGION          1..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..37
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAP8"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAP8"
FT   VAR_SEQ         165..266
FT                   /note="LNVPRSKRLFRDLVSLQVPEEQVLNAALREKLALLPPQARAPPPKEPPGPGP
FT                   DMTILCDPETLFYESPHLTLEGLPPLRLQLRPRPSEDTFLMHRTLRRWEA -> EGGRR
FT                   PAGRGSGGARRRSPPPLMRSQG (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_042174"
FT   CONFLICT        93
FT                   /note="G -> E (in Ref. 2; AAI49392)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   266 AA;  28726 MW;  2741227D3142B1B8 CRC64;
     MMVYNGSQLE SVEEGEAVAV PGPPPEPRAP EPGAPVPEPG LDLSLSPRSE SPGRGRPNCS
     PGRRKGRADR RGGARKGRQV RFLLAPPSPV RSGPPPAAAS SSEKPEAPQD LGTPVQQSSL
     ALSLELQAAR AAAGGQFDAA KAVEEQLRKS FQTRCGLEES VTEGLNVPRS KRLFRDLVSL
     QVPEEQVLNA ALREKLALLP PQARAPPPKE PPGPGPDMTI LCDPETLFYE SPHLTLEGLP
     PLRLQLRPRP SEDTFLMHRT LRRWEA