PPR42_MOUSE
ID PPR42_MOUSE Reviewed; 357 AA.
AC Q8R1Z4; Q9D5M1; Q9DAF9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 42;
DE AltName: Full=Leucine-rich repeat-containing protein 67;
DE AltName: Full=Testis leucine-rich repeat protein;
DE Short=TLRR;
GN Name=Ppp1r42; Synonyms=Lrrc67;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH KIFC1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18237440; DOI=10.1186/1471-2121-9-9;
RA Wang R., Sperry A.O.;
RT "Identification of a novel Leucine-rich repeat protein and candidate PP1
RT regulatory subunit expressed in developing spermatids.";
RL BMC Cell Biol. 9:9-9(2008).
RN [4]
RP INTERACTION WITH ACTIN; DYNEIN; PPP1CC; KIF5B AND TUBULIN, ASSOCIATION WITH
RP MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=19886865; DOI=10.1042/bc20090091;
RA Wang R., Kaul A., Sperry A.O.;
RT "TLRR (lrrc67) interacts with PP1 and is associated with a cytoskeletal
RT complex in the testis.";
RL Biol. Cell 102:173-189(2010).
RN [5]
RP FUNCTION, INTERACTION WITH PPP1CC, AND PHOSPHORYLATION.
RX PubMed=21738792; DOI=10.1371/journal.pone.0021767;
RA Wang R., Sperry A.O.;
RT "PP1 forms an active complex with TLRR (lrrc67), a putative PP1 regulatory
RT subunit, during the early stages of spermiogenesis in mice.";
RL PLoS ONE 6:E21767-E21767(2011).
CC -!- FUNCTION: Regulates phosphatase activity of protein phosphatase 1 (PP1)
CC complexes in the testis. {ECO:0000269|PubMed:21738792}.
CC -!- SUBUNIT: Interacts with PPP1CC isoform gamma-2; the interaction is
CC direct. Interacts with actin, dynein, KIF5B, KIFC1 and tubulin.
CC Associates with microtubules. {ECO:0000269|PubMed:18237440,
CC ECO:0000269|PubMed:19886865, ECO:0000269|PubMed:21738792}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Note=Colocalizes with alpha
CC tubulin to the manchette of developing spermatids. Detected to nuclear
CC rim in pachytene spermatocytes. Detected at nuclear surface, opposite
CC the acrosome in elongating spermatids. Detected at the
CC microtubule- organizing center (MTOC). Localized to the centrosomal
CC region of late-stage spermatids.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8R1Z4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R1Z4-2; Sequence=VSP_032590, VSP_032591;
CC Name=3;
CC IsoId=Q8R1Z4-3; Sequence=VSP_032589;
CC -!- TISSUE SPECIFICITY: Testis-specific. Expressed in spermatids (at
CC protein level). Testis-specific. {ECO:0000269|PubMed:18237440}.
CC -!- PTM: Phosphorylated; during the first round of spermatogenesis with a
CC marginal increase at 21 days after birth.
CC {ECO:0000269|PubMed:21738792}.
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DR EMBL; AK005871; BAB24290.1; -; mRNA.
DR EMBL; AK015164; BAB29732.1; -; mRNA.
DR EMBL; AK076637; BAC36427.1; -; mRNA.
DR EMBL; BC022722; AAH22722.1; -; mRNA.
DR CCDS; CCDS14817.1; -. [Q8R1Z4-1]
DR RefSeq; NP_663730.1; NM_145692.2. [Q8R1Z4-1]
DR AlphaFoldDB; Q8R1Z4; -.
DR SMR; Q8R1Z4; -.
DR IntAct; Q8R1Z4; 3.
DR MINT; Q8R1Z4; -.
DR STRING; 10090.ENSMUSP00000027049; -.
DR iPTMnet; Q8R1Z4; -.
DR PhosphoSitePlus; Q8R1Z4; -.
DR PaxDb; Q8R1Z4; -.
DR PRIDE; Q8R1Z4; -.
DR ProteomicsDB; 291729; -. [Q8R1Z4-1]
DR ProteomicsDB; 291730; -. [Q8R1Z4-2]
DR ProteomicsDB; 291731; -. [Q8R1Z4-3]
DR Antibodypedia; 12079; 93 antibodies from 19 providers.
DR DNASU; 69312; -.
DR Ensembl; ENSMUST00000027049; ENSMUSP00000027049; ENSMUSG00000025916. [Q8R1Z4-1]
DR Ensembl; ENSMUST00000130102; ENSMUSP00000115030; ENSMUSG00000025916. [Q8R1Z4-3]
DR GeneID; 69312; -.
DR KEGG; mmu:69312; -.
DR UCSC; uc007ahb.2; mouse. [Q8R1Z4-1]
DR UCSC; uc007ahd.2; mouse. [Q8R1Z4-2]
DR CTD; 286187; -.
DR MGI; MGI:1921138; Ppp1r42.
DR VEuPathDB; HostDB:ENSMUSG00000025916; -.
DR eggNOG; KOG2769; Eukaryota.
DR GeneTree; ENSGT00940000158260; -.
DR HOGENOM; CLU_149705_0_0_1; -.
DR InParanoid; Q8R1Z4; -.
DR OMA; IGDISLC; -.
DR OrthoDB; 1267922at2759; -.
DR PhylomeDB; Q8R1Z4; -.
DR TreeFam; TF329227; -.
DR BioGRID-ORCS; 69312; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ppp1r42; mouse.
DR PRO; PR:Q8R1Z4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8R1Z4; protein.
DR Bgee; ENSMUSG00000025916; Expressed in spermatid and 45 other tissues.
DR ExpressionAtlas; Q8R1Z4; baseline and differential.
DR Genevisible; Q8R1Z4; MM.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0002177; C:manchette; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0010921; P:regulation of phosphatase activity; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12799; LRR_4; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW Reference proteome; Repeat.
FT CHAIN 1..357
FT /note="Protein phosphatase 1 regulatory subunit 42"
FT /id="PRO_0000326177"
FT REPEAT 29..50
FT /note="LRR 1"
FT REPEAT 51..72
FT /note="LRR 2"
FT REPEAT 73..94
FT /note="LRR 3"
FT REPEAT 95..116
FT /note="LRR 4"
FT REPEAT 117..138
FT /note="LRR 5"
FT REPEAT 147..168
FT /note="LRR 6"
FT REPEAT 169..190
FT /note="LRR 7"
FT DOMAIN 204..242
FT /note="LRRCT"
FT REGION 329..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 146..357
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032589"
FT VAR_SEQ 185..186
FT /note="DL -> VT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032590"
FT VAR_SEQ 187..357
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032591"
SQ SEQUENCE 357 AA; 41151 MW; 46C5A57D53A604E1 CRC64;
MVRLTVDLIA KNSNLKPRKE ETLAQCLKKI THINFSDRNI DSIDDLSLCR NLSVLYLYDN
RISQVTNLNY TTNLTHLYLQ NNCISCIENL SSLKKLEKLY LGGNYIAVIE GLEGLEELRE
LHVESQRLPL GEKLLFDPRT LRSLAKSLST LNISNNNIDD IKDLEILENL NHLIAVDNQL
MHVKDLELLL KKLMKLWKMD LNGNPVCLKP KYRDKLILTS KSLEFLDGKE IKDMERQFLM
NWKASKDAKK ISKKRRSRSE DASNSYISNF ETVHHIVPVY YPQVGKPKVI FFSDVQRYLV
HGNASSKCSQ EDKTTITEDI GNLSLKESES SLTKNDIHEP HLLQNPKVKE NLSEKKE
