PPR29_MOUSE
ID PPR29_MOUSE Reviewed; 823 AA.
AC Q68FM6; Q69Z72; Q8CCW8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 29;
DE AltName: Full=Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2;
DE AltName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 6;
DE AltName: Full=Leucine-rich repeat-containing protein 62;
DE Flags: Precursor;
GN Name=Elfn2; Synonyms=Kiaa1904, Lrrc62, Ppp1r29;
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].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 339-823.
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622; SER-671 AND SER-675, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1)
CC complexes. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1CA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AK031970; BAC27630.1; -; mRNA.
DR EMBL; BC079588; AAH79588.1; -; mRNA.
DR EMBL; BC094219; AAH94219.1; -; mRNA.
DR EMBL; AK173294; BAD32572.1; -; mRNA.
DR CCDS; CCDS27621.1; -.
DR RefSeq; NP_898964.2; NM_183141.2.
DR RefSeq; XP_006520741.1; XM_006520678.3.
DR RefSeq; XP_017172014.1; XM_017316525.1.
DR RefSeq; XP_017172015.1; XM_017316526.1.
DR RefSeq; XP_017172017.1; XM_017316528.1.
DR AlphaFoldDB; Q68FM6; -.
DR SMR; Q68FM6; -.
DR BioGRID; 228897; 2.
DR IntAct; Q68FM6; 1.
DR MINT; Q68FM6; -.
DR STRING; 10090.ENSMUSP00000085960; -.
DR GlyConnect; 2641; 5 N-Linked glycans (1 site).
DR GlyGen; Q68FM6; 7 sites, 5 N-linked glycans (1 site).
DR iPTMnet; Q68FM6; -.
DR PhosphoSitePlus; Q68FM6; -.
DR SwissPalm; Q68FM6; -.
DR MaxQB; Q68FM6; -.
DR PaxDb; Q68FM6; -.
DR PeptideAtlas; Q68FM6; -.
DR PRIDE; Q68FM6; -.
DR ProteomicsDB; 291727; -.
DR Antibodypedia; 274; 64 antibodies from 16 providers.
DR DNASU; 207393; -.
DR Ensembl; ENSMUST00000088592; ENSMUSP00000085960; ENSMUSG00000043460.
DR Ensembl; ENSMUST00000229441; ENSMUSP00000155111; ENSMUSG00000043460.
DR GeneID; 207393; -.
DR KEGG; mmu:207393; -.
DR UCSC; uc007wrf.1; mouse.
DR CTD; 114794; -.
DR MGI; MGI:3608416; Elfn2.
DR VEuPathDB; HostDB:ENSMUSG00000043460; -.
DR eggNOG; ENOG502QVFI; Eukaryota.
DR GeneTree; ENSGT00940000159737; -.
DR HOGENOM; CLU_018770_0_0_1; -.
DR InParanoid; Q68FM6; -.
DR OMA; NLMVCEL; -.
DR OrthoDB; 190870at2759; -.
DR PhylomeDB; Q68FM6; -.
DR TreeFam; TF332887; -.
DR BioGRID-ORCS; 207393; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Elfn2; mouse.
DR PRO; PR:Q68FM6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q68FM6; protein.
DR Bgee; ENSMUSG00000043460; Expressed in subiculum and 101 other tissues.
DR Genevisible; Q68FM6; MM.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..823
FT /note="Protein phosphatase 1 regulatory subunit 29"
FT /id="PRO_0000256139"
FT TOPO_DOM 23..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..823
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 56..77
FT /note="LRR 1"
FT REPEAT 80..101
FT /note="LRR 2"
FT REPEAT 104..125
FT /note="LRR 3"
FT REPEAT 128..149
FT /note="LRR 4"
FT REPEAT 152..173
FT /note="LRR 5"
FT DOMAIN 185..247
FT /note="LRRCT"
FT DOMAIN 292..379
FT /note="Fibronectin type-III"
FT REGION 249..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 749
FT /note="L -> P (in Ref. 1; BAC27630)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 823 AA; 90029 MW; B8CC92E32D1AC4D7 CRC64;
MLRLGLCAAA LLCVCQPGAV RADCWLIEGD KGYVWLAICS QNQPPYETIP QHINSTVHDL
RLNENKLKAV LYSSLNRFGN LTDLNLTKNE ISYIEDGAFL GQTSLQVLQL GYNRLSNLTE
GMLRGMSRLQ FLFVQHNLIE VVTPTAFSEC PSLISIDLSS NRLSRLDGAT FASLASLMVC
ELAGNPFNCE CDLFGFLAWL VVFNNVTKNY DRLQCESPRE FAGYPLLVPR PYHSLNAITV
LQAKCRNGSM PARPVSHPTP YSTDAQREPD ENSGFNPDEI LSVEPPASST TDASAGPAIK
LHQVTFTSAT LVVIIPHPYS KMYVLVQYNN SYFSDVMTLK NKKEIVTLDK LRAHTEYTFC
VTSLRNSRRF NHTCLTFTTR DLVPGDLAPS TSTTTHYIMT ILGCLFGMVI VLGAVYYCLR
KRRMQEEKQK SVNVKKTILE MRYGADVDAG SIVHAAQKLG EPPVLPVARM SSIPSMVGEK
LPASKGLEAG LDTPKVATKG NYIEVRTGAA GDSLARPEEE LPEIENGQGS AAEISTIAKE
VDKVNQIINN CIDALKLDSA SFLGGGGGGG GGGDSDLAFE CQSLPAAPAA SSAATPGALE
RPSFLSPPYK ESSHHPLQRQ LSADAAVSRK TCSVSSSGSI KSAKVFSLDV PDHPTPTGLA
KSDSKYIEKG SPLNSPLDRL PLVPTGSSGS SGGGGGIHHL EVKPAYHCSE HRHSFPALYY
EEGADSLSQR VSFLKPLTRS KRDSTYSQLS PRHYYSGYSS SPEYSSESTH KIWERFRPYK
KHHREEVYMA AGHALRKKVQ FAKDEDLHDI LDYWKGVSAQ QKL
