PPR29_HUMAN
ID PPR29_HUMAN Reviewed; 820 AA.
AC Q5R3F8; Q96PY3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP FUNCTION, AND INTERACTION WITH PPP1CA.
RX PubMed=19389623; DOI=10.1016/j.chembiol.2009.02.012;
RA Hendrickx A., Beullens M., Ceulemans H., Den Abt T., Van Eynde A.,
RA Nicolaescu E., Lesage B., Bollen M.;
RT "Docking motif-guided mapping of the interactome of protein phosphatase-
RT 1.";
RL Chem. Biol. 16:365-371(2009).
CC -!- FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1)
CC complexes. {ECO:0000269|PubMed:19389623}.
CC -!- SUBUNIT: Interacts with PPP1CA. {ECO:0000269|PubMed:19389623}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB67797.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB067491; BAB67797.1; ALT_INIT; mRNA.
DR EMBL; Z94160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS33642.1; -.
DR RefSeq; NP_443138.2; NM_052906.4.
DR AlphaFoldDB; Q5R3F8; -.
DR SMR; Q5R3F8; -.
DR BioGRID; 125356; 37.
DR IntAct; Q5R3F8; 2.
DR MINT; Q5R3F8; -.
DR STRING; 9606.ENSP00000385277; -.
DR GlyGen; Q5R3F8; 7 sites.
DR iPTMnet; Q5R3F8; -.
DR PhosphoSitePlus; Q5R3F8; -.
DR BioMuta; ELFN2; -.
DR DMDM; 74755895; -.
DR EPD; Q5R3F8; -.
DR jPOST; Q5R3F8; -.
DR MassIVE; Q5R3F8; -.
DR MaxQB; Q5R3F8; -.
DR PaxDb; Q5R3F8; -.
DR PeptideAtlas; Q5R3F8; -.
DR PRIDE; Q5R3F8; -.
DR ProteomicsDB; 63725; -.
DR Antibodypedia; 274; 64 antibodies from 16 providers.
DR DNASU; 114794; -.
DR Ensembl; ENST00000402918.7; ENSP00000385277.1; ENSG00000166897.16.
DR GeneID; 114794; -.
DR KEGG; hsa:114794; -.
DR MANE-Select; ENST00000402918.7; ENSP00000385277.1; NM_052906.5; NP_443138.2.
DR UCSC; uc003asq.4; human.
DR CTD; 114794; -.
DR DisGeNET; 114794; -.
DR GeneCards; ELFN2; -.
DR HGNC; HGNC:29396; ELFN2.
DR HPA; ENSG00000166897; Group enriched (brain, retina).
DR neXtProt; NX_Q5R3F8; -.
DR OpenTargets; ENSG00000166897; -.
DR PharmGKB; PA162385040; -.
DR VEuPathDB; HostDB:ENSG00000166897; -.
DR eggNOG; ENOG502QVFI; Eukaryota.
DR GeneTree; ENSGT00940000159737; -.
DR HOGENOM; CLU_018770_0_0_1; -.
DR InParanoid; Q5R3F8; -.
DR OMA; NLMVCEL; -.
DR OrthoDB; 190870at2759; -.
DR PhylomeDB; Q5R3F8; -.
DR TreeFam; TF332887; -.
DR PathwayCommons; Q5R3F8; -.
DR SignaLink; Q5R3F8; -.
DR BioGRID-ORCS; 114794; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; ELFN2; human.
DR GenomeRNAi; 114794; -.
DR Pharos; Q5R3F8; Tdark.
DR PRO; PR:Q5R3F8; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q5R3F8; protein.
DR Bgee; ENSG00000166897; Expressed in cortical plate and 114 other tissues.
DR Genevisible; Q5R3F8; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
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..820
FT /note="Protein phosphatase 1 regulatory subunit 29"
FT /id="PRO_0000256138"
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..820
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 250..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FM6"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FM6"
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 239
FT /note="T -> I (in Ref. 1; BAB67797)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="P -> S (in Ref. 1; BAB67797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 820 AA; 89687 MW; 18BCDBDEC0F21212 CRC64;
MLRLGLCAAA LLCVCRPGAV RADCWLIEGD KGYVWLAICS QNQPPYETIP QHINSTVHDL
RLNENKLKAV LYSSLNRFGN LTDLNLTKNE ISYIEDGAFL GQSSLQVLQL GYNKLSNLTE
GMLRGMSRLQ FLFVQHNLIE VVTPTAFSEC PSLISIDLSS NRLSRLDGAT FASLASLMVC
ELAGNPFNCE CDLFGFLAWL VVFNNVTKNY DRLQCESPRE FAGYPLLVPR PYHSLNAITV
LQAKCRNGSL PARPVSHPTP YSTDAQREPD ENSGFNPDEI LSVEPPASST TDASAGPAIK
LHHVTFTSAT LVVIIPHPYS KMYILVQYNN SYFSDVMTLK NKKEIVTLDK LRAHTEYTFC
VTSLRNSRRF NHTCLTFTTR DPVPGDLAPS TSTTTHYIMT ILGCLFGMVI VLGAVYYCLR
KRRMQEEKQK SVNVKKTILE MRYGADVDAG SIVHAAQKLG EPPVLPVSRM ASIPSMIGEK
LPTAKGLEAG LDTPKVATKG NYIEVRTGAG GDGLARPEDD LPDLENGQGS AAEISTIAKE
VDKVNQIINN CIDALKLDSA SFLGGGSSSG DPELAFECQS LPAAAAASSA TGPGALERPS
FLSPPYKESS HHPLQRQLSA DAAVTRKTCS VSSSGSIKSA KVFSLDVPDH PAATGLAKGD
SKYIEKGSPL NSPLDRLPLV PAGSGGGSGG GGGIHHLEVK PAYHCSEHRH SFPALYYEEG
ADSLSQRVSF LKPLTRSKRD STYSQLSPRH YYSGYSSSPE YSSESTHKIW ERFRPYKKHH
REEVYMAAGH ALRKKVQFAK DEDLHDILDY WKGVSAQQKL
