PDCL2_MOUSE
ID PDCL2_MOUSE Reviewed; 240 AA.
AC Q78Y63; Q3V0H7; Q9DA99; Q9WUP3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Phosducin-like protein 2;
DE AltName: Full=MgcPhLP;
DE AltName: Full=Phosducin-like protein similar 1;
GN Name=Pdcl2;
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 [MRNA], AND RETRACTED PAPER.
RC STRAIN=C57BL/6 X DBA/2; TISSUE=Testis;
RX PubMed=12424248; DOI=10.1074/jbc.m207434200;
RA Lopez P., Yaman R., Lopez-Fernandez L.A., Vidal F., Puel D., Clertant P.,
RA Cuzin F., Rassoulzadegan M.;
RT "A novel germ line-specific gene of the phosducin-like protein (PhLP)
RT family. A meiotic function conserved from yeast to mice.";
RL J. Biol. Chem. 278:1751-1757(2003).
RN [2]
RP RETRACTION NOTICE OF PUBMED:12424248.
RX PubMed=31519761; DOI=10.1074/jbc.w119.010673;
RA Lopez P., Yaman R., Lopez-Fernandez L.A., Vidal F., Puel D., Clertant P.,
RA Cuzin F., Rassoulzadegan M.;
RT "Withdrawal: A novel germ line-specific gene of the phosducin-like protein
RT (PhLP) family: A meiotic function conserved from yeast to mice.";
RL J. Biol. Chem. 294:13832-13832(2019).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-240.
RC STRAIN=129/Sv;
RX PubMed=11116088; DOI=10.1101/gr.10.12.1928;
RA Wilsbacher L.D., Sangoram A.M., Antoch M.P., Takahashi J.S.;
RT "The mouse Clock locus: sequence and comparative analysis of 204 kb from
RT mouse chromosome 5.";
RL Genome Res. 10:1928-1940(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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).
RN [7]
RP STRUCTURE BY NMR OF 88-209.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the thioredoxin-like domain of phosducin-like
RT protein 2 (PDCL2).";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q78Y63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q78Y63-2; Sequence=VSP_022360;
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
CC -!- CAUTION: Reported to be expressed in male and female germ cells, to be
CC up-regulated at the protein level as early as 3 hours after chorionic
CC gonadotropin treatment in the ovary, and to interact with 14-3-3
CC proteins (PubMed:12424248). However, the publication has been retracted
CC due to image duplication and manipulation. The nucleotide sequence has
CC been confirmed by other studies (PubMed:11116088).
CC {ECO:0000269|PubMed:11116088, ECO:0000269|PubMed:12424248,
CC ECO:0000305|PubMed:31519761}.
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DR EMBL; AK005602; BAB24145.1; -; mRNA.
DR EMBL; AK005814; BAB24251.1; -; mRNA.
DR EMBL; AK006040; BAB24379.1; -; mRNA.
DR EMBL; AK132738; BAE21326.1; -; mRNA.
DR EMBL; AK133140; BAE21527.1; -; mRNA.
DR EMBL; BC048432; AAH48432.1; -; mRNA.
DR EMBL; AF146793; AAD30564.2; -; Genomic_DNA.
DR CCDS; CCDS39116.1; -. [Q78Y63-1]
DR CCDS; CCDS80304.1; -. [Q78Y63-2]
DR RefSeq; NP_001297566.1; NM_001310637.1. [Q78Y63-2]
DR RefSeq; NP_075997.1; NM_023508.7. [Q78Y63-1]
DR PDB; 2DBC; NMR; -; A=88-209.
DR PDBsum; 2DBC; -.
DR AlphaFoldDB; Q78Y63; -.
DR SMR; Q78Y63; -.
DR STRING; 10090.ENSMUSP00000031145; -.
DR PhosphoSitePlus; Q78Y63; -.
DR EPD; Q78Y63; -.
DR PaxDb; Q78Y63; -.
DR PRIDE; Q78Y63; -.
DR ProteomicsDB; 289332; -. [Q78Y63-1]
DR ProteomicsDB; 289333; -. [Q78Y63-2]
DR Antibodypedia; 44095; 80 antibodies from 24 providers.
DR DNASU; 79455; -.
DR Ensembl; ENSMUST00000031145; ENSMUSP00000031145; ENSMUSG00000029235. [Q78Y63-1]
DR Ensembl; ENSMUST00000122213; ENSMUSP00000113699; ENSMUSG00000029235. [Q78Y63-2]
DR GeneID; 79455; -.
DR KEGG; mmu:79455; -.
DR UCSC; uc008xuu.1; mouse. [Q78Y63-1]
DR CTD; 132954; -.
DR MGI; MGI:1890655; Pdcl2.
DR VEuPathDB; HostDB:ENSMUSG00000029235; -.
DR eggNOG; KOG3170; Eukaryota.
DR GeneTree; ENSGT00940000160654; -.
DR HOGENOM; CLU_072604_0_1_1; -.
DR InParanoid; Q78Y63; -.
DR OMA; DMRAIEI; -.
DR OrthoDB; 1247977at2759; -.
DR PhylomeDB; Q78Y63; -.
DR TreeFam; TF315179; -.
DR BioGRID-ORCS; 79455; 1 hit in 72 CRISPR screens.
DR EvolutionaryTrace; Q78Y63; -.
DR PRO; PR:Q78Y63; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q78Y63; protein.
DR Bgee; ENSMUSG00000029235; Expressed in seminiferous tubule of testis and 11 other tissues.
DR Genevisible; Q78Y63; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF02114; Phosducin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Reference proteome.
FT CHAIN 1..240
FT /note="Phosducin-like protein 2"
FT /id="PRO_0000246158"
FT REGION 89..240
FT /note="Thioredoxin fold"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022360"
FT CONFLICT 209
FT /note="N -> T (in Ref. 5; AAD30564)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..212
FT /note="PKK -> TKR (in Ref. 3; BAB24379)"
FT /evidence="ECO:0000305"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:2DBC"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2DBC"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:2DBC"
FT HELIX 123..138
FT /evidence="ECO:0007829|PDB:2DBC"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:2DBC"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2DBC"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:2DBC"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:2DBC"
FT TURN 179..183
FT /evidence="ECO:0007829|PDB:2DBC"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:2DBC"
SQ SEQUENCE 240 AA; 27770 MW; 580715EFE61E86F1 CRC64;
MQDPNEDTEW NEILRNFGIL PPKEEPKDEI EEMVLRLQQE AMVKPYEKMT LAQLKEAEDE
FDEEDIKAIE IYREKRLQEW KALKKKQKFG ELREISGNQY VNEVTNAEKD LWVVIHLYRS
SVPMCLVVNQ HLSVLARKFP ETKFVKAIVN SCIEHYHDNC LPTIFVYKNG QIEGKFIGII
ECGGINLKLE ELEWKLSEVG AIQSDLEENP KKGIADMMVS SIRNISIYDS DSSGSDTEAK
