PDXD1_MOUSE
ID PDXD1_MOUSE Reviewed; 787 AA.
AC Q99K01; Q3TCL3; Q3TN13; Q8BMK9; Q8BW02; Q8BW51; Q8BZZ4; Q9DC25;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Pyridoxal-dependent decarboxylase domain-containing protein 1;
DE EC=4.1.1.-;
GN Name=Pdxdc1;
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; 3 AND 5), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 223-787 (ISOFORM 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Lung, Ovary, Pituitary, Stomach, Testis, and
RC Urinary bladder;
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 STRAIN=Czech II; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687 AND SER-718, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687; THR-691 AND SER-748, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q99K01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99K01-2; Sequence=VSP_027346;
CC Name=3;
CC IsoId=Q99K01-3; Sequence=VSP_027345;
CC Name=4;
CC IsoId=Q99K01-4; Sequence=VSP_027344;
CC Name=5;
CC IsoId=Q99K01-5; Sequence=VSP_029421, VSP_029422;
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35991.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK004611; BAB23408.1; -; mRNA.
DR EMBL; AK030613; BAC27047.1; -; mRNA.
DR EMBL; AK033107; BAC28155.1; -; mRNA.
DR EMBL; AK054329; BAC35732.1; -; mRNA.
DR EMBL; AK075829; BAC35991.1; ALT_INIT; mRNA.
DR EMBL; AK163696; BAE37462.1; -; mRNA.
DR EMBL; AK165587; BAE38276.1; -; mRNA.
DR EMBL; AK170661; BAE41943.1; -; mRNA.
DR EMBL; BC005541; AAH05541.1; -; mRNA.
DR CCDS; CCDS37261.1; -. [Q99K01-3]
DR RefSeq; NP_001034622.1; NM_001039533.2. [Q99K01-3]
DR RefSeq; NP_001277946.1; NM_001291017.1.
DR RefSeq; NP_444411.2; NM_053181.3. [Q99K01-1]
DR AlphaFoldDB; Q99K01; -.
DR SMR; Q99K01; -.
DR BioGRID; 220462; 7.
DR IntAct; Q99K01; 3.
DR MINT; Q99K01; -.
DR STRING; 10090.ENSMUSP00000111471; -.
DR iPTMnet; Q99K01; -.
DR PhosphoSitePlus; Q99K01; -.
DR SwissPalm; Q99K01; -.
DR EPD; Q99K01; -.
DR jPOST; Q99K01; -.
DR MaxQB; Q99K01; -.
DR PaxDb; Q99K01; -.
DR PeptideAtlas; Q99K01; -.
DR PRIDE; Q99K01; -.
DR ProteomicsDB; 287814; -. [Q99K01-1]
DR ProteomicsDB; 287815; -. [Q99K01-2]
DR ProteomicsDB; 287816; -. [Q99K01-3]
DR ProteomicsDB; 287817; -. [Q99K01-4]
DR ProteomicsDB; 287818; -. [Q99K01-5]
DR Antibodypedia; 24937; 213 antibodies from 26 providers.
DR Ensembl; ENSMUST00000115802; ENSMUSP00000111468; ENSMUSG00000022680. [Q99K01-5]
DR Ensembl; ENSMUST00000115804; ENSMUSP00000111471; ENSMUSG00000022680. [Q99K01-3]
DR GeneID; 94184; -.
DR KEGG; mmu:94184; -.
DR UCSC; uc007ygl.2; mouse. [Q99K01-3]
DR UCSC; uc007ygm.2; mouse. [Q99K01-2]
DR UCSC; uc007ygn.2; mouse. [Q99K01-1]
DR CTD; 23042; -.
DR MGI; MGI:1920909; Pdxdc1.
DR VEuPathDB; HostDB:ENSMUSG00000022680; -.
DR eggNOG; KOG0630; Eukaryota.
DR GeneTree; ENSGT00390000009628; -.
DR HOGENOM; CLU_014327_0_0_1; -.
DR InParanoid; Q99K01; -.
DR OMA; RYCPLEL; -.
DR OrthoDB; 804210at2759; -.
DR PhylomeDB; Q99K01; -.
DR TreeFam; TF313101; -.
DR BioGRID-ORCS; 94184; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Pdxdc1; mouse.
DR PRO; PR:Q99K01; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q99K01; protein.
DR Bgee; ENSMUSG00000022680; Expressed in left colon and 263 other tissues.
DR ExpressionAtlas; Q99K01; baseline and differential.
DR Genevisible; Q99K01; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Decarboxylase; Lyase; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..787
FT /note="Pyridoxal-dependent decarboxylase domain-containing
FT protein 1"
FT /id="PRO_0000297678"
FT REGION 26..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 691
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P996"
FT VAR_SEQ 381..384
FT /note="VEDE -> GFSV (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029421"
FT VAR_SEQ 385..787
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029422"
FT VAR_SEQ 702
FT /note="P -> PVRLMSL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027344"
FT VAR_SEQ 703..787
FT /note="GQKPFKRSLRGSDAVSETSSVSHIEDLEKVEQLSSGLEHDNLEAHSPEQPPR
FT ATDLTARQTEALQNQAQHQEDDHSQVEELERLR -> DGNQGAET (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027345"
FT VAR_SEQ 780..787
FT /note="VEELERLR -> MGTRVQRLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027346"
FT CONFLICT 176
FT /note="I -> T (in Ref. 1; BAE38276)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="V -> I (in Ref. 2; AAH05541)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="R -> K (in Ref. 2; AAH05541)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="H -> Q (in Ref. 1; BAE38276)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="G -> W (in Ref. 1; BAC27047)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="T -> A (in Ref. 2; AAH05541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 787 AA; 87335 MW; 21B24DB271823DDC CRC64;
MDASLEKIAD PTLAEMGKNL KEAMRMLEKS PRRTEEENGK KPVSEDIPGP LQGSGQDMVS
ILQLVQNLMH GDEDEEPQST RIQNIGEQGH MALLGHSLGA YISTLDKEKL RKLTTRILSD
TTLWLRRIFR YENGCAYFHE EEREGLAKIC RLAIHSRYED FVVDGFNVLY NKKPVIYLSA
AARPGLGQYL CNQLGLPFPC LCRVPCNTMF GSQHQMDVAF LEKLIKDDVE RGRLPLLLVA
NAGTAAVGHT DKIGRLKELC EQYGIWLHVE GVNLATLALG YVSSSVLAAT KCDSMTLTPG
LWLGLPAVPA VTLYKHDDPA LTLVAGLTSN KPADKLRALP LWLSLQYLGL DGIVERIKHA
CHLSQRLQES LKKVDHIKIL VEDELSSPVV VFRFFQELPA SDSAFKAVPV SNIAPAAVGR
ERHSCDALNR WLGEQLKQLV PQCGLTVIDL EVDGTCVRFS PLMTAEGLGT RGEDVDQLIT
CIQSKLPVLT CTLQLREEFK QEVEGTAGLL YVDDPNWPGI GVVRYEHAND DDTSLKSDPE
GEKIHTGLLK KLNELESDLT FKIGPEYKSM KSCIYIGMAS DDVDVSELVE TIAVTAREIE
ENSRLLENMT EVVRKGIQEA QVQLQKANEE RLLEEGVLRQ IPVVGSVLNW FSPVQASQKG
RSFNLTAGSL ESTEYTYVHK VQGTGVTPPP TPLGTRSKQR LPGQKPFKRS LRGSDAVSET
SSVSHIEDLE KVEQLSSGLE HDNLEAHSPE QPPRATDLTA RQTEALQNQA QHQEDDHSQV
EELERLR
