PLD5_MOUSE
ID PLD5_MOUSE Reviewed; 536 AA.
AC Q3UNN8; Q3UVW3; Q497Q7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Inactive phospholipase D5;
DE Short=Inactive PLD 5;
DE AltName: Full=Inactive choline phosphatase 5;
DE AltName: Full=Inactive phosphatidylcholine-hydrolyzing phospholipase D5;
GN Name=Pld5;
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 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 2).
RC TISSUE=Pituitary;
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UNN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UNN8-2; Sequence=VSP_025729;
CC Name=3;
CC IsoId=Q3UNN8-3; Sequence=VSP_025728;
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, it lacks the
CC conserved active sites, suggesting that it has no phospholipase
CC activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00429.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK136851; BAE23146.1; -; mRNA.
DR EMBL; AK136888; BAE23156.1; -; mRNA.
DR EMBL; AK144116; BAE25709.1; -; mRNA.
DR EMBL; BC100428; AAI00429.1; ALT_SEQ; mRNA.
DR CCDS; CCDS15552.1; -. [Q3UNN8-1]
DR RefSeq; NP_001182745.1; NM_001195816.1.
DR RefSeq; NP_795890.2; NM_176916.4. [Q3UNN8-1]
DR RefSeq; XP_006496963.1; XM_006496900.3. [Q3UNN8-3]
DR RefSeq; XP_011237130.1; XM_011238828.1.
DR RefSeq; XP_011237131.1; XM_011238829.2.
DR RefSeq; XP_017176664.1; XM_017321175.1.
DR AlphaFoldDB; Q3UNN8; -.
DR SMR; Q3UNN8; -.
DR STRING; 10090.ENSMUSP00000069326; -.
DR GlyConnect; 2387; 1 N-Linked glycan (1 site).
DR GlyGen; Q3UNN8; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q3UNN8; -.
DR PhosphoSitePlus; Q3UNN8; -.
DR PaxDb; Q3UNN8; -.
DR PRIDE; Q3UNN8; -.
DR ProteomicsDB; 289678; -. [Q3UNN8-1]
DR ProteomicsDB; 289679; -. [Q3UNN8-2]
DR ProteomicsDB; 289680; -. [Q3UNN8-3]
DR Antibodypedia; 34707; 126 antibodies from 20 providers.
DR Ensembl; ENSMUST00000065967; ENSMUSP00000069326; ENSMUSG00000055214. [Q3UNN8-1]
DR GeneID; 319455; -.
DR KEGG; mmu:319455; -.
DR UCSC; uc007dtw.1; mouse. [Q3UNN8-1]
DR CTD; 200150; -.
DR MGI; MGI:2442056; Pld5.
DR VEuPathDB; HostDB:ENSMUSG00000055214; -.
DR eggNOG; KOG3603; Eukaryota.
DR GeneTree; ENSGT00950000183059; -.
DR InParanoid; Q3UNN8; -.
DR OMA; CATKEQR; -.
DR OrthoDB; 1057467at2759; -.
DR PhylomeDB; Q3UNN8; -.
DR TreeFam; TF313378; -.
DR BioGRID-ORCS; 319455; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pld5; mouse.
DR PRO; PR:Q3UNN8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3UNN8; protein.
DR Bgee; ENSMUSG00000055214; Expressed in cerebellar cortex and 31 other tissues.
DR ExpressionAtlas; Q3UNN8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR InterPro; IPR032803; PLDc_3.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13918; PLDc_3; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..536
FT /note="Inactive phospholipase D5"
FT /id="PRO_0000288607"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..536
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 215..242
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 434..460
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 503..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..208
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025728"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025729"
SQ SEQUENCE 536 AA; 61066 MW; 6A9D11644CF0FBBF CRC64;
MEIRQHEWLS ASPHEGFEQM RLKSRPKEPS PSLTRVGANF YSSVKQQDYS ASVWLRRKDK
LEHSQQKCIV IFALVCCFAV LVALIFSAVD IMGEDEDGLS EKNCQNKCRI ALVENIPEGL
NYSEDAPFHL PLFQGWMNLL NMAKKSVDIV SSHWDLNHTH PAACQGQRLF EKLLQLTSQN
IEVKLVSDVT ADSKVLEALK LKGAEVTYMN MTAYNKGRLQ SSFWIVDKQH VYIGSAGLDW
RSLGQMKELG VIFYNCSCLV LDLQRIFALY SSLKFKSRVP QTWSKRLYGV YDNEKKLQLQ
LNETKSQAFV SNSPKLFCPK NRSFDIDAIY SVIDDAKQYV YIAVTDYLPI SSTSSKRTYW
PDLDGKIREA LVLRSVKVRL LISFWKETDP LTFNFISSLK AICTEIANCS LKVKFFDLER
ENACATKEQK NQTFPKLNRN KYMVTDGAAY IGNFDWVGND FTQNAGTGLV INQADVRDNR
SIIKQLKDVF ERDWYSPYAK SIQPTKQPNC SSLSKLKSPS KQPAMANATG REPLSV
