GDPD4_MOUSE
ID GDPD4_MOUSE Reviewed; 632 AA.
AC Q3TT99; Q8BI25;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 4;
DE EC=3.1.-.-;
DE AltName: Full=Glycerophosphodiester phosphodiesterase 6;
GN Name=Gdpd4; Synonyms=Gde6;
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=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 [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15276213; DOI=10.1016/j.gene.2004.04.026;
RA Nogusa Y., Fujioka Y., Komatsu R., Kato N., Yanaka N.;
RT "Isolation and characterization of two serpentine membrane proteins
RT containing glycerophosphodiester phosphodiesterase, GDE2 and GDE6.";
RL Gene 337:173-179(2004).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15276213}. Membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in testis, in particular in spermatocytes.
CC {ECO:0000269|PubMed:15276213}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26496.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK029527; BAC26496.1; ALT_FRAME; mRNA.
DR EMBL; AK161500; BAE36426.1; -; mRNA.
DR CCDS; CCDS52318.1; -.
DR RefSeq; NP_808364.2; NM_177696.3.
DR AlphaFoldDB; Q3TT99; -.
DR SMR; Q3TT99; -.
DR STRING; 10090.ENSMUSP00000036772; -.
DR GlyGen; Q3TT99; 4 sites.
DR PhosphoSitePlus; Q3TT99; -.
DR PaxDb; Q3TT99; -.
DR PRIDE; Q3TT99; -.
DR ProteomicsDB; 265741; -.
DR DNASU; 233537; -.
DR Ensembl; ENSMUST00000041860; ENSMUSP00000036772; ENSMUSG00000035582.
DR Ensembl; ENSMUST00000170049; ENSMUSP00000131960; ENSMUSG00000035582.
DR GeneID; 233537; -.
DR KEGG; mmu:233537; -.
DR UCSC; uc012fpl.1; mouse.
DR CTD; 220032; -.
DR MGI; MGI:3606573; Gdpd4.
DR VEuPathDB; HostDB:ENSMUSG00000035582; -.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00940000156251; -.
DR HOGENOM; CLU_024259_2_0_1; -.
DR InParanoid; Q3TT99; -.
DR OMA; GFWFLWS; -.
DR OrthoDB; 404866at2759; -.
DR PhylomeDB; Q3TT99; -.
DR TreeFam; TF313692; -.
DR BioGRID-ORCS; 233537; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Gdpd4; mouse.
DR PRO; PR:Q3TT99; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3TT99; protein.
DR Bgee; ENSMUSG00000035582; Expressed in spermatocyte and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..632
FT /note="Glycerophosphodiester phosphodiesterase domain-
FT containing protein 4"
FT /id="PRO_0000251940"
FT TOPO_DOM 1..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..542
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 276..533
FT /note="GP-PDE"
FT REGION 596..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 308
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 310
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 323
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 165
FT /note="S -> T (in Ref. 1; BAC26496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 73220 MW; 895F009B4CDEDD80 CRC64;
MEETQDSSSS KPKNTDENFS LWIEQYFNHK CCITFLTGCY SCQWQYREWE KTELGSCCCS
RKEQFFYMCL VIAFILSVLF LFVWVETSNE YNGFDWVVYL GTGCWFFWSI LVLSAAGIMV
AYTTLLLLLG FLLLWERIEL NLHTSHKVFI CLVIVLCSFL LAVLSHFWKD KWLIAGLSLQ
IFAPFVHLSL ITVMIIISWP LSICVARLES EVKVRRYRMA DYEQEIQERC NVFQRLRALQ
IAAGLSFLII LLCLYLMPLG IYSPCILKKE NLGPKPTLFG HRGAPMLAPE NTMMSFEKAV
ELDVSGLETD IYLSFDSVPF LMHDYDLTRT TNIKEVLPSA AGNHTSNFNW TFLSTLNAGK
WFLKHKPFFG MKPLSEADKR RAGNQSIPQL SELLALAKRE QKIVIFDLFG PRPGHPLRNT
FVRRVVKVIL DSKIEQRLIF WLPGFDRDYV RFMAPGFQHV GRLWSIKDLT KHNITIINVD
YKRLFYAGLR DYKEAKIYIH VYVINEPWLF SLAWCSSINS VTTDNIELLN QLSRPLFFMT
PGFYMFMWLF LDIASAVIIG FVFCYNWIKE IKRERWLEAA ASSGLLHSET ITDITENNDA
SQQKPEVAPT SANLAPENMI ELQKTEPKTE NL
