PDZD8_MOUSE
ID PDZD8_MOUSE Reviewed; 1147 AA.
AC B9EJ80; Q3UMB1;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=PDZ domain-containing protein 8 {ECO:0000305};
GN Name=Pdzd8 {ECO:0000312|MGI:MGI:2677270};
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 TISSUE=Mammary gland {ECO:0000312|EMBL:BAE26187.1};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532 AND SER-973, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29097544; DOI=10.1126/science.aan6009;
RA Hirabayashi Y., Kwon S.K., Paek H., Pernice W.M., Paul M.A., Lee J.,
RA Erfani P., Raczkowski A., Petrey D.S., Pon L.A., Polleux F.;
RT "ER-mitochondria tethering by PDZD8 regulates Ca(2+) dynamics in mammalian
RT neurons.";
RL Science 358:623-630(2017).
CC -!- FUNCTION: Molecular tethering protein that connects endoplasmic
CC reticulum and mitochondria membranes (PubMed:29097544). PDZD8-dependent
CC endoplasmic reticulum-mitochondria membrane tethering is essential for
CC endoplasmic reticulum-mitochondria Ca(2+) transfer (PubMed:29097544).
CC In neurons, involved in the regulation of dendritic Ca(2+) dynamics by
CC regulating mitochondrial Ca(2+) uptake in neurons (PubMed:29097544).
CC {ECO:0000269|PubMed:29097544}.
CC -!- SUBUNIT: Interacts with MSN. {ECO:0000250|UniProtKB:Q8NEN9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:29097544}; Single-pass membrane protein
CC {ECO:0000255}. Note=Localizes at mitochondria-endoplasmic reticulum
CC contact sites. {ECO:0000269|PubMed:29097544}.
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that binds
CC phospholipids. {ECO:0000250|UniProtKB:A0FGR8}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK145020; BAE26187.1; -; mRNA.
DR EMBL; AC139040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141370; AAI41371.1; -; mRNA.
DR EMBL; BC141371; AAI41372.1; -; mRNA.
DR CCDS; CCDS29936.1; -.
DR RefSeq; NP_001028394.2; NM_001033222.3.
DR AlphaFoldDB; B9EJ80; -.
DR SMR; B9EJ80; -.
DR IntAct; B9EJ80; 2.
DR MINT; B9EJ80; -.
DR STRING; 10090.ENSMUSP00000096880; -.
DR iPTMnet; B9EJ80; -.
DR PhosphoSitePlus; B9EJ80; -.
DR jPOST; B9EJ80; -.
DR MaxQB; B9EJ80; -.
DR PaxDb; B9EJ80; -.
DR PeptideAtlas; B9EJ80; -.
DR PRIDE; B9EJ80; -.
DR ProteomicsDB; 287907; -.
DR Antibodypedia; 2575; 79 antibodies from 17 providers.
DR DNASU; 107368; -.
DR Ensembl; ENSMUST00000099274; ENSMUSP00000096880; ENSMUSG00000074746.
DR GeneID; 107368; -.
DR KEGG; mmu:107368; -.
DR UCSC; uc008ibj.2; mouse.
DR CTD; 118987; -.
DR MGI; MGI:2677270; Pdzd8.
DR VEuPathDB; HostDB:ENSMUSG00000074746; -.
DR eggNOG; KOG3532; Eukaryota.
DR GeneTree; ENSGT00390000017746; -.
DR HOGENOM; CLU_008594_0_0_1; -.
DR InParanoid; B9EJ80; -.
DR OMA; TLIECTR; -.
DR OrthoDB; 1195477at2759; -.
DR PhylomeDB; B9EJ80; -.
DR TreeFam; TF324166; -.
DR BioGRID-ORCS; 107368; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Pdzd8; mouse.
DR PRO; PR:B9EJ80; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; B9EJ80; protein.
DR Bgee; ENSMUSG00000074746; Expressed in otolith organ and 223 other tissues.
DR Genevisible; Q3UMB1; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IDA:UniProtKB.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IDA:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:MGI.
DR CDD; cd00029; C1; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR039275; PDZD8.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR21519; PTHR21519; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51847; SMP; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; Lipid transport; Lipid-binding;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc-finger.
FT CHAIN 1..1147
FT /note="PDZ domain-containing protein 8"
FT /id="PRO_0000442772"
FT TRANSMEM 2..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 87..293
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 365..448
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ZN_FING 833..884
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 504..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1021..1056
FT /evidence="ECO:0000255"
FT COMPBIAS 553..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..593
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEN9"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEN9"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEN9"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 660
FT /note="A -> V (in Ref. 1; BAE26187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1147 AA; 127739 MW; 70674471242ADD1B CRC64;
MGLLLLILAS AVLGSFLTLL AQFLLLYRRQ PEPRADEAAR AGDGFRYLKP VPGLPLREYL
YGGGAEELAA CSSEAGASST PTPDSPAPPT LETCYFLNAT ILFLFRELRD TALARRWVTK
KIKVEFEELL QTKTAGRLLE GLSLRDVFLG DTVPFIKTIR LVRPVVASGT GEPDDPDGDA
LPATCPEELA FEAEVEYNGG FHLAIDVDLV FGKSAYLFVK LSRVVGRLRF VLTRVPFTHW
FFSFVEDPLI DFEVRSQFEG RPMPQLTSII VNQLKKIIKR KHTLPSYKIR FKPFFPYQAL
QGFEEDEELI HIQQWALTEG RLKVTLLECS RLFIFGSYDR ETNVHCTLEL SSGVWEEKQR
SSIKTVELIK GNLQSVGLTL RLVQSTDGYA GHVIIETVAP NSPAAMADLQ RGDRLIAIGG
VKITSTLQVL KLIKQAGDRV LVYYQRPAGQ SSQDSLGQLE ESFLSSSCQA AYEEDAAGLS
ADTENRDLDS EFEDLASDVR VQTELKEETQ PLSHSPKRTP TTLSIKPLGA ISPVLNRKLI
SGIHPPPQKL PSKEGNKPST LKTSETTEAA QVSKPQGPTF KPPVPPRPQG RVPLPPTDTS
AQADPEAPEK PDKVLLPPPP ADKPAEKQVK SVDQGEDVAA GKQSSAKQEG VKDLPSESSA
PTKDSSDDPQ MWESSEVLYR NKVGKWSRTR ASCVFDIEAC HRYLNIALWC RDPFKLGGLI
CLGHVSLKLE EVALGCLATS NMEYLTKFRL EPPTPKAMVT RTALRNLSMQ KGFNDKFCFG
DITIHFKYLK EGEPDHHIVP NVEKEKELHL VEEVSTLPKE EHFVGQMSLS ENKHSFQDTQ
FQNPTWCDYC KKKVWTKAAS QCMFCAYVCH KKCQEKCLAE TPLCGATERR IDRTLKNLRL
EGQDPLLGLP PRVEIEANKS VNKTTGLTRH IINTSSRLLN LRQVSKTRLS EPGTDLVEPS
PKHTPNTSDN EGSDTEVCGS NSPSKRGNSA GIKLMRKEGG LDDSVFIAVK EIGRDLYRGL
PTEERIQKLE FMLDKLQNEI DQELEHNNSL VREEKETNDT RKKSVLSAAL AKSGERLQAL
TLLMIHYRAG IEDIETLENL SLDQHSKKMN KYADDTEEDL DSEISQLIDS QPFSNISDDL
FGPSESV
