PDZ11_MOUSE
ID PDZ11_MOUSE Reviewed; 140 AA.
AC Q9CZG9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=PDZ domain-containing protein 11;
GN Name=Pdzd11; Synonyms=Pdzk11;
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=Embryo;
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].
RC STRAIN=FVB/N; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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 [4]
RP FUNCTION, INTERACTION WITH PLEKHA7, AND SUBCELLULAR LOCATION.
RX PubMed=30463011; DOI=10.1016/j.celrep.2018.10.088;
RA Shah J., Rouaud F., Guerrera D., Vasileva E., Popov L.M., Kelley W.L.,
RA Rubinstein E., Carette J.E., Amieva M.R., Citi S.;
RT "A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
RT Promote alpha-Toxin Cytotoxicity.";
RL Cell Rep. 25:2132-2147(2018).
RN [5]
RP STRUCTURE BY NMR OF 37-127.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain from RIKEN cDNA 2700099c19.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: Mediates docking of ADAM10 to zonula adherens by interacting
CC with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10-
CC binding protein TSPAN33. {ECO:0000269|PubMed:30463011}.
CC -!- SUBUNIT: Interacts with ATP2B1, ATP2B2, ATP2B3, ATP2B4 and ATP7A (By
CC similarity). Interacts with PLEKHA7 (via WW domains) at zonula
CC adherens; this interaction is essential for the interaction between
CC PLEKHA7 and the ADAM10-binding protein TSPAN33 (PubMed:30463011).
CC Interacts with SLC5A6 (By similarity). {ECO:0000250|UniProtKB:Q5EBL8,
CC ECO:0000269|PubMed:30463011}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5EBL8}. Cell
CC junction, adherens junction {ECO:0000269|PubMed:30463011}. Cell
CC membrane {ECO:0000269|PubMed:30463011}.
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; AK012624; BAB28364.1; -; mRNA.
DR EMBL; BC004608; AAH04608.1; -; mRNA.
DR CCDS; CCDS30304.1; -.
DR RefSeq; NP_082579.1; NM_028303.3.
DR RefSeq; XP_006528365.1; XM_006528302.2.
DR RefSeq; XP_011245987.1; XM_011247685.1.
DR PDB; 1WI2; NMR; -; A=37-127.
DR PDBsum; 1WI2; -.
DR AlphaFoldDB; Q9CZG9; -.
DR SMR; Q9CZG9; -.
DR BioGRID; 215475; 6.
DR IntAct; Q9CZG9; 2.
DR MINT; Q9CZG9; -.
DR STRING; 10090.ENSMUSP00000051068; -.
DR iPTMnet; Q9CZG9; -.
DR PhosphoSitePlus; Q9CZG9; -.
DR SwissPalm; Q9CZG9; -.
DR EPD; Q9CZG9; -.
DR MaxQB; Q9CZG9; -.
DR PaxDb; Q9CZG9; -.
DR PeptideAtlas; Q9CZG9; -.
DR PRIDE; Q9CZG9; -.
DR ProteomicsDB; 288119; -.
DR Antibodypedia; 581; 75 antibodies from 18 providers.
DR DNASU; 72621; -.
DR Ensembl; ENSMUST00000015812; ENSMUSP00000015812; ENSMUSG00000015668.
DR Ensembl; ENSMUST00000059099; ENSMUSP00000051068; ENSMUSG00000015668.
DR GeneID; 72621; -.
DR KEGG; mmu:72621; -.
DR UCSC; uc009twe.1; mouse.
DR CTD; 51248; -.
DR MGI; MGI:1919871; Pdzd11.
DR VEuPathDB; HostDB:ENSMUSG00000015668; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000153222; -.
DR HOGENOM; CLU_133335_0_0_1; -.
DR InParanoid; Q9CZG9; -.
DR OMA; ERIYHSD; -.
DR OrthoDB; 1530562at2759; -.
DR PhylomeDB; Q9CZG9; -.
DR TreeFam; TF318964; -.
DR Reactome; R-MMU-196780; Biotin transport and metabolism.
DR Reactome; R-MMU-199220; Vitamin B5 (pantothenate) metabolism.
DR Reactome; R-MMU-425397; Transport of vitamins, nucleosides, and related molecules.
DR Reactome; R-MMU-6803544; Ion influx/efflux at host-pathogen interface.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 72621; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Pdzd11; mouse.
DR EvolutionaryTrace; Q9CZG9; -.
DR PRO; PR:Q9CZG9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CZG9; protein.
DR Bgee; ENSMUSG00000015668; Expressed in right kidney and 256 other tissues.
DR Genevisible; Q9CZG9; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0046930; C:pore complex; IMP:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0046931; P:pore complex assembly; IMP:UniProtKB.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome.
FT CHAIN 1..140
FT /note="PDZ domain-containing protein 11"
FT /id="PRO_0000058274"
FT DOMAIN 47..129
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1WI2"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1WI2"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1WI2"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1WI2"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:1WI2"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:1WI2"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1WI2"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:1WI2"
SQ SEQUENCE 140 AA; 16182 MW; 621668278201EF7C CRC64;
MDNRIPYDDY PVVFLPAYEN PPAWIPPHER VYHPDYNNEL TQFLPRIVTL KKPPGAQLGF
NIRGGKASQL GIFISKVIPD SDAHRAGLQE GDQVLAVNDV DFQDIEHSKA VEILKTAREI
SMRVRFFPYN YHRQKERTVH
