PDZ11_HUMAN
ID PDZ11_HUMAN Reviewed; 140 AA.
AC Q5EBL8; D3DVU3; Q6UWE1; Q9P0Q1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=PDZ domain-containing protein 11;
DE AltName: Full=ATPase-interacting PDZ protein;
DE AltName: Full=Plasma membrane calcium ATPase-interacting single-PDZ protein;
DE Short=PMCA-interacting single-PDZ protein;
GN Name=PDZD11; Synonyms=AIPP1, PDZK11, PISP;
GN ORFNames=HSPC227, UNQ6486/PRO21335;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Artery smooth muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Chondrosarcoma, and Muscle;
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 [9]
RP INTERACTION WITH ATP2B1; ATP2B2; ATP2B3 AND ATP2B4, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=12763866; DOI=10.1111/j.1749-6632.2003.tb07230.x;
RA Goellner G.M., DeMarco S.J., Strehler E.E.;
RT "Characterization of PISP, a novel single-PDZ protein that binds to all
RT plasma membrane Ca2+-ATPase b-splice variants.";
RL Ann. N. Y. Acad. Sci. 986:461-471(2003).
RN [10]
RP INTERACTION WITH ATP7A, AND IDENTIFICATION OF ALTERNATIVE SPLICING
RP (ISOFORMS 1 AND 2).
RX PubMed=16051599; DOI=10.1074/jbc.m505889200;
RA Stephenson S.E., Dubach D., Lim C.M., Mercer J.F., La Fontaine S.;
RT "A single PDZ domain protein interacts with the Menkes copper ATPase,
RT ATP7A. A new protein implicated in copper homeostasis.";
RL J. Biol. Chem. 280:33270-33279(2005).
RN [11]
RP INTERACTION WITH SLC5A6.
RX PubMed=21183659; DOI=10.1152/ajpgi.00530.2010;
RA Nabokina S.M., Subramanian V.S., Said H.M.;
RT "Association of PDZ-containing protein PDZD11 with the human sodium-
RT dependent multivitamin transporter.";
RL Am. J. Physiol. 300:G561-G567(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
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 [14]
RP VARIANT TYR-81.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
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
CC (PubMed:12763866, PubMed:16051599). Interacts with PLEKHA7 (via WW
CC domains) at zonula adherens; this interaction is essential for the
CC interaction between PLEKHA7 and the ADAM10-binding protein TSPAN33
CC (PubMed:30463011). Interacts with SLC5A6 (PubMed:21183659).
CC {ECO:0000269|PubMed:12763866, ECO:0000269|PubMed:16051599,
CC ECO:0000269|PubMed:21183659, ECO:0000269|PubMed:30463011}.
CC -!- INTERACTION:
CC Q5EBL8; Q04656: ATP7A; NbExp=4; IntAct=EBI-1644207, EBI-7706409;
CC Q5EBL8; Q86UL8-2: MAGI2; NbExp=3; IntAct=EBI-1644207, EBI-12081182;
CC Q5EBL8; Q9HAU0: PLEKHA5; NbExp=11; IntAct=EBI-1644207, EBI-945934;
CC Q5EBL8; Q9Y289: SLC5A6; NbExp=6; IntAct=EBI-1644207, EBI-3915941;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:12763866}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:30463011}. Cell membrane
CC {ECO:0000269|PubMed:30463011}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AIPP1a;
CC IsoId=Q5EBL8-1; Sequence=Displayed;
CC Name=2; Synonyms=AIPP1b;
CC IsoId=Q5EBL8-2; Sequence=VSP_015077;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:12763866}.
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DR EMBL; AF151061; AAF36147.1; -; mRNA.
DR EMBL; AY358829; AAQ89188.1; -; mRNA.
DR EMBL; AK024746; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR457149; CAG33430.1; -; mRNA.
DR EMBL; BX537725; CAD97820.1; -; mRNA.
DR EMBL; AL357752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05345.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05346.1; -; Genomic_DNA.
DR EMBL; BC012996; AAH12996.1; -; mRNA.
DR EMBL; BC089433; AAH89433.1; -; mRNA.
DR CCDS; CCDS14400.1; -. [Q5EBL8-1]
DR RefSeq; NP_057568.1; NM_016484.4. [Q5EBL8-1]
DR RefSeq; XP_011529275.1; XM_011530973.2.
DR RefSeq; XP_016885057.1; XM_017029568.1.
DR AlphaFoldDB; Q5EBL8; -.
DR SMR; Q5EBL8; -.
DR BioGRID; 119405; 46.
DR CORUM; Q5EBL8; -.
DR IntAct; Q5EBL8; 25.
DR MINT; Q5EBL8; -.
DR STRING; 9606.ENSP00000239666; -.
DR iPTMnet; Q5EBL8; -.
DR PhosphoSitePlus; Q5EBL8; -.
DR BioMuta; PDZD11; -.
DR DMDM; 73621365; -.
DR EPD; Q5EBL8; -.
DR jPOST; Q5EBL8; -.
DR MassIVE; Q5EBL8; -.
DR MaxQB; Q5EBL8; -.
DR PaxDb; Q5EBL8; -.
DR PeptideAtlas; Q5EBL8; -.
DR PRIDE; Q5EBL8; -.
DR ProteomicsDB; 62764; -. [Q5EBL8-1]
DR ProteomicsDB; 62765; -. [Q5EBL8-2]
DR Antibodypedia; 581; 75 antibodies from 18 providers.
DR DNASU; 51248; -.
DR Ensembl; ENST00000239666.9; ENSP00000239666.4; ENSG00000120509.11. [Q5EBL8-1]
DR Ensembl; ENST00000374454.1; ENSP00000363578.1; ENSG00000120509.11. [Q5EBL8-1]
DR GeneID; 51248; -.
DR KEGG; hsa:51248; -.
DR MANE-Select; ENST00000239666.9; ENSP00000239666.4; NM_016484.5; NP_057568.1.
DR UCSC; uc004dyd.2; human. [Q5EBL8-1]
DR CTD; 51248; -.
DR GeneCards; PDZD11; -.
DR HGNC; HGNC:28034; PDZD11.
DR HPA; ENSG00000120509; Low tissue specificity.
DR MIM; 300632; gene.
DR neXtProt; NX_Q5EBL8; -.
DR OpenTargets; ENSG00000120509; -.
DR PharmGKB; PA134968632; -.
DR VEuPathDB; HostDB:ENSG00000120509; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000153222; -.
DR HOGENOM; CLU_133335_0_0_1; -.
DR InParanoid; Q5EBL8; -.
DR OMA; ERIYHSD; -.
DR OrthoDB; 1530562at2759; -.
DR PhylomeDB; Q5EBL8; -.
DR TreeFam; TF318964; -.
DR PathwayCommons; Q5EBL8; -.
DR Reactome; R-HSA-196780; Biotin transport and metabolism.
DR Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
DR Reactome; R-HSA-425397; Transport of vitamins, nucleosides, and related molecules.
DR Reactome; R-HSA-6803544; Ion influx/efflux at host-pathogen interface.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; Q5EBL8; -.
DR SIGNOR; Q5EBL8; -.
DR BioGRID-ORCS; 51248; 15 hits in 713 CRISPR screens.
DR ChiTaRS; PDZD11; human.
DR GeneWiki; PDZD11; -.
DR GenomeRNAi; 51248; -.
DR Pharos; Q5EBL8; Tbio.
DR PRO; PR:Q5EBL8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5EBL8; protein.
DR Bgee; ENSG00000120509; Expressed in ileal mucosa and 181 other tissues.
DR Genevisible; Q5EBL8; HS.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPI: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 Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome; Secreted.
FT CHAIN 1..140
FT /note="PDZ domain-containing protein 11"
FT /id="PRO_0000058273"
FT DOMAIN 47..129
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT VAR_SEQ 1
FT /note="M -> MGWSCCLKLAGLLSLLNHFLSVLIHSSRALPE (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_015077"
FT VARIANT 81
FT /note="S -> Y (in dbSNP:rs1245281228)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069422"
SQ SEQUENCE 140 AA; 16131 MW; 601216B821A36DCE CRC64;
MDSRIPYDDY PVVFLPAYEN PPAWIPPHER VHHPDYNNEL TQFLPRTITL KKPPGAQLGF
NIRGGKASQL GIFISKVIPD SDAHRAGLQE GDQVLAVNDV DFQDIEHSKA VEILKTAREI
SMRVRFFPYN YHRQKERTVH
