MPDZ_HUMAN
ID MPDZ_HUMAN Reviewed; 2070 AA.
AC O75970; A6NLC2; B2RTS3; B7ZMI4; O43798; Q4LE30; Q5CZ80; Q5JTX3; Q5JTX6;
AC Q5JTX7; Q5JUC3; Q5JUC4; Q5VZ62; Q8N790;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Multiple PDZ domain protein;
DE AltName: Full=Multi-PDZ domain protein 1;
GN Name=MPDZ; Synonyms=MUPP1;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Eng L., Krapivinsky G., Clapham D.E.;
RT "Human homolog of MUPP1 protein.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 573-2070 (ISOFORM 1).
RC TISSUE=Amygdala;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1535-2070 (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1618-2070 (ISOFORM 1), TISSUE SPECIFICITY,
RP INTERACTION WITH HTR2C, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9537516; DOI=10.1016/s0014-5793(98)00141-0;
RA Ullmer C., Schmuck K., Figge A., Luebbert H.;
RT "Cloning and characterization of MUPP1, a novel PDZ domain protein.";
RL FEBS Lett. 424:63-68(1998).
RN [9]
RP INTERACTION WITH HUMAN ADENOVIRUS TYPE 9 E4-ORF1 PROTEIN (MICROBIAL
RP INFECTION) AND HUMAN PAPILLOMAVIRUS 18/HPV18 PROTEIN E6 (MICROBIAL
RP INFECTION).
RX PubMed=11000240; DOI=10.1128/jvi.74.20.9680-9693.2000;
RA Lee S.S., Glaunsinger B., Mantovani F., Banks L., Javier R.T.;
RT "Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus
RT E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins.";
RL J. Virol. 74:9680-9693(2000).
RN [10]
RP INTERACTION WITH HTR2A; HTR2B AND HTR2C, DOMAIN, AND FUNCTION.
RX PubMed=11150294; DOI=10.1074/jbc.m008089200;
RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J.,
RA Luebbert H., Ullmer C.;
RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10
RT of the multi-PDZ domain protein MUPP1.";
RL J. Biol. Chem. 276:12974-12982(2001).
RN [11]
RP INTERACTION WITH PLEKHA1 AND PLEKHA2, AND DOMAIN.
RX PubMed=11802782; DOI=10.1042/0264-6021:3610525;
RA Kimber W.A., Trinkle-Mulcahy L., Cheung P.C.F., Deak M., Marsden L.J.,
RA Kieloch A., Watt S., Javier R.T., Gray A., Downes C.P., Lucocq J.M.,
RA Alessi D.R.;
RT "Evidence that the tandem-pleckstrin-homology-domain-containing protein
RT TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-containing protein
RT MUPP1 in vivo.";
RL Biochem. J. 361:525-536(2002).
RN [12]
RP INTERACTION WITH CXADR, AND SUBCELLULAR LOCATION.
RX PubMed=15364909; DOI=10.1074/jbc.m409061200;
RA Coyne C.B., Voelker T., Pichla S.L., Bergelson J.M.;
RT "The coxsackievirus and adenovirus receptor interacts with the multi-PDZ
RT domain protein-1 (MUPP-1) within the tight junction.";
RL J. Biol. Chem. 279:48079-48084(2004).
RN [13]
RP INTERACTION WITH CRB1, AND SUBCELLULAR LOCATION.
RX PubMed=15316081; DOI=10.1242/jcs.01301;
RA van de Pavert S.A., Kantardzhieva A., Malysheva A., Meuleman J.,
RA Versteeg I., Levelt C., Klooster J., Geiger S., Seeliger M.W., Rashbass P.,
RA Le Bivic A., Wijnholds J.;
RT "Crumbs homologue 1 is required for maintenance of photoreceptor cell
RT polarization and adhesion during light exposure.";
RL J. Cell Sci. 117:4169-4177(2004).
RN [14]
RP INTERACTION WITH SYNGAP1; CAMK2A AND CAMK2B, MUTAGENESIS OF
RP 147-GLY--PHE-150, DOMAIN, AND FUNCTION.
RX PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
RA Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
RT "SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity
RT and NMDA receptor-dependent synaptic AMPA receptor potentiation.";
RL Neuron 43:563-574(2004).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP INVOLVEMENT IN HYC2, AND VARIANT HYC2 210-GLN--SER-2070 DEL.
RX PubMed=23240096; DOI=10.1136/jmedgenet-2012-101294;
RA Al-Dosari M.S., Al-Owain M., Tulbah M., Kurdi W., Adly N., Al-Hemidan A.,
RA Masoodi T.A., Albash B., Alkuraya F.S.;
RT "Mutation in MPDZ causes severe congenital hydrocephalus.";
RL J. Med. Genet. 50:54-58(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230 AND SER-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-790; SER-1078 AND
RP SER-1818, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP INVOLVEMENT IN HYC2, AND VARIANTS HYC2 210-GLN--SER-2070 DEL;
RP 744-ARG--SER-2070 DEL; 1071-ARG--SER-2070 DEL AND THR-1760.
RX PubMed=28556411; DOI=10.1002/ana.24964;
RA Shaheen R., Sebai M.A., Patel N., Ewida N., Kurdi W., Altweijri I.,
RA Sogaty S., Almardawi E., Seidahmed M.Z., Alnemri A., Madirevula S.,
RA Ibrahim N., Abdulwahab F., Hashem M., Al-Sheddi T., Alomar R., Alobeid E.,
RA Sallout B., AlBaqawi B., AlAali W., Ajaji N., Lesmana H., Hopkin R.J.,
RA Dupuis L., Mendoza-Londono R., Al Rukban H., Yoon G., Faqeih E.,
RA Alkuraya F.S.;
RT "The genetic landscape of familial congenital hydrocephalus.";
RL Ann. Neurol. 81:890-897(2017).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 117-227, X-RAY CRYSTALLOGRAPHY
RP (1.35 ANGSTROMS) OF 373-463, X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF
RP 1148-1243, X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1625-1716, X-RAY
RP CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1722-1806, X-RAY CRYSTALLOGRAPHY (1.7
RP ANGSTROMS) OF 1859-1951, AND X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF
RP 1983-2070.
RX PubMed=17384233; DOI=10.1110/ps.062657507;
RA Elkins J.M., Papagrigoriou E., Berridge G., Yang X., Phillips C.,
RA Gileadi C., Savitsky P., Doyle D.A.;
RT "Structure of PICK1 and other PDZ domains obtained with the help of self-
RT binding C-terminal extensions.";
RL Protein Sci. 16:683-694(2007).
CC -!- FUNCTION: Member of the NMDAR signaling complex that may play a role in
CC control of AMPAR potentiation and synaptic plasticity in excitatory
CC synapses (PubMed:11150294, PubMed:15312654). Promotes clustering of
CC HT2RC at the cell surface (By similarity).
CC {ECO:0000250|UniProtKB:O55164, ECO:0000269|PubMed:11150294,
CC ECO:0000269|PubMed:15312654}.
CC -!- SUBUNIT: Interacts with CLDN5, DLG4, GRIN1, F11R/JAM, CLDN1, NG2, CRB1,
CC MPP4 and PALS1 (By similarity). Interacts with HTR2A, HTR2B, HTR2C,
CC PLEKHA1/TAPP1, PLEKHA2/TAPP2, CXADR, SYNGAP1, CAMK2A and CAMK2B.
CC Interacts with FAT4 (via cytoplasmic domain) (By similarity). Interacts
CC with DLL1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8VBX6,
CC ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:11802782,
CC ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:15316081,
CC ECO:0000269|PubMed:15364909, ECO:0000269|PubMed:9537516}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus type 9
CC E4-ORF1 protein. {ECO:0000269|PubMed:11000240}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus
CC 18/HPV18 protein E6. {ECO:0000269|PubMed:11000240}.
CC -!- INTERACTION:
CC O75970; Q9H205: OR2AG1; NbExp=8; IntAct=EBI-821405, EBI-7590304;
CC O75970; Q9HB21: PLEKHA1; NbExp=6; IntAct=EBI-821405, EBI-2652984;
CC O75970; P32745: SSTR3; NbExp=5; IntAct=EBI-821405, EBI-6266935;
CC O75970; P04637: TP53; NbExp=3; IntAct=EBI-821405, EBI-366083;
CC O75970; Q9ERS5: Plekha2; Xeno; NbExp=5; IntAct=EBI-821405, EBI-8079166;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Apical cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Postsynaptic density. Cell projection, dendrite. Cell
CC junction, tight junction. Synapse. Synapse, synaptosome.
CC Note=Colocalizes with HTR2C on the apical membrane of epithelial
CC choroid plexus cells (By similarity). Highly enriched in postsynaptic
CC densities (PSD). Localized to punctae on dendrites of hippocampal
CC neurons and colocalizes with the synaptic marker DLG4. Localized mainly
CC in the Schmidt-Lanterman incisures of myelinating Schwann cells (By
CC similarity). In the retina, localizes to the sub-apical region adjacent
CC to the adherens junction complex at the outer limiting membrane.
CC Enriched at the tight junctions of epithelial cells. Association to the
CC tight junctions depends on CXADR. {ECO:0000250,
CC ECO:0000250|UniProtKB:O55164}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75970-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75970-2; Sequence=VSP_040451;
CC Name=3;
CC IsoId=O75970-3; Sequence=VSP_040450;
CC Name=4;
CC IsoId=O75970-5; Sequence=VSP_040450, VSP_040451;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, liver,
CC skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:9537516}.
CC -!- DOMAIN: The PDZ domain 1 binds NG2. The PDZ domains 7 and 10 bind the
CC Ad9 E4-ORF1 oncoprotein. The PDZ domain 9 binds F11R. The PDZ domain 10
CC binds the C-terminus of CLDN1 and KIT and the C-terminal PDZ-binding
CC motif of HTR2C. The PDZ domain 13 binds CXADR (By similarity). The PDZ
CC domain 2 binds CAMK2A and CAMK2B. The PDZ domains 10 and 13 bind
CC PLEKHA1 and PLEKHA2. The PDZ domain 13 binds SYNGAP1. {ECO:0000250,
CC ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:11802782,
CC ECO:0000269|PubMed:15312654}.
CC -!- DISEASE: Hydrocephalus, congenital, 2, with or without brain or eye
CC anomalies (HYC2) [MIM:615219]: A form of congenital hydrocephalus, a
CC disease characterized by onset in utero of enlarged ventricles due to
CC accumulation of ventricular cerebrospinal fluid. HYC2 affected
CC individuals have variable neurologic impairment. Some individuals have
CC other brain abnormalities, including lissencephaly, thinning of the
CC corpus callosum, and neuronal heterotopia. Most patients have delayed
CC motor development and some have delayed intellectual development and/or
CC seizures. Additional congenital features, including cardiac septal
CC defects, iris coloboma, and non-specific dysmorphic features, may be
CC observed. HYC2 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:23240096, ECO:0000269|PubMed:28556411}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC61870.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAC05409.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE06123.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI56786.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AF093419; AAC61870.1; ALT_SEQ; mRNA.
DR EMBL; AB210041; BAE06123.1; ALT_INIT; mRNA.
DR EMBL; AL161449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58704.1; -; Genomic_DNA.
DR EMBL; BC140793; AAI40794.1; -; mRNA.
DR EMBL; BC144564; AAI44565.1; -; mRNA.
DR EMBL; CR936648; CAI56786.1; ALT_SEQ; mRNA.
DR EMBL; AK098775; BAC05409.1; ALT_INIT; mRNA.
DR EMBL; AJ001319; CAA04680.1; -; mRNA.
DR CCDS; CCDS47951.1; -. [O75970-2]
DR CCDS; CCDS59119.1; -. [O75970-5]
DR CCDS; CCDS59120.1; -. [O75970-3]
DR CCDS; CCDS83342.1; -. [O75970-1]
DR RefSeq; NP_001248335.1; NM_001261406.1. [O75970-3]
DR RefSeq; NP_001248336.1; NM_001261407.1. [O75970-5]
DR RefSeq; NP_001317566.1; NM_001330637.1. [O75970-1]
DR RefSeq; NP_003820.2; NM_003829.4. [O75970-2]
DR RefSeq; XP_006716948.1; XM_006716885.3.
DR RefSeq; XP_006716949.1; XM_006716886.3. [O75970-1]
DR RefSeq; XP_006716950.1; XM_006716887.3. [O75970-1]
DR RefSeq; XP_006716951.1; XM_006716888.3. [O75970-2]
DR RefSeq; XP_006716952.1; XM_006716889.3.
DR RefSeq; XP_006716954.1; XM_006716891.3.
DR RefSeq; XP_016870742.1; XM_017015253.1. [O75970-5]
DR PDB; 2FCF; X-ray; 1.76 A; A=1148-1243.
DR PDB; 2FNE; X-ray; 1.83 A; A/B/C=1983-2070.
DR PDB; 2IWN; X-ray; 1.35 A; A=373-463.
DR PDB; 2IWO; X-ray; 1.70 A; A/B=1859-1951.
DR PDB; 2IWP; X-ray; 2.15 A; A/B=1859-1951.
DR PDB; 2IWQ; X-ray; 1.80 A; A=1148-1243.
DR PDB; 2O2T; X-ray; 2.70 A; A/B=117-227.
DR PDB; 2OPG; X-ray; 1.50 A; A/B=1625-1716.
DR PDB; 2QG1; X-ray; 1.40 A; A=1722-1806.
DR PDBsum; 2FCF; -.
DR PDBsum; 2FNE; -.
DR PDBsum; 2IWN; -.
DR PDBsum; 2IWO; -.
DR PDBsum; 2IWP; -.
DR PDBsum; 2IWQ; -.
DR PDBsum; 2O2T; -.
DR PDBsum; 2OPG; -.
DR PDBsum; 2QG1; -.
DR AlphaFoldDB; O75970; -.
DR SMR; O75970; -.
DR BioGRID; 114307; 81.
DR CORUM; O75970; -.
DR ELM; O75970; -.
DR IntAct; O75970; 45.
DR MINT; O75970; -.
DR STRING; 9606.ENSP00000439807; -.
DR iPTMnet; O75970; -.
DR PhosphoSitePlus; O75970; -.
DR BioMuta; MPDZ; -.
DR EPD; O75970; -.
DR jPOST; O75970; -.
DR MassIVE; O75970; -.
DR MaxQB; O75970; -.
DR PaxDb; O75970; -.
DR PeptideAtlas; O75970; -.
DR PRIDE; O75970; -.
DR ProteomicsDB; 50330; -. [O75970-1]
DR ProteomicsDB; 50331; -. [O75970-2]
DR ProteomicsDB; 50332; -. [O75970-3]
DR ProteomicsDB; 7263; -.
DR Antibodypedia; 4615; 89 antibodies from 19 providers.
DR DNASU; 8777; -.
DR Ensembl; ENST00000319217.12; ENSP00000320006.7; ENSG00000107186.17. [O75970-1]
DR Ensembl; ENST00000447879.6; ENSP00000415208.1; ENSG00000107186.17. [O75970-3]
DR Ensembl; ENST00000536827.5; ENSP00000444151.1; ENSG00000107186.17. [O75970-5]
DR Ensembl; ENST00000541718.5; ENSP00000439807.1; ENSG00000107186.17. [O75970-2]
DR GeneID; 8777; -.
DR KEGG; hsa:8777; -.
DR MANE-Select; ENST00000319217.12; ENSP00000320006.7; NM_001378778.1; NP_001365707.1.
DR UCSC; uc003zlb.5; human. [O75970-1]
DR CTD; 8777; -.
DR DisGeNET; 8777; -.
DR GeneCards; MPDZ; -.
DR HGNC; HGNC:7208; MPDZ.
DR HPA; ENSG00000107186; Tissue enhanced (liver).
DR MalaCards; MPDZ; -.
DR MIM; 603785; gene.
DR MIM; 615219; phenotype.
DR neXtProt; NX_O75970; -.
DR OpenTargets; ENSG00000107186; -.
DR Orphanet; 269505; Congenital communicating hydrocephalus.
DR PharmGKB; PA30914; -.
DR VEuPathDB; HostDB:ENSG00000107186; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000155586; -.
DR HOGENOM; CLU_002378_0_0_1; -.
DR InParanoid; O75970; -.
DR OMA; ADELLEX; -.
DR OrthoDB; 1419918at2759; -.
DR PhylomeDB; O75970; -.
DR TreeFam; TF330709; -.
DR PathwayCommons; O75970; -.
DR SignaLink; O75970; -.
DR BioGRID-ORCS; 8777; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; MPDZ; human.
DR EvolutionaryTrace; O75970; -.
DR GeneWiki; MPDZ; -.
DR GenomeRNAi; 8777; -.
DR Pharos; O75970; Tbio.
DR PRO; PR:O75970; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O75970; protein.
DR Bgee; ENSG00000107186; Expressed in calcaneal tendon and 191 other tissues.
DR ExpressionAtlas; O75970; baseline and differential.
DR Genevisible; O75970; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR Gene3D; 2.30.42.10; -; 13.
DR InterPro; IPR015132; L27_2.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR032078; MPDZ.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF09045; L27_2; 1.
DR Pfam; PF16667; MPDZ_u10; 1.
DR Pfam; PF00595; PDZ; 13.
DR SMART; SM00228; PDZ; 13.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50156; SSF50156; 13.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 13.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Cell projection; Host-virus interaction; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome;
KW Tight junction.
FT CHAIN 1..2070
FT /note="Multiple PDZ domain protein"
FT /id="PRO_0000094594"
FT DOMAIN 1..63
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 137..224
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 257..337
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 377..463
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 553..634
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 700..786
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1008..1089
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1151..1243
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1350..1433
FT /note="PDZ 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1483..1564
FT /note="PDZ 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1629..1712
FT /note="PDZ 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1725..1807
FT /note="PDZ 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1862..1948
FT /note="PDZ 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1987..2070
FT /note="PDZ 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1121..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1170
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VBX6"
FT MOD_RES 1818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55164"
FT VAR_SEQ 1248..1280
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040450"
FT VAR_SEQ 1794..1822
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_040451"
FT VARIANT 92
FT /note="S -> L (in dbSNP:rs17273542)"
FT /id="VAR_056115"
FT VARIANT 210..2070
FT /note="Missing (in HYC2; dbSNP:rs372127610)"
FT /evidence="ECO:0000269|PubMed:23240096,
FT ECO:0000269|PubMed:28556411"
FT /id="VAR_081122"
FT VARIANT 351
FT /note="L -> F (in dbSNP:rs3739757)"
FT /id="VAR_056116"
FT VARIANT 702
FT /note="E -> K (in dbSNP:rs4741289)"
FT /id="VAR_056117"
FT VARIANT 702
FT /note="E -> V (in dbSNP:rs4740548)"
FT /id="VAR_056118"
FT VARIANT 744..2070
FT /note="Missing (in HYC2; dbSNP:rs922703465)"
FT /evidence="ECO:0000269|PubMed:28556411"
FT /id="VAR_081123"
FT VARIANT 1071..2070
FT /note="Missing (in HYC2; dbSNP:rs376078512)"
FT /evidence="ECO:0000269|PubMed:28556411"
FT /id="VAR_081124"
FT VARIANT 1604
FT /note="T -> A (in dbSNP:rs16930134)"
FT /id="VAR_056119"
FT VARIANT 1663
FT /note="G -> R (in dbSNP:rs2274648)"
FT /id="VAR_056120"
FT VARIANT 1760
FT /note="A -> T (in HYC2; unknown pathological significance;
FT dbSNP:rs1554644827)"
FT /evidence="ECO:0000269|PubMed:28556411"
FT /id="VAR_081125"
FT MUTAGEN 147..150
FT /note="GLGF->PSES: Loss of interaction with CAMK2A."
FT /evidence="ECO:0000269|PubMed:15312654"
FT CONFLICT 1950
FT /note="V -> M (in Ref. 6; CAI56786)"
FT /evidence="ECO:0000305"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:2O2T"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:2O2T"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2O2T"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2O2T"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:2O2T"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:2O2T"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2O2T"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:2O2T"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:2O2T"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:2IWN"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:2IWN"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:2IWN"
FT HELIX 415..419
FT /evidence="ECO:0007829|PDB:2IWN"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:2IWN"
FT HELIX 441..449
FT /evidence="ECO:0007829|PDB:2IWN"
FT STRAND 453..463
FT /evidence="ECO:0007829|PDB:2IWN"
FT STRAND 1150..1154
FT /evidence="ECO:0007829|PDB:2FCF"
FT STRAND 1164..1167
FT /evidence="ECO:0007829|PDB:2FCF"
FT STRAND 1185..1190
FT /evidence="ECO:0007829|PDB:2FCF"
FT STRAND 1192..1194
FT /evidence="ECO:0007829|PDB:2FCF"
FT HELIX 1195..1199
FT /evidence="ECO:0007829|PDB:2FCF"
FT STRAND 1207..1211
FT /evidence="ECO:0007829|PDB:2FCF"
FT HELIX 1221..1229
FT /evidence="ECO:0007829|PDB:2FCF"
FT STRAND 1233..1240
FT /evidence="ECO:0007829|PDB:2FCF"
FT STRAND 1626..1633
FT /evidence="ECO:0007829|PDB:2OPG"
FT STRAND 1641..1645
FT /evidence="ECO:0007829|PDB:2OPG"
FT STRAND 1653..1659
FT /evidence="ECO:0007829|PDB:2OPG"
FT HELIX 1664..1668
FT /evidence="ECO:0007829|PDB:2OPG"
FT STRAND 1676..1680
FT /evidence="ECO:0007829|PDB:2OPG"
FT HELIX 1690..1698
FT /evidence="ECO:0007829|PDB:2OPG"
FT STRAND 1702..1710
FT /evidence="ECO:0007829|PDB:2OPG"
FT STRAND 1723..1729
FT /evidence="ECO:0007829|PDB:2QG1"
FT STRAND 1737..1741
FT /evidence="ECO:0007829|PDB:2QG1"
FT STRAND 1744..1746
FT /evidence="ECO:0007829|PDB:2QG1"
FT STRAND 1750..1754
FT /evidence="ECO:0007829|PDB:2QG1"
FT HELIX 1759..1763
FT /evidence="ECO:0007829|PDB:2QG1"
FT STRAND 1771..1775
FT /evidence="ECO:0007829|PDB:2QG1"
FT HELIX 1785..1794
FT /evidence="ECO:0007829|PDB:2QG1"
FT STRAND 1797..1804
FT /evidence="ECO:0007829|PDB:2QG1"
FT STRAND 1861..1866
FT /evidence="ECO:0007829|PDB:2IWO"
FT TURN 1869..1871
FT /evidence="ECO:0007829|PDB:2IWO"
FT STRAND 1875..1883
FT /evidence="ECO:0007829|PDB:2IWO"
FT STRAND 1886..1895
FT /evidence="ECO:0007829|PDB:2IWO"
FT HELIX 1900..1904
FT /evidence="ECO:0007829|PDB:2IWO"
FT STRAND 1912..1916
FT /evidence="ECO:0007829|PDB:2IWO"
FT HELIX 1926..1935
FT /evidence="ECO:0007829|PDB:2IWO"
FT STRAND 1938..1945
FT /evidence="ECO:0007829|PDB:2IWO"
FT STRAND 1984..1990
FT /evidence="ECO:0007829|PDB:2FNE"
FT STRAND 1998..2007
FT /evidence="ECO:0007829|PDB:2FNE"
FT STRAND 2010..2019
FT /evidence="ECO:0007829|PDB:2FNE"
FT HELIX 2024..2028
FT /evidence="ECO:0007829|PDB:2FNE"
FT STRAND 2036..2040
FT /evidence="ECO:0007829|PDB:2FNE"
FT HELIX 2050..2059
FT /evidence="ECO:0007829|PDB:2FNE"
FT STRAND 2062..2070
FT /evidence="ECO:0007829|PDB:2FNE"
SQ SEQUENCE 2070 AA; 221618 MW; A4D304C20401FD45 CRC64;
MLEAIDKNRA LHAAERLQTK LRERGDVANE DKLSLLKSVL QSPLFSQILS LQTSVQQLKD
QVNIATSATS NIEYAHVPHL SPAVIPTLQN ESFLLSPNNG NLEALTGPGI PHINGKPACD
EFDQLIKNMA QGRHVEVFEL LKPPSGGLGF SVVGLRSENR GELGIFVQEI QEGSVAHRDG
RLKETDQILA INGQALDQTI THQQAISILQ KAKDTVQLVI ARGSLPQLVS PIVSRSPSAA
STISAHSNPV HWQHMETIEL VNDGSGLGFG IIGGKATGVI VKTILPGGVA DQHGRLCSGD
HILKIGDTDL AGMSSEQVAQ VLRQCGNRVK LMIARGAIEE RTAPTALGIT LSSSPTSTPE
LRVDASTQKG EESETFDVEL TKNVQGLGIT IAGYIGDKKL EPSGIFVKSI TKSSAVEHDG
RIQIGDQIIA VDGTNLQGFT NQQAVEVLRH TGQTVLLTLM RRGMKQEAEL MSREDVTKDA
DLSPVNASII KENYEKDEDF LSSTRNTNIL PTEEEGYPLL SAEIEEIEDA QKQEAALLTK
WQRIMGINYE IVVAHVSKFS ENSGLGISLE ATVGHHFIRS VLPEGPVGHS GKLFSGDELL
EVNGITLLGE NHQDVVNILK ELPIEVTMVC CRRTVPPTTQ SELDSLDLCD IELTEKPHVD
LGEFIGSSET EDPVLAMTDA GQSTEEVQAP LAMWEAGIQH IELEKGSKGL GFSILDYQDP
IDPASTVIII RSLVPGGIAE KDGRLLPGDR LMFVNDVNLE NSSLEEAVEA LKGAPSGTVR
IGVAKPLPLS PEEGYVSAKE DSFLYPPHSC EEAGLADKPL FRADLALVGT NDADLVDEST
FESPYSPEND SIYSTQASIL SLHGSSCGDG LNYGSSLPSS PPKDVIENSC DPVLDLHMSL
EELYTQNLLQ RQDENTPSVD ISMGPASGFT INDYTPANAI EQQYECENTI VWTESHLPSE
VISSAELPSV LPDSAGKGSE YLLEQSSLAC NAECVMLQNV SKESFERTIN IAKGNSSLGM
TVSANKDGLG MIVRSIIHGG AISRDGRIAI GDCILSINEE STISVTNAQA RAMLRRHSLI
GPDIKITYVP AEHLEEFKIS LGQQSGRVMA LDIFSSYTGR DIPELPEREE GEGEESELQN
TAYSNWNQPR RVELWREPSK SLGISIVGGR GMGSRLSNGE VMRGIFIKHV LEDSPAGKNG
TLKPGDRIVE VDGMDLRDAS HEQAVEAIRK AGNPVVFMVQ SIINRPRKSP LPSLLHNLYP
KYNFSSTNPF ADSLQINADK APSQSESEPE KAPLCSVPPP PPSAFAEMGS DHTQSSASKI
SQDVDKEDEF GYSWKNIRER YGTLTGELHM IELEKGHSGL GLSLAGNKDR SRMSVFIVGI
DPNGAAGKDG RLQIADELLE INGQILYGRS HQNASSIIKC APSKVKIIFI RNKDAVNQMA
VCPGNAVEPL PSNSENLQNK ETEPTVTTSD AAVDLSSFKN VQHLELPKDQ GGLGIAISEE
DTLSGVIIKS LTEHGVAATD GRLKVGDQIL AVDDEIVVGY PIEKFISLLK TAKMTVKLTI
HAENPDSQAV PSAAGAASGE KKNSSQSLMV PQSGSPEPES IRNTSRSSTP AIFASDPATC
PIIPGCETTI EISKGRTGLG LSIVGGSDTL LGAIIIHEVY EEGAACKDGR LWAGDQILEV
NGIDLRKATH DEAINVLRQT PQRVRLTLYR DEAPYKEEEV CDTLTIELQK KPGKGLGLSI
VGKRNDTGVF VSDIVKGGIA DADGRLMQGD QILMVNGEDV RNATQEAVAA LLKCSLGTVT
LEVGRIKAGP FHSERRPSQS SQVSEGSLSS FTFPLSGSST SESLESSSKK NALASEIQGL
RTVEMKKGPT DSLGISIAGG VGSPLGDVPI FIAMMHPTGV AAQTQKLRVG DRIVTICGTS
TEGMTHTQAV NLLKNASGSI EMQVVAGGDV SVVTGHQQEP ASSSLSFTGL TSSSIFQDDL
GPPQCKSITL ERGPDGLGFS IVGGYGSPHG DLPIYVKTVF AKGAASEDGR LKRGDQIIAV
NGQSLEGVTH EEAVAILKRT KGTVTLMVLS
