PDZD2_RAT
ID PDZD2_RAT Reviewed; 2766 AA.
AC Q9QZR8;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 02-JUN-2021, entry version 113.
DE RecName: Full=PDZ domain-containing protein 2;
DE AltName: Full=PDZ domain-containing protein 3;
DE AltName: Full=Plakophilin-related armadillo repeat protein-interacting PDZ protein;
DE Contains:
DE RecName: Full=Processed PDZ domain-containing protein 2;
GN Name=Pdzd2; Synonyms=Papin, Pdzk3, Pin1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CTNND2 AND PKP4, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=10896674; DOI=10.1074/jbc.m005384200;
RA Deguchi M., Iizuka T., Hata Y., Nishimura W., Hirao K., Yao I., Kawabe H.,
RA Takai Y.;
RT "A novel multiple PSD-95/Dlg-A/ZO-1 protein interacting with neural
RT plakophilin-related armadillo repeat protein/delta-catenin and p0071.";
RL J. Biol. Chem. 275:29875-29880(2000).
RN [2]
RP SITE CRITICAL TO PROTEOLYSIS, MUTAGENESIS OF ASP-2402 AND ASP-2404,
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12671685; DOI=10.1038/sj.embor.embor804;
RA Yeung M.-L., Tam T.S.M., Tsang A.C.C., Yao K.-M.;
RT "Proteolytic cleavage of PDZD2 generates a secreted peptide containing two
RT PDZ domains.";
RL EMBO Rep. 4:412-418(2003).
RN [3]
RP INTERACTION WITH SCN10A.
RX PubMed=12591166; DOI=10.1016/s0169-328x(02)00661-7;
RA Malik-Hall M., Poon W.-Y.L., Baker M.D., Wood J.N., Okuse K.;
RT "Sensory neuron proteins interact with the intracellular domains of sodium
RT channel NaV1.8.";
RL Brain Res. Mol. Brain Res. 110:298-304(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; SER-891; SER-895 AND
RP SER-1767, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBUNIT: Interacts with SCN10A, CTNND2 and PKP4.
CC {ECO:0000269|PubMed:10896674, ECO:0000269|PubMed:12591166}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12671685}. Cytoplasm
CC {ECO:0000250|UniProtKB:O15018}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:12671685}. Cell junction
CC {ECO:0000269|PubMed:10896674}. Note=At cell-cell contacts in lung
CC epithelial cells (PubMed:10896674).
CC -!- SUBCELLULAR LOCATION: [Processed PDZ domain-containing protein 2]:
CC Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in the heart, liver, brain, spleen, lung,
CC kidney, testis and skeletal muscle. {ECO:0000269|PubMed:10896674,
CC ECO:0000269|PubMed:12671685}.
CC -!- PTM: A secreted form is produced by caspase-mediated proteolytic
CC cleavage.
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DR EMBL; AF169411; AAD55940.1; -; mRNA.
DR RefSeq; NP_075229.1; NM_022940.1.
DR SMR; Q9QZR8; -.
DR IntAct; Q9QZR8; 2.
DR MINT; Q9QZR8; -.
DR STRING; 10116.ENSRNOP00000017937; -.
DR iPTMnet; Q9QZR8; -.
DR PhosphoSitePlus; Q9QZR8; -.
DR SwissPalm; Q9QZR8; -.
DR PaxDb; Q9QZR8; -.
DR PRIDE; Q9QZR8; -.
DR GeneID; 65034; -.
DR KEGG; rno:65034; -.
DR CTD; 23037; -.
DR RGD; 619958; Pdzd2.
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; Q9QZR8; -.
DR OrthoDB; 225688at2759; -.
DR PhylomeDB; Q9QZR8; -.
DR PRO; PR:Q9QZR8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
DR Gene3D; 2.30.42.10; -; 6.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 5.
DR SMART; SM00228; PDZ; 6.
DR SUPFAM; SSF50156; SSF50156; 6.
DR PROSITE; PS50106; PDZ; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cytoplasm; Endoplasmic reticulum; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Secreted.
FT CHAIN 1..2766
FT /note="PDZ domain-containing protein 2"
FT /id="PRO_0000058295"
FT CHAIN ?2403..2766
FT /note="Processed PDZ domain-containing protein 2"
FT /id="PRO_0000302757"
FT DOMAIN 85..177
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 334..419
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 535..621
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 679..764
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 2550..2634
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 2678..2763
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 189..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..1909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1924..1967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2015..2070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2146..2174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2262..2397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2424..2450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2465..2496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2635..2667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..1860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2056..2070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2262..2350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2360..2394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2428..2442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2465..2479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 2402..2403
FT /note="Cleavage; by caspases"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 2402..2411
FT /note="DLDKLCNGED->I: Loss of proteolytic cleavage."
FT MUTAGEN 2402
FT /note="D->A: Loss of proteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:12671685"
FT MUTAGEN 2404
FT /note="D->A: No loss of proteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:12671685"
SQ SEQUENCE 2766 AA; 293890 MW; 1DC34DF7B4A6D1DD CRC64;
MPITQDNALL HLPLLYEWLQ NSLREGGDSP EQRLCQAAIQ KLQEYIQLNL AVDESTVPPD
HSPPEMEICT VYLTKQLGDT ETVGLSFGNI PVFGDYGEKR RGGKKRKTHQ GPVLDVGCIW
VTELRKNSPA GKSGKVRLRD EILSLNGQLM VGVDVTGASY LAEQCWNGGF IYLIMLRRFK
QKAHVTYNGN SGNSSEPGET PTLELGDQTS KKGKRTRKFG VISRPSISKT PEDSKSSSGC
DTADDPNSEL ENGADPELGN GHAFELENGP HSLKDVAGPH LERSEADSEV ELRVPKTEAP
LSDSNDKRRF SKTGKTDFQS SDCLAREEVG RIWKMELLKE SDGLGIQVSG GRGSKRSPHA
IVVTQVKEGG AAHRDGRLSL GDELLVINGH LLVGLSHEEA VAILRSATGM VQLVVASKMP
GSEESQDVGS SEESKGNLES PKQGNCKTKL KSRLSGGVHR LESVEEYNEL MVRNGDPRIR
MLEVSRDGRK HSLPQLLDST GTSQEYHIVK KSTRSLSTTH VESPWRLIRP SVISIIGLYK
EKGKGLGFSI AGGRDCIRGQ MGIFVKTIFP NGSAAEDGRL KEGDEILDVN GIPIKGLTFQ
EAIHTFKQIR SGLFVLTVRT KLLSPSLTPC STPTHMSRSS SPSFNTNSGG TPAGGGQEEG
GSSSLGRKAP GPKDRIVMEV TLNKEPRVGL GIGACCLALE NSPPGIYIHS LAPGSVAKME
SNLSRGDQIL EVNSVNVRHA ALSKVHAILS KCPPGPVRLV IGRHPNPKVS EQEMDEVIAR
STYQESREAN SSPGLGTPLK SPSLAKKDSL LSESELSQYF VHDGQGSLSD FVVAGSEDED
HPGSGYETSE DGSLLPVPSA HKARANSLVT LGSQRTSGLL HKQVTVARQA SLPGSPQVLR
NPLLRQRRVR CYDSNGGSDD EDFDGEGDCI SLPGVLPGPG KPLVEDDTRP ALTTSSKSID
VNKQEERLQK PLVSKACSVP LLGSSLDSEH SILNGAGGTP PKVASLPGSG ETPKNGPRGS
GRKEMSGSRS SPKLEYRVPT DTQSPRSPEN HTSPPQKSEN LVSRHKPVAR ISPHYKRSDA
EEAPGGTANG PCAQDLKVQA SPVKDPVTSR QPGGTAEKEL RGNPTPGDSS VPTNCGPAST
PCHPNIGLPT ENPQGAAPEC GPHPGTGWDG SSEHLCSPGK SREVHPDSSE TPTVAEQVHQ
PESLSQPVSP RTSEPESQGI SKMKPPSQRC VSPREKASTP PDSSRAWAAP GDSSPSTRRI
AVPMSTGAAP ATAIPQASLV SQERSRGLSG PSKGLGTKEL CIPKSLKDGA LLEDTAPASG
KMSHASSPSG PVATERTLSG SPENPVTDID NFIEEASEAR LSQSPQKADC RAHGDTFESQ
PPGGAGSSSS HHAQMVRSDQ TSSPRKTGGT GSPPPQQWAL QPSVLDSIHP DKHLAVNKTF
LNNYSRNFSN FHEDSISLSG PGGSSEPSPS SMYGNAEDSS SDPESLAEDP GAAARNNWSP
PLSPESSPKE GSSESEDERI EICSTDGCPG TPVTAPPPTQ VALCPVLPVQ QRAVCKPVGD
ICERACFVPG ASRTSIPDSS QPFSFLDVSS EEPETWASIN ASQNHMPVCT EGIMDVTSTS
SNMGDSQSSQ MTRHCRNAPF VLGNPDMVND LGRDLLDEGA PKEGAAAASV MRSVFALGAE
GPKNGEAVLA DLHIAERGNL EDLLQKPKTI SRRPILTWFK EINKDSQGSH LRSTSEKEQS
SMLALGPGSK ANMVNTGHRK GVTVPKSPPS RQKSQENKDL PPKSPVETLG NCQKPKCSPK
LKRLNSKGKA SPEVPVAIST KGSRNDHRKT LPSPQASHKM FSKAVSHRLH IADQEEPKNT
AGDTPKPPQC VPESKPPQAA LGSLRTSASD TSIRTFTSPL TSPKLLPEQG ANSRFHMAVY
LESDTSCPTT SRSPRSGPEG KAPHANSGSA SPPASRASLA LAGIRQSKQF TPGRADLLVS
EATQPQGICE KGAEKKVSDP PQRTNQLKIV EISSERVPKN ACGDRPPESD RKGGFLTQNN
CQEKSAIRLR QSEESSPEHT PFPPSQASQV EREIRWSFSM AKPATSSSSS LQLPAKLPES
FQGKSSQMPA SVGVPKNGVP IGLAGEESPY FTPRPATRTY SMPAQFSSHF GREGPSPHSP
SHSPQDPQVP AMGGKLSEKT AKGVTNGQGV YSVKPLLETS KNLSPVDGRD VSADPETSCL
IPDKVKVTRR QYCCEQSWPH ESTSFFSVKQ RIKSFENLAN SDRPTAKCAT SPFLSVSSKP
PINRRSSGSI PSGSPSDMTS RSLRRSLSSC SESQSEASSL LPQMTKSPSS MTLTVSRQNP
PDTSNKGPSP DPKKSLVPVG IPTSTVSPAS PSKRNKSSVR HAQPSPVSRS KLQERRTLSM
PDLDKLCNGE DDSASPGAVL FKTQLEITPR RSKGSQATSP AGSPARGHAD FNGSTFLSCP
MNGGTRAYTK GNSPPASEPA IATGSREEGE SVWATPSGKS WSVSLDRLLA SVGNQQRLQG
ILSLVGSKSP ILTLIQEAKA QSETKEDICF IVLNKKEGSG LGFSVAGGAD VEPKSVMVHR
VFSQGVASQE GTVSRGDFLL SVNGTSLAGL AHSEVTKVLH QAELHKHALM IIKKGNDQPG
PSFKQEPPSA NGKGPFPRRT LPLEPGAGRN GAAHDALCVE VLKTSAGLGL SLDGGKSSVS
GEGPLVIKRV YKGGAAERAG TIEAGDEILA INGKPLVGLV HFDAWNIMKS VPEGPVQLVI
RKHRDS
