DEND_MOUSE
ID DEND_MOUSE Reviewed; 710 AA.
AC Q80TS7; Q3TPT2; Q3TY46;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Dendrin;
GN Name=Ddn; Synonyms=Gm748, Kiaa0749;
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=Hippocampus, and Visual cortex;
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-710.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-710.
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17251388; DOI=10.1681/asn.2006060675;
RA Patrakka J., Xiao Z., Nukui M., Takemoto M., He L., Oddsson A., Perisic L.,
RA Kaukinen A., Szigyarto C.A.-K., Uhlen M., Jalanko H., Betsholtz C.,
RA Tryggvason K.;
RT "Expression and subcellular distribution of novel glomerulus-associated
RT proteins Dendrin, Ehd3, Sh2d4a, Plekhh2, and 2310066E14Rik.";
RL J. Am. Soc. Nephrol. 18:689-697(2007).
RN [6]
RP FUNCTION, INTERACTION WITH CD2AP; NPHS1 AND NPHS2, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=17537921; DOI=10.1073/pnas.0700917104;
RA Asanuma K., Campbell K.N., Kim K., Faul C., Mundel P.;
RT "Nuclear relocation of the nephrin and CD2AP-binding protein dendrin
RT promotes apoptosis of podocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10134-10139(2007).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=18356187; DOI=10.1093/ndt/gfn100;
RA Duner F., Patrakka J., Xiao Z., Larsson J., Vlamis-Gardikas A.,
RA Pettersson E., Tryggvason K., Hultenby K., Wernerson A.;
RT "Dendrin expression in glomerulogenesis and in human minimal change
RT nephrotic syndrome.";
RL Nephrol. Dial. Transplant. 23:2504-2511(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Promotes apoptosis of kidney glomerular podocytes. Podocytes
CC are highly specialized cells essential to the ultrafiltration of blood,
CC resulting in the extraction of urine and the retention of protein.
CC {ECO:0000269|PubMed:17537921}.
CC -!- SUBUNIT: Forms a ternary complex with MAGI2 and SH3KBP1; recruits DDN
CC to the cytoplasm (By similarity). Interacts with MAGI1 (By similarity).
CC Interacts with ACTN1 and may interact with WWC1 (By similarity).
CC Interacts with the podocyte slit diaphragm proteins CD2AP, NPHS1 and
CC NPHS2; the interaction with CD2AP and NPHS1 is direct. {ECO:0000250,
CC ECO:0000269|PubMed:17537921}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm.
CC Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Perikaryon
CC {ECO:0000250}. Nucleus. Note=Enriched at the cytoplasmic insertion of
CC the slit diaphragm into the foot process of podocytes and associated
CC with polyribosomes in dendrites. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Two forms of 81 kDa and 89 kDa are expressed in
CC brain. The 81 kDa form is the only one found in kidney podocytes.
CC {ECO:0000269|PubMed:17251388, ECO:0000269|PubMed:17537921}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing podocytes during
CC glomerulogenesis. {ECO:0000269|PubMed:18356187}.
CC -!- MISCELLANEOUS: The 81 and 89 kDa forms are detected by an antibody
CC raised against a C-terminal peptide arguing for alternative N-terminal
CC sequences.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI57996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI57997.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE34717.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EDL04165.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK158894; BAE34717.1; ALT_INIT; mRNA.
DR EMBL; AK164154; BAE37653.1; -; mRNA.
DR EMBL; CH466550; EDL04165.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK122363; BAC65645.1; -; mRNA.
DR EMBL; BC157995; AAI57996.1; ALT_INIT; mRNA.
DR EMBL; BC157996; AAI57997.1; ALT_INIT; mRNA.
DR CCDS; CCDS49723.1; -.
DR RefSeq; NP_001013763.1; NM_001013741.1.
DR PDB; 6J69; X-ray; 2.75 A; B=222-246.
DR PDB; 6JJZ; X-ray; 1.65 A; C/D=222-235.
DR PDB; 6JK0; X-ray; 3.10 A; A=222-241.
DR PDB; 6JK1; X-ray; 2.00 A; A/B=222-241.
DR PDB; 6KKG; X-ray; 2.15 A; C/D=222-241.
DR PDB; 7BQG; X-ray; 1.55 A; A=225-235.
DR PDBsum; 6J69; -.
DR PDBsum; 6JJZ; -.
DR PDBsum; 6JK0; -.
DR PDBsum; 6JK1; -.
DR PDBsum; 6KKG; -.
DR PDBsum; 7BQG; -.
DR AlphaFoldDB; Q80TS7; -.
DR SMR; Q80TS7; -.
DR BioGRID; 199079; 2.
DR IntAct; Q80TS7; 2.
DR STRING; 10090.ENSMUSP00000074895; -.
DR iPTMnet; Q80TS7; -.
DR PhosphoSitePlus; Q80TS7; -.
DR PaxDb; Q80TS7; -.
DR PRIDE; Q80TS7; -.
DR ProteomicsDB; 279373; -.
DR Antibodypedia; 74886; 7 antibodies from 4 providers.
DR Ensembl; ENSMUST00000075444; ENSMUSP00000074895; ENSMUSG00000059213.
DR GeneID; 13199; -.
DR KEGG; mmu:13199; -.
DR UCSC; uc007xny.1; mouse.
DR CTD; 23109; -.
DR MGI; MGI:108101; Ddn.
DR VEuPathDB; HostDB:ENSMUSG00000059213; -.
DR eggNOG; ENOG502SA8Z; Eukaryota.
DR GeneTree; ENSGT00390000016495; -.
DR HOGENOM; CLU_422079_0_0_1; -.
DR InParanoid; Q80TS7; -.
DR OMA; MLDGPLF; -.
DR OrthoDB; 638730at2759; -.
DR PhylomeDB; Q80TS7; -.
DR TreeFam; TF337173; -.
DR BioGRID-ORCS; 13199; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q80TS7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80TS7; protein.
DR Bgee; ENSMUSG00000059213; Expressed in CA1 field of hippocampus and 86 other tissues.
DR ExpressionAtlas; Q80TS7; baseline and differential.
DR Genevisible; Q80TS7; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR InterPro; IPR026500; Dendrin.
DR PANTHER; PTHR16757; PTHR16757; 1.
DR Pfam; PF15498; Dendrin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse.
FT CHAIN 1..710
FT /note="Dendrin"
FT /id="PRO_0000079862"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..131
FT /note="Nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 186..236
FT /note="Interaction with MAGI2"
FT /evidence="ECO:0000250"
FT REGION 213..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..435
FT /note="Interaction with ACTN1"
FT /evidence="ECO:0000250"
FT REGION 390..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..708
FT /note="Interaction with CD2AP and NPHS1"
FT /evidence="ECO:0000250"
FT REGION 469..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 103..134
FT /evidence="ECO:0000255"
FT COMPBIAS 104..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 679
FT /note="S -> I (in Ref. 1; BAE37653)"
FT /evidence="ECO:0000305"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6JK1"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6JK1"
SQ SEQUENCE 710 AA; 76407 MW; 8EDF4A92AE6A9BB7 CRC64;
MLDGPLFSEG PDSPRELQDE ESGSCLWVQK SKLLVIEVKT ISCHYSRRAP SRQSMDIQAS
YWARGPQSRT CRLRPGSPEP PPRRPWASRV LQEATNWRAG PPAEVRAREQ EKRKAASQER
EAKETERKRR KAGGARRSPL GQPRPEPRNA LRAAQPTGFP VFSRPERFGQ VGRAPRPSVL
PQGDPGVAWA GPWGGRRPGP PSYEAHLLLR GSAGTAPRRR WDRPPPYVAP PSYEGPHRTL
GTKRGPELSR APTSSAPVPA TTRTEGGRTK KRLDPRIYRD VLGAWGLRQG RGLLGGAPGC
TAARARPESC KGAIEKSSGL VAAGLNSAGD SHSQGKTTGG PGTDAALSRS AISSPPRPVP
RSRQHLRGSR KGKEGSEQIW LPTCWLASPK KPPVRHSQTL PRPWAPGGTG WKESLGQREG
AEHETLEVWK VTRRAHTLPR ISRGPAGREG IFVIDATCVV IKSQYVPTPR TQQGQLVPSG
ESCSVSDSLS QPKPCHEEEG EGAAANPSVC QKRLLSSRVL NQPSEGRECE AEVGQQGDSS
LEERSSSGLG FPVGEVNPRD APTQPGSQEH PTLGPAAPVC AGSLKGSEAA GVPRRAGGGW
ARTPGPYAGA LREAVSRIRR HTAPDSDSDE AEDLSVHSGS SDGSDTDAPG ASWRNERTLP
ALGNTRPREG GKTAGLSDSI REIVDVISQT EEGFIREDTR KTPQGNRERE
