DEND_RAT
ID DEND_RAT Reviewed; 707 AA.
AC P50617; P97543;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Dendrin;
GN Name=Ddn; Synonyms=Den;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8915891;
RX DOI=10.1002/(sici)1097-4547(19961015)46:2<138::aid-jnr2>3.0.co;2-i;
RA Neuner-Jehle M., Denizot J.-P., Borbely A.A., Mallet J.;
RT "Characterization and sleep deprivation-induced expression modulation of
RT dendrin, a novel dendritic protein in rat brain neurons.";
RL J. Neurosci. Res. 46:138-151(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-707, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9073398; DOI=10.1006/mcne.1996.0594;
RA Herb A., Wisden W., Catania M.V., Marechal D., Dresse A., Seeburg P.H.;
RT "Prominent dendritic localization in forebrain neurons of a novel mRNA and
RT its product, dendrin.";
RL Mol. Cell. Neurosci. 8:367-374(1997).
RN [3]
RP INTERACTION WITH MAGI1 AND MAGI2, AND TISSUE SPECIFICITY.
RX PubMed=16751601; DOI=10.1093/jb/mvj105;
RA Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K.,
RA Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.;
RT "CIN85 is localized at synapses and forms a complex with S-SCAM via
RT dendrin.";
RL J. Biochem. 139:931-939(2006).
RN [4]
RP INTERACTION WITH CD2AP; NPHS1 AND NPHS2.
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 [5]
RP INDUCTION BY NICOTINE.
RX PubMed=19046379; DOI=10.1111/j.1460-9568.2008.06483.x;
RA Schochet T.L., Bremer Q.Z., Brownfield M.S., Kelley A.E., Landry C.F.;
RT "The dendritically targeted protein Dendrin is induced by acute nicotine in
RT cortical regions of adolescent rat brain.";
RL Eur. J. Neurosci. 28:1967-1979(2008).
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 -!- SUBUNIT: Forms a ternary complex with MAGI2 and SH3KBP1; recruits DDN
CC to the cytoplasm. Interacts with MAGI1. Interacts with ACTN1 and may
CC interact with WWC1 (By similarity). Interacts with the podocyte slit
CC diaphragm proteins CD2AP, NPHS1 and NPHS2; the interaction with CD2AP
CC and NPHS1 is direct. {ECO:0000250, ECO:0000269|PubMed:16751601,
CC ECO:0000269|PubMed:17537921}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane;
CC Peripheral membrane protein. Cytoplasm {ECO:0000250}. Endoplasmic
CC reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
CC Perikaryon. Nucleus {ECO:0000250}. Note=Enriched at the cytoplasmic
CC insertion of the slit diaphragm into the foot process of podocytes and
CC associated with polyribosomes in dendrites. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in forebrain structures,
CC particularly in neocortex, olfactory bulb, hippocampus, caudate-
CC putamen, and limbic system (at protein level). Also detected in spleen,
CC liver, kidney and placenta (at protein level).
CC {ECO:0000269|PubMed:16751601, ECO:0000269|PubMed:8915891,
CC ECO:0000269|PubMed:9073398}.
CC -!- INDUCTION: By sleep deprivation. By acute nicotine in adolescent brain
CC (at protein level). {ECO:0000269|PubMed:19046379}.
CC -!- MISCELLANEOUS: There are 2 forms of 81 kDa and 89 kDa detected in brain
CC by an antibody raised against a C-terminal peptide arguing for
CC alternative N-terminal sequences.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA65407.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA70204.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X96589; CAA65407.1; ALT_FRAME; mRNA.
DR EMBL; Y09000; CAA70204.1; ALT_INIT; mRNA.
DR RefSeq; NP_112255.1; NM_030993.1.
DR RefSeq; XP_008763894.1; XM_008765672.2.
DR AlphaFoldDB; P50617; -.
DR BioGRID; 247185; 1.
DR IntAct; P50617; 1.
DR STRING; 10116.ENSRNOP00000019854; -.
DR iPTMnet; P50617; -.
DR PhosphoSitePlus; P50617; -.
DR PaxDb; P50617; -.
DR PRIDE; P50617; -.
DR Ensembl; ENSRNOT00000089060; ENSRNOP00000069004; ENSRNOG00000059605.
DR GeneID; 25113; -.
DR KEGG; rno:25113; -.
DR UCSC; RGD:2497; rat.
DR CTD; 23109; -.
DR RGD; 2497; Ddn.
DR eggNOG; ENOG502SA8Z; Eukaryota.
DR GeneTree; ENSGT00390000016495; -.
DR InParanoid; P50617; -.
DR OrthoDB; 638730at2759; -.
DR PhylomeDB; P50617; -.
DR TreeFam; TF337173; -.
DR PRO; PR:P50617; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; TAS:RGD.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR026500; Dendrin.
DR PANTHER; PTHR16757; PTHR16757; 1.
DR Pfam; PF15498; Dendrin; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse.
FT CHAIN 1..707
FT /note="Dendrin"
FT /id="PRO_0000079863"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..131
FT /note="Nuclear localization"
FT REGION 186..236
FT /note="Interaction with MAGI2"
FT /evidence="ECO:0000250"
FT REGION 213..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..434
FT /note="Interaction with ACTN1"
FT /evidence="ECO:0000250"
FT REGION 342..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..707
FT /note="Interaction with CD2AP and NPHS1"
FT /evidence="ECO:0000269|PubMed:17537921"
FT REGION 517..707
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 342..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TS7"
FT CONFLICT 195
FT /note="G -> D (in Ref. 1; CAA65407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 76004 MW; 3C6F21E03DA23DAE CRC64;
MLDGPLFSEG PDSPRELQDE ESGSCLWVQK SKLLVIEVKT ISCHYSRRAA SRQSMDIQAS
YWARGPQNRT CRLRPGSPEP PPRRPWASRV LQEATNWRAG PPAEVRAREQ EKRKAASQER
EAKETERKRR KAGGARRSPL GQPRPELRNA LRAAQPTGFP VFSRPERFGQ VGRAPRPSAL
PQGDPGVAWA GPWGGRRPGP PSYEAHLLLR GAAGTAPRRR WDRPPPYVAP PSYEGPHRTL
GTKRGPELSR APTSSAPVPA TTRTEGGRTK KRLDPRIYRD VLGAWGLRQG RGLLGGAPGC
AAARARPESC KGAVEKSSGL AAAGLNSGGD GHSQAKTTGP VTEVALSGST ISSPPRPVPR
SRQHLRGSRK GKEGSEEMWL PTCWLSSPKK PPVRHSQTLP RPWAPGGTGW KESLGQREGT
EHETLEVWKV TRRAHTLPRS SRGPAGREGI FVIDATCVVI KSQYVPTPRT QQRQLAPSGE
SCIVSDSLRQ PKPCLEEEGK GAAANPSVCQ KRLLSSRVLN PPSEGREFEA EGRQQGDSSL
EERSSSGLGF PVGEVNPRDA PTHPGSPEHS TLGPAAPGCA GSVKGPEAAG VPRRAGGGWA
RTPGPYAGAL REAVSRIRRH TAPDSDSDEA EDLSAHSGSS DGSDTDAPGA SWRNERTLPA
VGNTRPREGG KTAELGDSIG EILDVISQTE EGLVREDTRK TPQGKRE
