DEND_HUMAN
ID DEND_HUMAN Reviewed; 711 AA.
AC O94850;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Dendrin;
GN Name=DDN; Synonyms=KIAA0749;
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 GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-711.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP INTERACTION WITH WWC1.
RC TISSUE=Brain;
RX PubMed=12559952; DOI=10.1016/s0006-291x(02)02945-5;
RA Kremerskothen J., Plaas C., Buether K., Finger I., Veltel S., Matanis T.,
RA Liedtke T., Barnekow A.;
RT "Characterization of KIBRA, a novel WW domain-containing protein.";
RL Biochem. Biophys. Res. Commun. 300:862-867(2003).
RN [4]
RP INTERACTION WITH MAGI1; MAGI2 AND SH3KBP1.
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 [5]
RP INTERACTION WITH ACTN1; MAGI1 AND MAGI2, AND SUBCELLULAR LOCATION.
RX PubMed=16464232; DOI=10.1111/j.1471-4159.2006.03679.x;
RA Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A.;
RT "Postsynaptic recruitment of Dendrin depends on both dendritic mRNA
RT transport and synaptic anchoring.";
RL J. Neurochem. 96:1659-1666(2006).
RN [6]
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 [7]
RP TISSUE SPECIFICITY.
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).
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 (By
CC similarity). {ECO:0000250}.
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. Interacts with the podocyte slit diaphragm proteins
CC CD2AP, NPHS1 and NPHS2; the interaction with CD2AP and NPHS1 is direct
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O94850; Q96B97: SH3KBP1; NbExp=5; IntAct=EBI-5240523, EBI-346595;
CC O94850; O88382: Magi2; Xeno; NbExp=3; IntAct=EBI-5240523, EBI-696179;
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane;
CC Peripheral membrane protein. Cytoplasm. Endoplasmic reticulum membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Perikaryon {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Enriched at the cytoplasmic insertion of the slit diaphragm into
CC the foot process of podocytes and associated with polyribosomes in
CC dendrites. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain and kidney.
CC Expressed in kidney glomerular capillary loops (at protein level).
CC {ECO:0000269|PubMed:17251388, ECO:0000269|PubMed:18356187}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34469.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC011603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB018292; BAA34469.1; ALT_INIT; mRNA.
DR CCDS; CCDS31791.2; -.
DR RefSeq; NP_055901.2; NM_015086.1.
DR AlphaFoldDB; O94850; -.
DR SMR; O94850; -.
DR BioGRID; 116733; 5.
DR CORUM; O94850; -.
DR IntAct; O94850; 8.
DR STRING; 9606.ENSP00000390590; -.
DR iPTMnet; O94850; -.
DR PhosphoSitePlus; O94850; -.
DR BioMuta; DDN; -.
DR jPOST; O94850; -.
DR MassIVE; O94850; -.
DR MaxQB; O94850; -.
DR PaxDb; O94850; -.
DR PeptideAtlas; O94850; -.
DR PRIDE; O94850; -.
DR ProteomicsDB; 50479; -.
DR Antibodypedia; 74886; 7 antibodies from 4 providers.
DR DNASU; 23109; -.
DR Ensembl; ENST00000421952.3; ENSP00000390590.2; ENSG00000181418.8.
DR GeneID; 23109; -.
DR KEGG; hsa:23109; -.
DR MANE-Select; ENST00000421952.3; ENSP00000390590.2; NM_015086.2; NP_055901.2.
DR UCSC; uc001rsv.2; human.
DR CTD; 23109; -.
DR DisGeNET; 23109; -.
DR GeneCards; DDN; -.
DR HGNC; HGNC:24458; DDN.
DR HPA; ENSG00000181418; Group enriched (brain, skeletal muscle).
DR MIM; 610588; gene.
DR neXtProt; NX_O94850; -.
DR OpenTargets; ENSG00000181418; -.
DR PharmGKB; PA134906790; -.
DR VEuPathDB; HostDB:ENSG00000181418; -.
DR eggNOG; ENOG502SA8Z; Eukaryota.
DR GeneTree; ENSGT00390000016495; -.
DR HOGENOM; CLU_422079_0_0_1; -.
DR InParanoid; O94850; -.
DR OMA; MLDGPLF; -.
DR OrthoDB; 638730at2759; -.
DR PhylomeDB; O94850; -.
DR TreeFam; TF337173; -.
DR PathwayCommons; O94850; -.
DR SignaLink; O94850; -.
DR BioGRID-ORCS; 23109; 144 hits in 1068 CRISPR screens.
DR ChiTaRS; DDN; human.
DR GenomeRNAi; 23109; -.
DR Pharos; O94850; Tbio.
DR PRO; PR:O94850; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O94850; protein.
DR Bgee; ENSG00000181418; Expressed in gluteal muscle and 124 other tissues.
DR Genevisible; O94850; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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..711
FT /note="Dendrin"
FT /id="PRO_0000079861"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..273
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 REGION 324..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..436
FT /note="Interaction with ACTN1"
FT /evidence="ECO:0000269|PubMed:16464232"
FT REGION 408..709
FT /note="Interaction with CD2AP and NPHS1"
FT /evidence="ECO:0000250"
FT REGION 479..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 102..134
FT /evidence="ECO:0000255"
FT COMPBIAS 104..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
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 MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TS7"
FT VARIANT 661
FT /note="E -> G (in dbSNP:rs10783299)"
FT /id="VAR_059651"
SQ SEQUENCE 711 AA; 75996 MW; D55B3CBE792519D4 CRC64;
MLDGPLFSEG PDSPRELQDE ESGSCLWVQK SKLLVIEVKT ISCHYSRRAP SRQPMDFQAS
HWARGFQNRT CGPRPGSPQP PPRRPWASRV LQEATNWRAG PLAEVRAREQ EKRKAASQER
EAKETERKRR KAGGARRSPP GRPRPEPRNA PRVAQLAGLP APLRPERLAP VGRAPRPSAQ
PQSDPGSAWA GPWGGRRPGP PSYEAHLLLR GSAGTAPRRR WDRPPPYVAP PSYEGPHRTL
GTKRGPGNSQ VPTSSAPAAT PARTDGGRTK KRLDPRIYRD VLGAWGLRQG QGLLGGSPGC
GAARARPEPG KGVVEKSLGL AAADLNSGSD SHPQAKATGS AGTEIAPAGS ATAAPCAPHP
APRSRHHLKG SREGKEGEQI WFPKCWIPSP KKQPPRHSQT LPRPWAPGGT GWRESLGLGE
GAGPETLEGW KATRRAHTLP RSSQGLSRGE GVFVIDATCV VIRSQYVPTP RTQQVQLLPS
GVTRVVGDSP SQSKPGKEEG EGATVFPSPC QKRLSSSRLL HQPGGGRGGE AEGGRPGDST
LEERTFRILG LPAPEVNLRD APTQPGSPEH QALGPAASGA QGRAEGSEVA VVQRRAGRGW
ARTPGPYAGA LREAVSRIRR HTAPDSDTDE AEELSVHSGS SDGSDTEAPG ASWRNERTLP
EVGNSSPEED GKTAELSDSV GEILDVISQT EEVLFGVRDI RGTQQGNRKR Q
