DEN2A_MOUSE
ID DEN2A_MOUSE Reviewed; 1000 AA.
AC Q8C4S8; Q3TJU2; Q3TUG3; Q3UXA3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=DENN domain-containing protein 2A;
GN Name=Dennd2a;
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=Cerebellum, and Head;
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 PROTEIN SEQUENCE OF 210-217, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
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: Guanine nucleotide exchange factor (GEF) which may activate
CC RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting
CC inactive GDP-bound Rab proteins into their active GTP-bound form. May
CC play a role in late endosomes back to trans-Golgi network/TGN transport
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Associated with actin filaments. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22660.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK081176; BAC38157.1; -; mRNA.
DR EMBL; AK135781; BAE22660.1; ALT_INIT; mRNA.
DR EMBL; AK160784; BAE36008.1; -; mRNA.
DR EMBL; AK167298; BAE39403.1; -; mRNA.
DR CCDS; CCDS20023.1; -.
DR RefSeq; NP_766065.1; NM_172477.4.
DR AlphaFoldDB; Q8C4S8; -.
DR SMR; Q8C4S8; -.
DR BioGRID; 229109; 2.
DR STRING; 10090.ENSMUSP00000045367; -.
DR iPTMnet; Q8C4S8; -.
DR PhosphoSitePlus; Q8C4S8; -.
DR jPOST; Q8C4S8; -.
DR MaxQB; Q8C4S8; -.
DR PaxDb; Q8C4S8; -.
DR PRIDE; Q8C4S8; -.
DR ProteomicsDB; 279369; -.
DR Antibodypedia; 32452; 39 antibodies from 13 providers.
DR DNASU; 209773; -.
DR Ensembl; ENSMUST00000036877; ENSMUSP00000045367; ENSMUSG00000038456.
DR GeneID; 209773; -.
DR KEGG; mmu:209773; -.
DR UCSC; uc009blx.1; mouse.
DR CTD; 27147; -.
DR MGI; MGI:2444961; Dennd2a.
DR VEuPathDB; HostDB:ENSMUSG00000038456; -.
DR eggNOG; KOG3569; Eukaryota.
DR GeneTree; ENSGT00950000182931; -.
DR HOGENOM; CLU_008960_1_1_1; -.
DR InParanoid; Q8C4S8; -.
DR OMA; KPIFFRQ; -.
DR OrthoDB; 138384at2759; -.
DR PhylomeDB; Q8C4S8; -.
DR TreeFam; TF320336; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 209773; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Dennd2a; mouse.
DR PRO; PR:Q8C4S8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8C4S8; protein.
DR Bgee; ENSMUSG00000038456; Expressed in floor plate of midbrain and 188 other tissues.
DR ExpressionAtlas; Q8C4S8; baseline and differential.
DR Genevisible; Q8C4S8; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00800; uDENN; 1.
DR PROSITE; PS50211; DENN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1000
FT /note="DENN domain-containing protein 2A"
FT /id="PRO_0000242683"
FT DOMAIN 559..708
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 730..863
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 865..960
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 67
FT /note="K -> E (in Ref. 1; BAE36008)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="Q -> L (in Ref. 1; BAE39403)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="K -> E (in Ref. 1; BAE39403)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="A -> V (in Ref. 1; BAE22660)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="E -> G (in Ref. 1; BAE39403)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="A -> P (in Ref. 1; BAE22660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1000 AA; 113094 MW; 8866696B3B25303B CRC64;
MLEARVDMLS SNMIISGPAA DLGAKEASRP WKKQLNSVPN SGPSARARAQ PQPLSIKDKI
SKWEGKKEPP ASDPARQTDG QEDHLPSCKV ERRGSELTRT KNGMRLETER LQNDSRARTV
CQDTEQLPGP RPIDGQPELS QHRGRELKPS DLRFQSDHLS VLRQVKRLEK ALKDGSAGLD
PQMPGTCYSP HCLPDKTEED LPSLESHEKG GVLAAGRRAH HLEVREPGPE ISEDWKGQES
VYRGSRWYPP KPFINPVPKP RRTFKHAGEG DKDVSPGISF KKEKRNLPPL PSLPPPPPPL
PSSPPPTSVN RRLWTGRQRP SADHRKSYEF EDLLQSSSEN SRVDWYAQTK LGLTRTLSEE
NVYEDILDPP MKENPYEDVE LHGRCLGKKC VLTFPASPTS SIPDTSTKQS LSKSAFFRQN
SERRNLKLLD TRKLSRDGAG SPLRTSPPST PSSPDDTFFN LGDLQNGRKK KKIPRLVLRI
NAIYEARRGK KRVKRLSQST ESNSGKVTDE NSESDSDTEE KLKAHSQRLV NVKSRLKQAP
RYSSLDRDLI EYQERQLFEY FVVVSLHKKQ AGAAYVPELT QQFPLKLEKS FKFMREAEDQ
LKAIPQFCFP DAKDWAPVQE FTSETFSFVL TGEDGSRRFG YCRRLLPGGK GKRLPEVYCI
VSRLGCFSLF SKILDEVEKR RGISPALVQP LMRSVMEAPF PALGKTIIVK NFLPGSGTEV
IELCRPLDSR LEHVDFESLF SSLSVRHLVS VFASLLLERR VIFIADKLST LSKCCHAMVA
LIYPFSWQHT YIPVLPPAMI DIVCSPTPFL IGLLSSSLPL LRELPLEEVL VVDLINDRFL
RQMEDEDSIL PRKLQVALEH ILEQRNDLAC DQDGGPLDCV HGPESSSLSE VVSEAFVRFF
VEIVGHYPLF LTSGEERSLQ REAFRKAVSS KSLRRFLEVF METQTFRGFI QERELRRQDA
KGLFEVRAQE YLETLPSGEH SGVNKFLKGL GNKMKFLHKK