DEN6A_MOUSE
ID DEN6A_MOUSE Reviewed; 605 AA.
AC Q8BH65; Q3UX21; Q6KAP4; Q8BSG0; Q8C4Z7; Q8K2E8; Q8R136;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein DENND6A;
DE AltName: Full=DENN domain-containing protein 6A;
GN Name=Dennd6a;
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] (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain, Egg, Ovary, Oviduct, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 419-605 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION.
RX PubMed=21330364; DOI=10.1074/jbc.r110.217067;
RA Marat A.L., Dokainish H., McPherson P.S.;
RT "DENN domain proteins: regulators of Rab GTPases.";
RL J. Biol. Chem. 286:13791-13800(2011).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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) for RAB14. Component
CC of an endocytic recycling pathway that is required for the control of
CC ADAM10 transport, shedding of N-cadherin/CDH2 by ADAM9 or ADAM10 and
CC regulation of cell-cell junctions. Required for RAB14 recruitment to
CC recycling endosomes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BH65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BH65-2; Sequence=VSP_025920, VSP_025921;
CC Name=3;
CC IsoId=Q8BH65-3; Sequence=VSP_025918;
CC Name=4;
CC IsoId=Q8BH65-4; Sequence=VSP_025918, VSP_025919;
CC -!- SIMILARITY: Belongs to the DENND6 family. {ECO:0000305}.
CC -!- CAUTION: Identified as having similarity to the core DENN family and
CC referred to as DENN6A. Prediction methods do not indicate a DENN domain
CC for this sequence and, the exact role of the DENN or the DENN-like
CC domain in GEF activity needs to be clarified. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21413.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK131163; BAD21413.1; ALT_INIT; mRNA.
DR EMBL; AK033036; BAC28133.1; -; mRNA.
DR EMBL; AK054197; BAC35690.1; -; mRNA.
DR EMBL; AK054295; BAC35721.1; -; mRNA.
DR EMBL; AK080327; BAC37879.1; -; mRNA.
DR EMBL; AK132219; BAE21040.1; -; mRNA.
DR EMBL; AK135953; BAE22742.1; -; mRNA.
DR EMBL; AK163396; BAE37333.1; -; mRNA.
DR EMBL; BC025603; AAH25603.1; -; mRNA.
DR EMBL; BC031553; AAH31553.1; -; mRNA.
DR CCDS; CCDS49430.1; -. [Q8BH65-1]
DR CCDS; CCDS84101.1; -. [Q8BH65-2]
DR CCDS; CCDS88601.1; -. [Q8BH65-3]
DR RefSeq; NP_001127937.1; NM_001134465.2. [Q8BH65-1]
DR RefSeq; NP_001272395.1; NM_001285466.1. [Q8BH65-3]
DR RefSeq; NP_001272396.1; NM_001285467.1. [Q8BH65-3]
DR RefSeq; NP_666081.1; NM_145969.4. [Q8BH65-2]
DR RefSeq; XP_006518841.1; XM_006518778.1. [Q8BH65-3]
DR RefSeq; XP_006518842.1; XM_006518779.1. [Q8BH65-3]
DR AlphaFoldDB; Q8BH65; -.
DR BioGRID; 229272; 27.
DR IntAct; Q8BH65; 26.
DR STRING; 10090.ENSMUSP00000039361; -.
DR iPTMnet; Q8BH65; -.
DR PhosphoSitePlus; Q8BH65; -.
DR EPD; Q8BH65; -.
DR jPOST; Q8BH65; -.
DR MaxQB; Q8BH65; -.
DR PaxDb; Q8BH65; -.
DR PeptideAtlas; Q8BH65; -.
DR PRIDE; Q8BH65; -.
DR ProteomicsDB; 279195; -. [Q8BH65-1]
DR ProteomicsDB; 279196; -. [Q8BH65-2]
DR ProteomicsDB; 279197; -. [Q8BH65-3]
DR ProteomicsDB; 279198; -. [Q8BH65-4]
DR Antibodypedia; 31568; 51 antibodies from 15 providers.
DR DNASU; 211922; -.
DR Ensembl; ENSMUST00000037585; ENSMUSP00000039361; ENSMUSG00000040818. [Q8BH65-1]
DR Ensembl; ENSMUST00000203874; ENSMUSP00000144906; ENSMUSG00000040818. [Q8BH65-2]
DR Ensembl; ENSMUST00000224111; ENSMUSP00000153187; ENSMUSG00000040818. [Q8BH65-3]
DR Ensembl; ENSMUST00000224248; ENSMUSP00000152966; ENSMUSG00000040818. [Q8BH65-3]
DR GeneID; 211922; -.
DR KEGG; mmu:211922; -.
DR UCSC; uc007ssv.1; mouse. [Q8BH65-3]
DR UCSC; uc007ssw.3; mouse. [Q8BH65-1]
DR UCSC; uc007ssx.2; mouse. [Q8BH65-2]
DR CTD; 201627; -.
DR MGI; MGI:2442980; Dennd6a.
DR VEuPathDB; HostDB:ENSMUSG00000040818; -.
DR eggNOG; KOG2432; Eukaryota.
DR GeneTree; ENSGT00390000005529; -.
DR HOGENOM; CLU_017013_0_1_1; -.
DR InParanoid; Q8BH65; -.
DR OMA; EANLEHW; -.
DR OrthoDB; 252077at2759; -.
DR PhylomeDB; Q8BH65; -.
DR TreeFam; TF320228; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 211922; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Dennd6a; mouse.
DR PRO; PR:Q8BH65; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BH65; protein.
DR Bgee; ENSMUSG00000040818; Expressed in animal zygote and 63 other tissues.
DR ExpressionAtlas; Q8BH65; baseline and differential.
DR Genevisible; Q8BH65; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; ISS:UniProtKB.
DR InterPro; IPR018307; ABL9/DENND6_dom.
DR InterPro; IPR024224; DENND6.
DR InterPro; IPR037516; Tripartite_DENN.
DR PANTHER; PTHR13677; PTHR13677; 1.
DR Pfam; PF09794; Avl9; 1.
DR PROSITE; PS50211; DENN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endosome;
KW Guanine-nucleotide releasing factor; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..605
FT /note="Protein DENND6A"
FT /id="PRO_0000289117"
FT DOMAIN 60..239
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 265..390
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 392..525
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 507
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWF6"
FT VAR_SEQ 1..224
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025918"
FT VAR_SEQ 424..605
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025919"
FT VAR_SEQ 538..559
FT /note="DLLLWIQKHTEVETVDLVLKLK -> VRKKCISTCKCSEYKSILRGLE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025920"
FT VAR_SEQ 560..605
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025921"
SQ SEQUENCE 605 AA; 68967 MW; 4745B81A08B08FEE CRC64;
MALPGPAVFG PGSRGSLDEA GAEGREAAAL AAAGVALEDE EEDDGRRGLL RWDGFSAWLH
CVCVVGFDLE LGQAVEVIYP QHSKLTDKEK TNICYLSFPD SNSGCLGDTQ FCFRFRQSSG
RRVSLHCLLD EFDKDLPVYL KKDPAYFYGY VYFRQVRDKT LKRGYFQKSL VLISKLPYIH
FFHTVLKQIA PEYFEKNEPY LEAACNDVDR WPAPVPGKTL HLPIMGLVMK VRIPTCHDKP
GTTQMVQLTQ QADTHTSIIL PTVHEVDLFR CFCPVFLHSQ MLWELVLLGE PLVVMAPSPS
ESSETVLALV NCISPLKYFS DFRPYFTIHD SEFKEYTTRT QAPPSVILGV TNPFFAKTLQ
HWPHIIRIGD LKPAGEIPKQ VKVKKLKNLK TLDSKPGVYT SYKPYLNRDE EIIKQLQKGI
QQKRPSEAQS VILRRYFLEL TQSFIIPLER YVASLMPLQK SISPWKSPPQ LRQFLPEEFM
KTLEKTGPQL TSGIKGDWIG LYRQFLKSPN FDGWFKTRRK EMTQKLEALH LEALCEEDLL
LWIQKHTEVE TVDLVLKLKN KLLQAGRESL PVKPDTVEKL RTHIDAIILA LPDDLQGILL
KTGMT
