DEN5A_MOUSE
ID DEN5A_MOUSE Reviewed; 1287 AA.
AC Q6PAL8; Q62146; Q8C829; Q8VDF6; Q9QYZ2;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DENN domain-containing protein 5A;
DE AltName: Full=Rab6-interacting protein 1;
DE Short=Rab6IP1;
GN Name=Dennd5a; Synonyms=Rab6ip1;
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 [MRNA].
RC STRAIN=ICR;
RA Goud B.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 703-1287.
RC STRAIN=C57BL/6J; TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 705-890, AND INTERACTION WITH RAB6A.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7782346; DOI=10.1074/jbc.270.24.14801;
RA Janoueix-Lerosey I., Jollivet F., Camonis J., Marche P.N., Goud B.;
RT "Two-hybrid system screen with the small GTP-binding protein Rab6.
RT Identification of a novel mouse GDP dissociation inhibitor isoform and two
RT other potential partners of Rab6.";
RL J. Biol. Chem. 270:14801-14808(1995).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1079 AND SER-1085, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
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).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=22558185; DOI=10.1371/journal.pone.0035637;
RA Fernandes H., Franklin E., Jollivet F., Bliedtner K., Khan A.R.;
RT "Mapping the interactions between a RUN domain from DENND5/Rab6IP1 and
RT sorting nexin 1.";
RL PLoS ONE 7:E35637-E35637(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 707-1090 IN COMPLEX WITH RAB6A,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-763; TYR-932 AND LEU-935.
RX PubMed=19141279; DOI=10.1016/j.str.2008.10.014;
RA Recacha R., Boulet A., Jollivet F., Monier S., Houdusse A., Goud B.,
RA Khan A.R.;
RT "Structural basis for recruitment of Rab6-interacting protein 1 to Golgi
RT via a RUN domain.";
RL Structure 17:21-30(2009).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate
CC RAB6A and RAB39A and/or RAB39B. Promotes the exchange of GDP to GTP,
CC converting inactive GDP-bound Rab proteins into their active GTP-bound
CC form (By similarity). Involved in the negative regulation of neurite
CC outgrowth (By similarity). {ECO:0000250|UniProtKB:G3V7Q0,
CC ECO:0000250|UniProtKB:Q6IQ26}.
CC -!- SUBUNIT: Interacts with RAB6A bound to GTP.
CC {ECO:0000269|PubMed:19141279, ECO:0000269|PubMed:7782346}.
CC -!- INTERACTION:
CC Q6PAL8; P20340-1: RAB6A; Xeno; NbExp=4; IntAct=EBI-15750630, EBI-8851226;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:19141279, ECO:0000269|PubMed:22558185}.
CC -!- SIMILARITY: Belongs to the RAB6IP1 family. {ECO:0000305}.
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DR EMBL; AJ245569; CAB55599.1; -; mRNA.
DR EMBL; BC022119; AAH22119.1; -; mRNA.
DR EMBL; BC060230; AAH60230.1; -; mRNA.
DR EMBL; AK048609; BAC33389.1; -; mRNA.
DR EMBL; L40894; AAA78787.1; -; mRNA.
DR CCDS; CCDS21741.1; -.
DR PIR; A56956; A56956.
DR RefSeq; NP_001298068.1; NM_001311139.1.
DR RefSeq; NP_067469.1; NM_021494.1.
DR PDB; 3CWZ; X-ray; 3.20 A; B=707-1090.
DR PDBsum; 3CWZ; -.
DR AlphaFoldDB; Q6PAL8; -.
DR SMR; Q6PAL8; -.
DR BioGRID; 202551; 7.
DR DIP; DIP-287N; -.
DR IntAct; Q6PAL8; 1.
DR STRING; 10090.ENSMUSP00000079295; -.
DR iPTMnet; Q6PAL8; -.
DR PhosphoSitePlus; Q6PAL8; -.
DR EPD; Q6PAL8; -.
DR jPOST; Q6PAL8; -.
DR MaxQB; Q6PAL8; -.
DR PaxDb; Q6PAL8; -.
DR PeptideAtlas; Q6PAL8; -.
DR PRIDE; Q6PAL8; -.
DR ProteomicsDB; 279621; -.
DR Antibodypedia; 24203; 115 antibodies from 20 providers.
DR DNASU; 19347; -.
DR Ensembl; ENSMUST00000080437; ENSMUSP00000079295; ENSMUSG00000035901.
DR GeneID; 19347; -.
DR KEGG; mmu:19347; -.
DR UCSC; uc009jek.1; mouse.
DR CTD; 23258; -.
DR MGI; MGI:1201681; Dennd5a.
DR VEuPathDB; HostDB:ENSMUSG00000035901; -.
DR eggNOG; KOG2080; Eukaryota.
DR GeneTree; ENSGT00940000153678; -.
DR InParanoid; Q6PAL8; -.
DR OMA; KVTQEMY; -.
DR OrthoDB; 53600at2759; -.
DR PhylomeDB; Q6PAL8; -.
DR TreeFam; TF313237; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 19347; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Dennd5a; mouse.
DR EvolutionaryTrace; Q6PAL8; -.
DR PRO; PR:Q6PAL8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6PAL8; protein.
DR Bgee; ENSMUSG00000035901; Expressed in cerebellar nuclear complex and 248 other tissues.
DR ExpressionAtlas; Q6PAL8; baseline and differential.
DR Genevisible; Q6PAL8; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030904; C:retromer complex; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR Gene3D; 1.20.58.900; -; 3.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF02759; RUN; 2.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00593; RUN; 2.
DR SMART; SM00800; uDENN; 1.
DR SUPFAM; SSF140741; SSF140741; 2.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS50826; RUN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Golgi apparatus; Guanine-nucleotide releasing factor;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1287
FT /note="DENN domain-containing protein 5A"
FT /id="PRO_0000097143"
FT DOMAIN 57..259
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 278..414
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 416..598
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 787..950
FT /note="RUN 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 954..1062
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 1134..1280
FT /note="RUN 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ26"
FT MOD_RES 1079
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ26"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ26"
FT MUTAGEN 763
FT /note="K->E: Abolishes the interaction with RAP6A and
FT localization to Golgi membrane."
FT /evidence="ECO:0000269|PubMed:19141279"
FT MUTAGEN 932
FT /note="Y->S: Abolishes the interaction with RAP6A and
FT localization to Golgi membrane; when associated with Ala-
FT 935."
FT /evidence="ECO:0000269|PubMed:19141279"
FT MUTAGEN 935
FT /note="L->A: Abolishes the interaction with RAP6A and
FT localization to Golgi membrane; when associated with Ser-
FT 932."
FT /evidence="ECO:0000269|PubMed:19141279"
FT CONFLICT 37..60
FT /note="Missing (in Ref. 1; CAB55599)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="T -> E (in Ref. 4; AAA78787)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="K -> E (in Ref. 3; BAC33389)"
FT /evidence="ECO:0000305"
FT CONFLICT 871..872
FT /note="IQ -> ME (in Ref. 4; AAA78787)"
FT /evidence="ECO:0000305"
FT CONFLICT 888..890
FT /note="VRL -> GAT (in Ref. 4; AAA78787)"
FT /evidence="ECO:0000305"
FT HELIX 742..772
FT /evidence="ECO:0007829|PDB:3CWZ"
FT HELIX 784..805
FT /evidence="ECO:0007829|PDB:3CWZ"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:3CWZ"
FT STRAND 812..814
FT /evidence="ECO:0007829|PDB:3CWZ"
FT HELIX 816..830
FT /evidence="ECO:0007829|PDB:3CWZ"
FT HELIX 864..872
FT /evidence="ECO:0007829|PDB:3CWZ"
FT HELIX 880..894
FT /evidence="ECO:0007829|PDB:3CWZ"
FT HELIX 897..904
FT /evidence="ECO:0007829|PDB:3CWZ"
FT HELIX 908..914
FT /evidence="ECO:0007829|PDB:3CWZ"
FT TURN 920..922
FT /evidence="ECO:0007829|PDB:3CWZ"
FT HELIX 924..934
FT /evidence="ECO:0007829|PDB:3CWZ"
FT HELIX 935..938
FT /evidence="ECO:0007829|PDB:3CWZ"
FT TURN 944..948
FT /evidence="ECO:0007829|PDB:3CWZ"
FT STRAND 952..962
FT /evidence="ECO:0007829|PDB:3CWZ"
FT STRAND 975..983
FT /evidence="ECO:0007829|PDB:3CWZ"
FT STRAND 997..1003
FT /evidence="ECO:0007829|PDB:3CWZ"
FT STRAND 1007..1015
FT /evidence="ECO:0007829|PDB:3CWZ"
FT STRAND 1024..1033
FT /evidence="ECO:0007829|PDB:3CWZ"
FT TURN 1034..1036
FT /evidence="ECO:0007829|PDB:3CWZ"
FT STRAND 1039..1049
FT /evidence="ECO:0007829|PDB:3CWZ"
FT STRAND 1057..1062
FT /evidence="ECO:0007829|PDB:3CWZ"
SQ SEQUENCE 1287 AA; 146653 MW; 9A48FE3DDC6A2BF1 CRC64;
MSGGGGGGGS APSRFADYFV ICGLDTETGL EPDELSALCQ YIQASKARDG ASPFISSTTE
GENFEQTPLR RTFKSKVLAR YPENVDWNPF DQDAVGMLCM PKGLAFKTQA DPREPQFHAF
IITREDGSRT FGFALTFYEE VTSKQICSAM QTLYHMHNAE YDVLHAPLAD GGDQSGMEDG
EGIPGTKLQR FNSYDISRDT LYVSKCICLI TPMSFMKACR SVLQQLHQAV TSPQPPPLPL
ESYIYNVLYE VPLPPPGRSL KFSGVYGPII CQRPSTNELP LFDFPVKEVF ELLGVENVFQ
LFTCALLEFQ ILLYSQHYQR LMTVAETITA LMFPFQWQHV YVPILPASLL HFLDAPVPYL
MGLHSNGLDD RSKLELPQEA NLCFVDVDNH FIELPEDLPQ FPNKLEFVQE VSEILMAFGV
PPEGNLHCSE SASKLKRIRA SELVSDKRNG NIAGSPLHSY ELLKENETIA RLQALVKRTG
VSLEKLEVRE DPSSNKDFKV QCDEEELRIY QLNIQIREVF ANRFTQMFAD YEVFVIQPSQ
DKESWFTNRE QMQNFDKASF LSDQPEPYLP FLSRFLETQM FASFIDNKIM CHDDDDKDPV
LRVFDSRVDK IRLLNVRTPT LRTSMYQKCT TVDEAEKAIE LRLAKIDHTA VHPHLLDMKI
GQGKYEPGFF PKLQSDVLCT GPASNKWTKR NAPAQWRRKD RQKQHTEHLR LDNDQREKYI
QEARNMGSTI RQPKLSNLSP SVIAQTNWKF VEGLLKECRN KTKRMLVEKM GREAVELGHG
EVNITGVEEN TLIASLCDLL ERIWSHGLQV KQGKSALWSH LLHYQENRQR KLTSGSLSTS
GILLDSERRK SDASAVMSPL RISLIQDMRH IQNIGEIKTD VGKARAWVRL SMEKKLLSRH
LKQLLSDHEL TKKLYKRYAF LRCDDEKEQF LYHLLSFNAV DYFCFTNVFT TILIPYHILI
VPSKKLGGSM FTANPWICIS GELGETQILQ IPRNVLEMTF ECQNLGKLTT VQIGHDNSGL
YAKWLVECVM VRNEVTGHTY KFPCGRWLGK GMDDGSLERV LVGELLTSLP EVDERPCRTP
PLQQSPSVIR RLVTISPNNK PKLNTGQIQE SIGEAVNGIV KHFHKPEKER GSLTLLLCGE
CGLVSALEQA FQHGFKSPRL FKNVFIWDFL EKAQTYYETL EQNDVVPEEN WHTRARNFCR
FVTAVNNTPR NIGKDGKFQM LVCLGARDHL LHHWIALLAD CPITAHMYED VALIKDHTLV
NSLIRVLQTL QEFNITLDTS LVKGIDI
