DEN5B_MOUSE
ID DEN5B_MOUSE Reviewed; 1274 AA.
AC A2RSQ0; Q8BII7; Q8BWK2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DENN domain-containing protein 5B;
DE AltName: Full=Rab6IP1-like protein;
GN Name=Dennd5b;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-934.
RC STRAIN=C57BL/6J; TISSUE=Heart;
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] OF 1-934.
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, 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).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate
CC RAB39A and/or RAB39B. Promotes the exchange of GDP to GTP, converting
CC inactive GDP-bound Rab proteins into their active GTP-bound form (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RAB6IP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI32200.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI32536.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAC34394.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AC132412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK050728; BAC34394.1; ALT_SEQ; mRNA.
DR EMBL; AK052296; BAC34923.1; -; mRNA.
DR EMBL; BC132199; AAI32200.1; ALT_SEQ; mRNA.
DR EMBL; BC132535; AAI32536.1; ALT_SEQ; mRNA.
DR CCDS; CCDS20714.2; -.
DR RefSeq; NP_796166.2; NM_177192.3.
DR AlphaFoldDB; A2RSQ0; -.
DR SMR; A2RSQ0; -.
DR BioGRID; 236116; 6.
DR STRING; 10090.ENSMUSP00000107182; -.
DR iPTMnet; A2RSQ0; -.
DR PhosphoSitePlus; A2RSQ0; -.
DR MaxQB; A2RSQ0; -.
DR PaxDb; A2RSQ0; -.
DR PeptideAtlas; A2RSQ0; -.
DR PRIDE; A2RSQ0; -.
DR ProteomicsDB; 279622; -.
DR Antibodypedia; 55109; 74 antibodies from 15 providers.
DR DNASU; 320560; -.
DR Ensembl; ENSMUST00000111557; ENSMUSP00000107182; ENSMUSG00000030313.
DR GeneID; 320560; -.
DR KEGG; mmu:320560; -.
DR UCSC; uc009ett.1; mouse.
DR CTD; 160518; -.
DR MGI; MGI:2444273; Dennd5b.
DR VEuPathDB; HostDB:ENSMUSG00000030313; -.
DR eggNOG; KOG2080; Eukaryota.
DR GeneTree; ENSGT00940000153678; -.
DR HOGENOM; CLU_004201_2_0_1; -.
DR InParanoid; A2RSQ0; -.
DR OMA; NTIHMYE; -.
DR OrthoDB; 53600at2759; -.
DR PhylomeDB; A2RSQ0; -.
DR TreeFam; TF313237; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 320560; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Dennd5b; mouse.
DR PRO; PR:A2RSQ0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; A2RSQ0; protein.
DR Bgee; ENSMUSG00000030313; Expressed in retrosplenial region and 221 other tissues.
DR ExpressionAtlas; A2RSQ0; baseline and differential.
DR Genevisible; A2RSQ0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:1905885; P:positive regulation of triglyceride transport; IDA:CACAO.
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 Acetylation; Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUT9"
FT CHAIN 2..1274
FT /note="DENN domain-containing protein 5B"
FT /id="PRO_0000326532"
FT TRANSMEM 916..936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 39..244
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 263..399
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 401..581
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 772..932
FT /note="RUN 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 936..1044
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 1118..1267
FT /note="RUN 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUT9"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUT9"
FT MOD_RES 1062
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL8"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAL8"
FT MOD_RES 1076
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUT9"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ26"
FT CONFLICT 37
FT /note="E -> G (in Ref. 2; BAC34394)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="P -> R (in Ref. 2; BAC34923)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="C -> S (in Ref. 2; BAC34923)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="P -> Q (in Ref. 2; BAC34923)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="L -> H (in Ref. 2; BAC34394)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1274 AA; 144629 MW; A29B06B3AB9FC946 CRC64;
MSGSSAAPGP GSGSSPAACR FAHYFVLCGI DADSGLEPDE LAGENFDQSP LRRTFKSKVL
AHYPQNIEWN PFDQDAVNML CMPKGLSFRT QADNKEPQFH SFIITREDGS RTYGFVLTFY
EEVTSKQICT AMQTLYQMHN AEQYSSVYAS SSCSMDSLAS SIDEGDATSL LKLQRYNSYD
INRDTLYVSK SICLITPLPF MQACKKFLFQ LHKAVTSQQP PPLPLESYIH NILYEVPLPP
PGRSLKFYGV YEPVICQRPG PNELPLSDYP LREACELLGL ENLVQVFTCV LLEMQTLLYS
QDYQRLMTVA EGITTLLFPF QWQHVYVPIL PASLLHFLDA PVPYLMGLQS KEGTDRSKLE
LPQEANLCFV DIDNHFIELP EEFPQFPNKV DFIQELSEVL LQFGIPPEGS LHSSESATKL
KNMVLKDLAN DKKNGNVPNN SVSVYELLKG SETIARLQAL AKRTGVTMEK IDLPASLSEK
EKDLKLQCEE ADLRDSQLNV QLREVFANRF TQMFADYEAF VIQTAQDMES WLTNREQMQN
FDKASFLSDQ PEPYLPFLSR FIETQMFATF IDNKIMSQWE EKDPLLRVFD SRIEKIRLYN
VRAPTLRTSI YQKCSSLKEA AQSIEQRLMK MDHTAIHPHL LDMKIGQGKY EQGFFPKLQS
DVLATGPANN NRWVSRSATA QRRKERLRQS SEHIGLDSDL REKYMQEARS LGKNLRQPKL
SDLSPAVIAQ TNWKFVEGLL KECRMKTKRM LVEKMGHEAV ELGHGEANIT GLEENTLIAS
LCDLLERIWS HGLLVKQGKS ALWSHLLQFQ DREEKQEHLT DSPVALGPER RKSDSGVMLP
TLRVSLIQDM RHIQNMTEIK TDVGRARAWI RLSLEKKLLS QHLKQLLSNQ PLTKKLYKRY
AFLRCEEERE QFLYHLLSLN AVDYFCFTSV FTTIMIPYRS VIIPIKKLSN AIITSNPWIC
VSGELGDTGV MQIPKNLLEM TFECQNLGKL TTVQIGHDNS GLLAKWLVDC VMVRNEITGH
TYRFPCGRWL GKGVDDGSLE RILIGELMTS ASDEDLGKQC RTPPQQKSPT TTRRLSITSL
TGKPAKPNAG QIQEGIGEAV NNIVKHFHKP EKERGSLTVL LCGENGLVAA LEQVFHHGFK
SARIFHKNVF IWDFVEKAVA YFETTDQILD NEGDVLIQKP SSKTFCHYVN AINTAPRNIG
KDGKFQILVC LGTRDHLLPQ WIPLLAECPA ITRMYEENAL LRDHMTVNSL IRILQTIQDF
TIVLEGSLIK GVDV
