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Protein

Guanine nucleotide exchange factor DBS

Gene

Mcf2l

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways. Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus.1 Publication

GO - Molecular functioni

  • lipid binding Source: UniProtKB-KW
  • Rho guanyl-nucleotide exchange factor activity Source: UniProtKB

GO - Biological processi

  • intracellular signal transduction Source: InterPro
  • positive regulation of GTPase activity Source: GOC
  • positive regulation of Rho protein signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-RNO-193648. NRAGE signals death through JNK.
R-RNO-194840. Rho GTPase cycle.
R-RNO-416482. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide exchange factor DBS
Alternative name(s):
DBL's big sister
MCF2-transforming sequence-like protein
OST oncogene1 Publication
Gene namesi
Name:Mcf2l
Synonyms:Ost1 Publication
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi619782. Mcf2l.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extrinsic component of membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11491149Guanine nucleotide exchange factor DBSPRO_0000080937Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei457 – 4571PhosphoserineCombined sources
Modified residuei462 – 4621PhosphoserineCombined sources
Modified residuei471 – 4711PhosphoserineCombined sources
Modified residuei480 – 4801PhosphoserineCombined sources
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei622 – 6221PhosphothreonineBy similarity
Modified residuei1033 – 10331PhosphoserineBy similarity
Modified residuei1034 – 10341PhosphoserineBy similarity
Modified residuei1041 – 10411PhosphoserineBy similarity
Modified residuei1042 – 10421PhosphoserineBy similarity

Post-translational modificationi

Mainly phosphorylated on serine.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ63406.
PRIDEiQ63406.

PTM databases

iPTMnetiQ63406.
PhosphoSiteiQ63406.

Expressioni

Tissue specificityi

Highest expression in the brain, where it is found in neurons and alpha-tanycytes (at protein level). Detected in brain, and at lower levels in the heart.1 Publication

Gene expression databases

ExpressionAtlasiQ63406. baseline and differential.
GenevisibleiQ63406. RN.

Interactioni

Subunit structurei

Interacts with GTP-bound RAC1 (PubMed:7957046). Interacts with CDC42. Interacts with RHOA. Interacts with CCPG1, which results in specific inhibition of its exchange activity toward RHOA, but does not affect its activity on CDC42 (By similarity).By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023352.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 224173CRAL-TRIOPROSITE-ProRule annotationAdd
BLAST
Repeati355 – 454100SpectrinAdd
BLAST
Domaini632 – 812181DHPROSITE-ProRule annotationAdd
BLAST
Domaini830 – 946117PHPROSITE-ProRule annotationAdd
BLAST
Domaini1055 – 111662SH3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili503 – 52826Sequence analysisAdd
BLAST

Domaini

The CRAL-TRIO domain mediates interaction with various inositol phospholipids, such as phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol 5-phosphate (PI5P).By similarity
The DH domain is involved in interaction with CCPG1.By similarity

Sequence similaritiesi

Belongs to the MCF2 family.Curated
Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 1 spectrin repeat.Curated

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiENOG410IPNH. Eukaryota.
ENOG410XNYV. LUCA.
GeneTreeiENSGT00760000119030.
HOGENOMiHOG000231361.
HOVERGENiHBG062385.
InParanoidiQ63406.
OrthoDBiEOG7KQ210.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF13716. CRAL_TRIO_2. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00435. Spectrin. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00516. SEC14. 1 hit.
SM00326. SH3. 1 hit.
SM00150. SPEC. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNCWCFIFC KERVRSNSSS PQHDGTSREE ADHQVDVSDG IRLVPDKAEA
60 70 80 90 100
TMATASDEIM HQDIVPLCAA DIQEQLKKRF AYLSGGRGQD GSPVITFPDY
110 120 130 140 150
PAFSEIPDKE FQNVMTYLTS IPSLQDAGIG FILVIDRRQD KWTSVKASVL
160 170 180 190 200
RIAASFPANL QLVLVLRPTG FFQRTLSDIA FKFNRDEFKM KVPVMMLSSV
210 220 230 240 250
PELHGYIDKS QLTEDLGGTL DYCHSRWLCH RTAIESFALM VKQTAQMLQA
260 270 280 290 300
FGTELAETEL PNDVQSTSLV LSAHTEKKAK VKEDLQLALT EGNSILESLR
310 320 330 340 350
EPLAESIVHS VNQDQLDNQA TVKRLLTQLN ETEAAFDEFW AKHQQKLEQC
360 370 380 390 400
LQLRHFEQGF REVKTALDSM SQKIAAFTDV GNSLAHVQHL LKDLTTFEEK
410 420 430 440 450
SSVAVDKARA LSLEGQQLIE NRHYAVDSIH PKCEELQHLC DHFASEVTRR
460 470 480 490 500
RDLLSKSLEL HSLLETSMKW SDEGIFLLAS QPVDKCQSQD GAEAALQEIE
510 520 530 540 550
KFLETGAENK IQELNKIYKE YECILNQDLL EHVQKVFQKQ ESTEEMFHRR
560 570 580 590 600
QASLKKLAAK QTRPVQPVAP RPEALTKSPS PSPGSWRSSE NSSSEGNALR
610 620 630 640 650
RGPYRRAKSE MSEPRQGRTS STGEEEESLA ILRRHVMNEL LDTERAYVEE
660 670 680 690 700
LLCVLEGYAA EMDNPLMAHL ISTGLQNKKN ILFGNMEEIY HFHNRIFLRE
710 720 730 740 750
LESCIDCPEL VGRCFLERME EFQIYEKYCQ NKPRSESLWR QCSDCPFFQE
760 770 780 790 800
CQKKLDHKLS LDSYLLKPVQ RITKYQLLLK EMLKYSKHCE GAEDLQEALS
810 820 830 840 850
SILGILKAVN DSMHLIAITG YDGNLGDLGK LLMQGSFSVW TDHKKGHTKV
860 870 880 890 900
KELARFKPMQ RHLFLHEKAV LFCKKREENG EGYEKAPSYS YKQSLNMTAV
910 920 930 940 950
GITENVKGDT KKFEIWYNAR EEVYIIQAPT PEIKAAWVNE IRKVLTSQLQ
960 970 980 990 1000
ACREASQHRA LEQSHSLPLP TPASTSPTKG STRNVKKLED RKTDPLCLEG
1010 1020 1030 1040 1050
CVSSSLPKPP EKGKGWSKTS HSLEAPEEDG GWSSAEELIN SSDAEEDGGV
1060 1070 1080 1090 1100
GPRKLVPGKY TVLMDGEKGG SDTLAMRSGD MVEVVEEGTE GLWYVRDLTS
1110 1120 1130 1140
SKEGWVPASS LATLLGKSSS AQCLSSSGKT HCARQLCPEP AKILSPEPV
Length:1,149
Mass (Da):129,410
Last modified:April 20, 2010 - v3
Checksum:i1735D8565A965963
GO

Sequence cautioni

The sequence CAA84713.1 differs from that shown.Probable cloning artifact.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC117058 Genomic DNA. No translation available.
Z35654 mRNA. Translation: CAA84713.1. Sequence problems.
PIRiS51620.
UniGeneiRn.81062.

Genome annotation databases

EnsembliENSRNOT00000043170; ENSRNOP00000047024; ENSRNOG00000028426.
UCSCiRGD:619782. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC117058 Genomic DNA. No translation available.
Z35654 mRNA. Translation: CAA84713.1. Sequence problems.
PIRiS51620.
UniGeneiRn.81062.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023352.

PTM databases

iPTMnetiQ63406.
PhosphoSiteiQ63406.

Proteomic databases

PaxDbiQ63406.
PRIDEiQ63406.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000043170; ENSRNOP00000047024; ENSRNOG00000028426.
UCSCiRGD:619782. rat.

Organism-specific databases

RGDi619782. Mcf2l.

Phylogenomic databases

eggNOGiENOG410IPNH. Eukaryota.
ENOG410XNYV. LUCA.
GeneTreeiENSGT00760000119030.
HOGENOMiHOG000231361.
HOVERGENiHBG062385.
InParanoidiQ63406.
OrthoDBiEOG7KQ210.

Enzyme and pathway databases

ReactomeiR-RNO-193648. NRAGE signals death through JNK.
R-RNO-194840. Rho GTPase cycle.
R-RNO-416482. G alpha (12/13) signalling events.

Miscellaneous databases

PROiQ63406.

Gene expression databases

ExpressionAtlasiQ63406. baseline and differential.
GenevisibleiQ63406. RN.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF13716. CRAL_TRIO_2. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00435. Spectrin. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00516. SEC14. 1 hit.
SM00326. SH3. 1 hit.
SM00150. SPEC. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "A novel oncogene, ost, encodes a guanine nucleotide exchange factor that potentially links Rho and Rac signaling pathways."
    Horii Y., Beeler J.F., Sakaguchi K., Tachibana M., Miki T.
    EMBO J. 13:4776-4786(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-1058, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAC1, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Osteosarcoma.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457; SER-462; SER-471 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCF2L_RAT
AccessioniPrimary (citable) accession number: Q63406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 20, 2010
Last modified: June 8, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.