Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9EPJ9

- ARFG1_MOUSE

UniProt

Q9EPJ9 - ARFG1_MOUSE

Protein

ADP-ribosylation factor GTPase-activating protein 1

Gene

Arfgap1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri22 – 4524C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ARF GTPase activator activity Source: InterPro
    2. GTPase activator activity Source: MGI
    3. protein binding Source: IntAct
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. protein transport Source: UniProtKB-KW
    2. regulation of ARF GTPase activity Source: InterPro
    3. vesicle-mediated transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_106572. XBP1(S) activates chaperone genes.
    REACT_227904. COPI Mediated Transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ADP-ribosylation factor GTPase-activating protein 1
    Short name:
    ARF GAP 1
    Alternative name(s):
    ADP-ribosylation factor 1 GTPase-activating protein
    Short name:
    ARF1 GAP
    ARF1-directed GTPase-activating protein
    Gene namesi
    Name:Arfgap1
    Synonyms:Arf1gap
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2183559. Arfgap1.

    Subcellular locationi

    Cytoplasm By similarity. Golgi apparatus By similarity
    Note: Associates with the Golgi complex.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: Ensembl
    2. Golgi membrane Source: Ensembl
    3. nuclear membrane Source: Ensembl
    4. plasma membrane Source: Ensembl
    5. synapse Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 414414ADP-ribosylation factor GTPase-activating protein 1PRO_0000074191Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei135 – 1351PhosphothreonineBy similarity
    Modified residuei189 – 1891PhosphothreonineBy similarity
    Modified residuei231 – 2311N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9EPJ9.
    PaxDbiQ9EPJ9.
    PRIDEiQ9EPJ9.

    PTM databases

    PhosphoSiteiQ9EPJ9.

    Expressioni

    Gene expression databases

    BgeeiQ9EPJ9.
    GenevestigatoriQ9EPJ9.

    Interactioni

    Subunit structurei

    Interacts with ARF1. Interacts with the COPI coat proteins, KDELR1 and TMED2. It is probably a component of the COPI coat protein complex. The interaction with TMED2 inhibits the GAP activity By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Lrrk2Q5S0063EBI-6288020,EBI-2693710

    Protein-protein interaction databases

    BioGridi230805. 1 interaction.
    IntActiQ9EPJ9. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EPJ9.
    SMRiQ9EPJ9. Positions 3-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 124118Arf-GAPPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The region downstream of Arf-GAP domain is essential to GAP activity in vivo. This region may be required for its targeting to Golgi membranes By similarity.By similarity

    Sequence similaritiesi

    Contains 1 Arf-GAP domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri22 – 4524C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5347.
    GeneTreeiENSGT00670000098104.
    HOGENOMiHOG000008494.
    HOVERGENiHBG050562.
    InParanoidiA8WIR9.
    KOiK12492.
    OMAiQNENANR.
    OrthoDBiEOG7C8GH3.
    PhylomeDBiQ9EPJ9.
    TreeFamiTF105931.

    Family and domain databases

    InterProiIPR001164. ArfGAP.
    [Graphical view]
    PfamiPF01412. ArfGap. 1 hit.
    [Graphical view]
    PRINTSiPR00405. REVINTRACTNG.
    SMARTiSM00105. ArfGap. 1 hit.
    [Graphical view]
    PROSITEiPS50115. ARFGAP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9EPJ9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASPRTRKVL KEVRAQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR    50
    GLGVHLSFVR SVTMDKWKDI ELEKMKAGGN AKFREFLETQ DDYEPSWSLQ 100
    DKYSSRAAAL FRDKVATLAE GKEWSLESSP AQNWTPPQPK TLQFTAHRAS 150
    GQPQSAAASG DKAFEDWLND DLGSYQGAQE NRYVGFGNTV PPQKREDDFL 200
    NNAMSSLYSG WSSFTTGASK FASAAKEGAT KFGSQASQKA SELGHSLNEN 250
    VLKPAQEKVK EGRIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAED 300
    SSDRPLEGHS YQNSSGDNSQ NSNIDQSFWE TFGSAEPPKA KSPSSDSWTC 350
    ADASTGRRSS DSWDVWGSGS ASNNKNSNSD GWESWEGASG EGRAKATKKA 400
    APSTADEGWD NQNW 414
    Length:414
    Mass (Da):45,288
    Last modified:August 16, 2004 - v2
    Checksum:i72A3279D185714C0
    GO
    Isoform 2 (identifier: Q9EPJ9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         259-280: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:392
    Mass (Da):42,957
    Checksum:iFC2BDDA150130CA2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti112 – 1121R → K in CAC18721. 1 PublicationCurated
    Sequence conflicti188 – 1881N → K in CAC18721. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei259 – 28022Missing in isoform 2. 1 PublicationVSP_011303Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ401461 mRNA. Translation: CAC18721.1.
    AK030295 mRNA. Translation: BAC26883.1.
    AK030520 mRNA. Translation: BAC27002.1.
    AK145879 mRNA. Translation: BAE26720.1.
    AK168007 mRNA. Translation: BAE39994.1.
    BX649560 Genomic DNA. Translation: CAM23227.1.
    BX649560 Genomic DNA. Translation: CAM23229.1.
    CCDSiCCDS17190.1. [Q9EPJ9-1]
    CCDS50843.1. [Q9EPJ9-2]
    RefSeqiNP_001171177.1. NM_001177706.1. [Q9EPJ9-2]
    NP_001171178.1. NM_001177707.1.
    NP_001171179.1. NM_001177708.1.
    NP_001171180.1. NM_001177709.1. [Q9EPJ9-2]
    NP_665703.2. NM_145760.3. [Q9EPJ9-1]
    XP_006500658.1. XM_006500595.1. [Q9EPJ9-1]
    XP_006500661.1. XM_006500598.1. [Q9EPJ9-2]
    UniGeneiMm.33765.
    Mm.470800.

    Genome annotation databases

    EnsembliENSMUST00000029092; ENSMUSP00000029092; ENSMUSG00000027575. [Q9EPJ9-1]
    ENSMUST00000108859; ENSMUSP00000104487; ENSMUSG00000027575. [Q9EPJ9-2]
    ENSMUST00000108860; ENSMUSP00000104488; ENSMUSG00000027575. [Q9EPJ9-2]
    GeneIDi228998.
    KEGGimmu:228998.
    UCSCiuc008okj.2. mouse. [Q9EPJ9-1]
    uc008okm.2. mouse. [Q9EPJ9-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ401461 mRNA. Translation: CAC18721.1 .
    AK030295 mRNA. Translation: BAC26883.1 .
    AK030520 mRNA. Translation: BAC27002.1 .
    AK145879 mRNA. Translation: BAE26720.1 .
    AK168007 mRNA. Translation: BAE39994.1 .
    BX649560 Genomic DNA. Translation: CAM23227.1 .
    BX649560 Genomic DNA. Translation: CAM23229.1 .
    CCDSi CCDS17190.1. [Q9EPJ9-1 ]
    CCDS50843.1. [Q9EPJ9-2 ]
    RefSeqi NP_001171177.1. NM_001177706.1. [Q9EPJ9-2 ]
    NP_001171178.1. NM_001177707.1.
    NP_001171179.1. NM_001177708.1.
    NP_001171180.1. NM_001177709.1. [Q9EPJ9-2 ]
    NP_665703.2. NM_145760.3. [Q9EPJ9-1 ]
    XP_006500658.1. XM_006500595.1. [Q9EPJ9-1 ]
    XP_006500661.1. XM_006500598.1. [Q9EPJ9-2 ]
    UniGenei Mm.33765.
    Mm.470800.

    3D structure databases

    ProteinModelPortali Q9EPJ9.
    SMRi Q9EPJ9. Positions 3-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230805. 1 interaction.
    IntActi Q9EPJ9. 1 interaction.

    PTM databases

    PhosphoSitei Q9EPJ9.

    Proteomic databases

    MaxQBi Q9EPJ9.
    PaxDbi Q9EPJ9.
    PRIDEi Q9EPJ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029092 ; ENSMUSP00000029092 ; ENSMUSG00000027575 . [Q9EPJ9-1 ]
    ENSMUST00000108859 ; ENSMUSP00000104487 ; ENSMUSG00000027575 . [Q9EPJ9-2 ]
    ENSMUST00000108860 ; ENSMUSP00000104488 ; ENSMUSG00000027575 . [Q9EPJ9-2 ]
    GeneIDi 228998.
    KEGGi mmu:228998.
    UCSCi uc008okj.2. mouse. [Q9EPJ9-1 ]
    uc008okm.2. mouse. [Q9EPJ9-2 ]

    Organism-specific databases

    CTDi 55738.
    MGIi MGI:2183559. Arfgap1.

    Phylogenomic databases

    eggNOGi COG5347.
    GeneTreei ENSGT00670000098104.
    HOGENOMi HOG000008494.
    HOVERGENi HBG050562.
    InParanoidi A8WIR9.
    KOi K12492.
    OMAi QNENANR.
    OrthoDBi EOG7C8GH3.
    PhylomeDBi Q9EPJ9.
    TreeFami TF105931.

    Enzyme and pathway databases

    Reactomei REACT_106572. XBP1(S) activates chaperone genes.
    REACT_227904. COPI Mediated Transport.

    Miscellaneous databases

    NextBioi 379297.
    PROi Q9EPJ9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9EPJ9.
    Genevestigatori Q9EPJ9.

    Family and domain databases

    InterProi IPR001164. ArfGAP.
    [Graphical view ]
    Pfami PF01412. ArfGap. 1 hit.
    [Graphical view ]
    PRINTSi PR00405. REVINTRACTNG.
    SMARTi SM00105. ArfGap. 1 hit.
    [Graphical view ]
    PROSITEi PS50115. ARFGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and functional characterisation of mouse ARF1GAP."
      Venkateswarlu K.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Ovary, Pituitary, Placenta and Uterus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiARFG1_MOUSE
    AccessioniPrimary (citable) accession number: Q9EPJ9
    Secondary accession number(s): A8WIR9
    , A8WIS1, Q3TI52, Q8BMM6, Q8BMQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 27, 2003
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3