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ARFP1_MOUSE
ID   ARFP1_MOUSE             Reviewed;         373 AA.
AC   G5E8V9; A2RSX9; E9Q3G5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Arfaptin-1;
DE   AltName: Full=ADP-ribosylation factor-interacting protein 1;
GN   Name=Arfip1 {ECO:0000312|MGI:MGI:1277120};
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] (ISOFORM 2).
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   [3] {ECO:0007744|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: Plays a role in controlling biogenesis of secretory granules
CC       at the trans-Golgi network. Mechanisitically, binds ARF-GTP at the neck
CC       of a growing secretory granule precursor and forms a protective
CC       scaffold. Once the granule precursor has been completely loaded, active
CC       PRKD1 phosphorylates ARFIP1 and releases it from ARFs. In turn, ARFs
CC       induce fission. Through this mechanism, ensures proper secretory
CC       granule formation at the Golgi of pancreatic beta cells.
CC       {ECO:0000250|UniProtKB:P53367}.
CC   -!- SUBUNIT: Forms homodimers or heterodimers with ARFIP2. Interacts with
CC       non-myristoylated GTP-bound ARF3, but not to GDP-bound ARF3. Interacts
CC       with ARF1. Binds with lower affinity to ARF5 and with very little
CC       affinity to ARF6. Interacts with ARL1. Interacts with ATG9A.
CC       {ECO:0000250|UniProtKB:P53367}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P53367}.
CC       Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250|UniProtKB:P53367}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=G5E8V9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=G5E8V9-2; Sequence=VSP_061208;
CC       Name=3;
CC         IsoId=G5E8V9-3; Sequence=VSP_061209;
CC   -!- PTM: Phosphorylated by PRKD1; phosphorylation delocalizes ARFIP1 from
CC       the Golgi and disrupts its ability to inhibit the activity of ADP-
CC       ribosylation factor, an important component of the vesicle scission
CC       machinery. {ECO:0000250|UniProtKB:P53367}.
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DR   EMBL; BC132291; AAI32292.1; -; mRNA.
DR   EMBL; BC144758; AAI44759.1; -; mRNA.
DR   CCDS; CCDS38466.1; -. [G5E8V9-1]
DR   CCDS; CCDS79931.1; -. [G5E8V9-2]
DR   RefSeq; NP_001074562.1; NM_001081093.2. [G5E8V9-1]
DR   RefSeq; NP_001280730.1; NM_001293801.1. [G5E8V9-2]
DR   RefSeq; XP_006502545.1; XM_006502482.3. [G5E8V9-1]
DR   AlphaFoldDB; G5E8V9; -.
DR   SMR; G5E8V9; -.
DR   STRING; 10090.ENSMUSP00000122964; -.
DR   iPTMnet; G5E8V9; -.
DR   PhosphoSitePlus; G5E8V9; -.
DR   EPD; G5E8V9; -.
DR   jPOST; G5E8V9; -.
DR   MaxQB; G5E8V9; -.
DR   PaxDb; G5E8V9; -.
DR   PeptideAtlas; G5E8V9; -.
DR   PRIDE; G5E8V9; -.
DR   ProteomicsDB; 330963; -.
DR   ProteomicsDB; 337187; -.
DR   ProteomicsDB; 366098; -.
DR   DNASU; 99889; -.
DR   Ensembl; ENSMUST00000098990; ENSMUSP00000096588; ENSMUSG00000074513. [G5E8V9-2]
DR   Ensembl; ENSMUST00000107687; ENSMUSP00000103315; ENSMUSG00000074513. [G5E8V9-3]
DR   Ensembl; ENSMUST00000143514; ENSMUSP00000122964; ENSMUSG00000074513. [G5E8V9-1]
DR   GeneID; 99889; -.
DR   KEGG; mmu:99889; -.
DR   UCSC; uc008pqe.2; mouse. [G5E8V9-1]
DR   UCSC; uc008pqf.2; mouse.
DR   CTD; 27236; -.
DR   MGI; MGI:1277120; Arfip1.
DR   VEuPathDB; HostDB:ENSMUSG00000074513; -.
DR   eggNOG; KOG3876; Eukaryota.
DR   GeneTree; ENSGT00950000183040; -.
DR   HOGENOM; CLU_047975_2_0_1; -.
DR   InParanoid; G5E8V9; -.
DR   OMA; EHDEGIQ; -.
DR   OrthoDB; 1179170at2759; -.
DR   PhylomeDB; G5E8V9; -.
DR   TreeFam; TF314945; -.
DR   BioGRID-ORCS; 99889; 0 hits in 71 CRISPR screens.
DR   ChiTaRS; Arfip1; mouse.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; G5E8V9; protein.
DR   Bgee; ENSMUSG00000074513; Expressed in secondary oocyte and 62 other tissues.
DR   ExpressionAtlas; G5E8V9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR   GO; GO:0032588; C:trans-Golgi network membrane; ISO:MGI.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:MGI.
DR   GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; ISO:MGI.
DR   GO; GO:1905280; P:negative regulation of retrograde transport, endosome to Golgi; ISO:MGI.
DR   GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   GO; GO:0050708; P:regulation of protein secretion; ISO:MGI.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR010504; AH_dom.
DR   InterPro; IPR030793; Arfaptin-1.
DR   InterPro; IPR030798; Arfaptin_fam.
DR   PANTHER; PTHR12141; PTHR12141; 1.
DR   PANTHER; PTHR12141:SF4; PTHR12141:SF4; 1.
DR   Pfam; PF06456; Arfaptin; 1.
DR   SMART; SM01015; Arfaptin; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   PROSITE; PS50870; AH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Golgi apparatus; Membrane;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P53367"
FT   CHAIN           2..373
FT                   /note="Arfaptin-1"
FT                   /id="PRO_0000453921"
FT   DOMAIN          153..353
FT                   /note="AH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00294"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P53367"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53367"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53367"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53367"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53367"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53367"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53367"
FT   MOD_RES         361
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P53367"
FT   VAR_SEQ         68..99
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_061208"
FT   VAR_SEQ         92..98
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_061209"
SQ   SEQUENCE   373 AA;  41518 MW;  D0A5E279BCF2D52C CRC64;
     MAQESPKNSA AEIPVTSNGE VDDAHEHGYN RDLKHSLPSG LGLSETQITS HGFDSTKEGV
     TEAGAPQGSS APPLPCVLSP SRVAASKLTQ QAGDLTVPAG GQRTHTKGGP VILADEIKNP
     AMEKLELVRK WSLNTYKCTR QIISEKLGRG SRTVDLELEA QIDILRDNKK KYENILKLAQ
     TLSTQLFQMV HTQKQLGDAF ADLSLKSLEL HEEFGYNADT QKLLAKNGET LLGAINFFIA
     SVNTLVNKTI EDTLMTVKQY ENARVEYDAY RTDLEELNLG PRDANTLPKI EQSQHLFQIH
     KEKYDKMRSD VSVKLKFLEE NKVKVLRNQL VLFHSAVAAY FAGNQKQLEL TLKQFHVRLK
     TPGVDAPSWL EEQ
 
 
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