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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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