ARFP1_RAT
ID ARFP1_RAT Reviewed; 366 AA.
AC Q9JHU5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Arfaptin-1 {ECO:0000250|UniProtKB:P53367};
DE AltName: Full=ADP-ribosylation factor-interacting protein 1 {ECO:0000250|UniProtKB:P53367};
GN Name=Arfip1 {ECO:0000312|RGD:708401};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Laporte S.A., Caron M.G.;
RT "Cloning of the rat arfaptin 1.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 ---------------------------------------------------------------------------
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; AY004875; AAF91077.1; -; mRNA.
DR RefSeq; NP_068531.1; NM_021763.1.
DR AlphaFoldDB; Q9JHU5; -.
DR SMR; Q9JHU5; -.
DR IntAct; Q9JHU5; 1.
DR STRING; 10116.ENSRNOP00000014236; -.
DR iPTMnet; Q9JHU5; -.
DR PhosphoSitePlus; Q9JHU5; -.
DR jPOST; Q9JHU5; -.
DR PaxDb; Q9JHU5; -.
DR PeptideAtlas; Q9JHU5; -.
DR PRIDE; Q9JHU5; -.
DR GeneID; 60382; -.
DR KEGG; rno:60382; -.
DR UCSC; RGD:708401; rat.
DR CTD; 27236; -.
DR RGD; 708401; Arfip1.
DR VEuPathDB; HostDB:ENSRNOG00000010533; -.
DR eggNOG; KOG3876; Eukaryota.
DR HOGENOM; CLU_047975_2_0_1; -.
DR InParanoid; Q9JHU5; -.
DR PhylomeDB; Q9JHU5; -.
DR PRO; PR:Q9JHU5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010533; Expressed in duodenum and 19 other tissues.
DR ExpressionAtlas; Q9JHU5; baseline and differential.
DR Genevisible; Q9JHU5; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:RGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:RGD.
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:RGD.
DR GO; GO:1905280; P:negative regulation of retrograde transport, endosome to Golgi; ISO:RGD.
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:RGD.
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; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P53367"
FT CHAIN 2..366
FT /note="Arfaptin-1"
FT /id="PRO_0000064666"
FT DOMAIN 146..346
FT /note="AH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00294"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..74
FT /note="Polar 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:0007744|PubMed:22673903"
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 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53367"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53367"
SQ SEQUENCE 366 AA; 40779 MW; 1737B54006E30FAB CRC64;
MAEESPKNSA AEIPVTSNGE VGDAHEHGYN RDLKHSLPSG LGLSETQITS HGFDSTKEGV
TEAGASQGSS APPLPCVLSP SRVAASQLTQ HAGGQRTHTK GGPVILADEI KNPAMEKLEL
VRKWSLNTYK CTRQIISEKL GRGSRTVDLE LEAQIDILRD NKKKYENILK LAQTLSTQLF
QMVHTQKQLG DAFADLSLKS LELHEEFGYN ADTQKLLAKN GETLLGAINF FIASVNTLVN
KTIEDTLMTV KQYENARIEY DAYRTDLEEL NLGPRDANTL PKIEQSQHLF QIHKEKYDKM
RSDVSVKLKF LEENKVKVLR NQLALFHSAV AAYFAGNQKQ LEQTLKQFHV KLKTPGVDAP
SWLEEQ
