ID   ARFP2_RAT               Reviewed;         341 AA.
AC   Q6AY65;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Arfaptin-2 {ECO:0000250|UniProtKB:P53365};
DE   AltName: Full=ADP-ribosylation factor-interacting protein 2 {ECO:0000250|UniProtKB:P53365};
GN   Name=Arfip2 {ECO:0000312|RGD:1303204};
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 [LARGE SCALE MRNA].
RC   STRAIN=Brown Norway; TISSUE=Kidney;
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).
CC   -!- FUNCTION: Plays a role in constitutive metalloproteinase (MMP)
CC       secretion from the trans Golgi network. May have important functions
CC       during vesicle biogenesis at certain cargo subdomains, which could be
CC       predominantly utilized by secreted MMPs, such as MMP7 and MMP2. Also
CC       involved in autophagy by regulating the starvation-dependent
CC       trafficking of ATG9A vesicles which deliver the phosphatidylinositol 4-
CC       kinase beta (PI4KB) to the autophagosome initiation site. Involved in
CC       phagophore growth during mitophagy by regulating ATG9A trafficking to
CC       mitochondria. In addition, plays a role in NF-kappa-B inhibition by
CC       interacting with IKBKB and IKBKG. {ECO:0000250|UniProtKB:P53365}.
CC   -!- SUBUNIT: Forms homodimers or heterodimers with ARFIP1. Interacts with
CC       RAC1. Specifically binds to GTP-bound ARF1 and ARF6, but binds to
CC       RAC1.GTP and RAC1.GDP with similar affinities. Interacts with ARL1.
CC       Interacts (via N-terminus) with IKBKB and IKBKG; these interactions
CC       inhibit activation of NF-kappa-B. {ECO:0000250|UniProtKB:P53365}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P53365}.
CC       Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250|UniProtKB:P53365}.
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DR   EMBL; BC079174; AAH79174.1; -; mRNA.
DR   RefSeq; NP_001004222.1; NM_001004222.1.
DR   RefSeq; XP_006229995.1; XM_006229933.3.
DR   AlphaFoldDB; Q6AY65; -.
DR   SMR; Q6AY65; -.
DR   STRING; 10116.ENSRNOP00000025159; -.
DR   PaxDb; Q6AY65; -.
DR   PRIDE; Q6AY65; -.
DR   Ensembl; ENSRNOT00000025159; ENSRNOP00000025159; ENSRNOG00000018440.
DR   GeneID; 293344; -.
DR   KEGG; rno:293344; -.
DR   UCSC; RGD:1303204; rat.
DR   CTD; 23647; -.
DR   RGD; 1303204; Arfip2.
DR   eggNOG; KOG3876; Eukaryota.
DR   GeneTree; ENSGT00950000183040; -.
DR   HOGENOM; CLU_047975_2_0_1; -.
DR   InParanoid; Q6AY65; -.
DR   OMA; HTNSTEE; -.
DR   OrthoDB; 1179170at2759; -.
DR   PhylomeDB; Q6AY65; -.
DR   TreeFam; TF314945; -.
DR   Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   PRO; PR:Q6AY65; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018440; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q6AY65; RN.
DR   GO; GO:0005938; C:cell cortex; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0001726; C:ruffle; ISO:RGD.
DR   GO; GO:0032588; C:trans-Golgi network membrane; ISO:RGD.
DR   GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0140090; F:membrane curvature sensor activity; 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:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; ISS:UniProtKB.
DR   GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR010504; AH_dom.
DR   InterPro; IPR030798; Arfaptin_fam.
DR   PANTHER; PTHR12141; PTHR12141; 1.
DR   Pfam; PF06456; Arfaptin; 1.
DR   SMART; SM01015; Arfaptin; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   PROSITE; PS50870; AH; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..341
FT                   /note="Arfaptin-2"
FT                   /id="PRO_0000064669"
FT   DOMAIN          121..321
FT                   /note="AH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00294"
FT   REGION          46..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53365"
SQ   SEQUENCE   341 AA;  37773 MW;  AA3BE39EF0C75037 CRC64;
     MTDGILGKAA TMEIPIHGNG EAGQLPEDDG LEQDLQQVMV SGPNLNETSI VSGGYGGSGD
     GLIPTGSGRH PSHSTSPSGP GDEVARGIAG EKFDIVKKWG INTYKCTKQL LSERFGRGSR
     TVDLELELQI ELLRETKRKY ESVLQLGRAL TAHLYSLLQT QHALGDAFAD LSQKSPELQE
     EFGYNAETQK LLCKNGETLL GAVNFFVSSI NTLVTKTMED TLMTVKQYEA ARLEYDAYRT
     DLEELSLGPR DAGTRGRLES AQATFQTHRD KYEKLRGDVA IKLKFLEENK IKVMHKQLLL
     FHNAVSAYFA GNQKQLEQTL QQFNIKLRPP GAEKPSWLEE Q