ARFP2_MOUSE
ID ARFP2_MOUSE Reviewed; 341 AA.
AC Q8K221; Q3U3G6; Q9D7M3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
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|MGI:MGI:1924182};
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 MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
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 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; AK009100; BAB26070.1; -; mRNA.
DR EMBL; AK154772; BAE32820.1; -; mRNA.
DR EMBL; BC013794; AAH13794.1; -; mRNA.
DR EMBL; BC022942; AAH22942.1; -; mRNA.
DR EMBL; BC034520; AAH34520.1; -; mRNA.
DR CCDS; CCDS21656.1; -.
DR RefSeq; NP_084078.3; NM_029802.4.
DR AlphaFoldDB; Q8K221; -.
DR SMR; Q8K221; -.
DR BioGRID; 218408; 9.
DR IntAct; Q8K221; 1.
DR STRING; 10090.ENSMUSP00000120387; -.
DR iPTMnet; Q8K221; -.
DR PhosphoSitePlus; Q8K221; -.
DR EPD; Q8K221; -.
DR MaxQB; Q8K221; -.
DR PaxDb; Q8K221; -.
DR PeptideAtlas; Q8K221; -.
DR PRIDE; Q8K221; -.
DR ProteomicsDB; 296341; -.
DR Antibodypedia; 23860; 239 antibodies from 27 providers.
DR DNASU; 76932; -.
DR Ensembl; ENSMUST00000084782; ENSMUSP00000081840; ENSMUSG00000030881.
DR Ensembl; ENSMUST00000131446; ENSMUSP00000120387; ENSMUSG00000030881.
DR GeneID; 76932; -.
DR KEGG; mmu:76932; -.
DR UCSC; uc009iyr.2; mouse.
DR CTD; 23647; -.
DR MGI; MGI:1924182; Arfip2.
DR VEuPathDB; HostDB:ENSMUSG00000030881; -.
DR eggNOG; KOG3876; Eukaryota.
DR GeneTree; ENSGT00950000183040; -.
DR HOGENOM; CLU_047975_2_0_1; -.
DR InParanoid; Q8K221; -.
DR OMA; HTNSTEE; -.
DR OrthoDB; 1179170at2759; -.
DR PhylomeDB; Q8K221; -.
DR TreeFam; TF314945; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 76932; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Arfip2; mouse.
DR PRO; PR:Q8K221; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K221; protein.
DR Bgee; ENSMUSG00000030881; Expressed in dentate gyrus of hippocampal formation granule cell and 247 other tissues.
DR ExpressionAtlas; Q8K221; baseline and differential.
DR Genevisible; Q8K221; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:MGI.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0140090; F:membrane curvature sensor activity; 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:0030036; P:actin cytoskeleton organization; ISO:MGI.
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 1: Evidence at protein level;
KW Autophagy; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..341
FT /note="Arfaptin-2"
FT /id="PRO_0000064668"
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"
FT CONFLICT 107
FT /note="T -> K (in Ref. 2; AAH34520)"
FT /evidence="ECO:0000305"
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
