ARFP2_HUMAN
ID ARFP2_HUMAN Reviewed; 341 AA.
AC P53365; B4DX86; B4E306; D3DQT5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Arfaptin-2 {ECO:0000303|PubMed:9038142};
DE AltName: Full=ADP-ribosylation factor-interacting protein 2 {ECO:0000303|PubMed:9038142};
DE AltName: Full=Partner of RAC1 {ECO:0000303|PubMed:8670882};
DE Short=POR1 {ECO:0000303|PubMed:8670882};
GN Name=ARFIP2 {ECO:0000303|PubMed:30917996, ECO:0000312|HGNC:HGNC:17160};
GN Synonyms=POR1 {ECO:0000303|PubMed:8670882};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9038142; DOI=10.1074/jbc.272.9.5421;
RA Kanoh H., Williger B.-T., Exton J.H.;
RT "Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation
RT factor, is recruited to Golgi membranes.";
RL J. Biol. Chem. 272:5421-5429(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-341 (ISOFORM 1).
RX PubMed=8670882;
RA van Aelst L., Joneson T., Bar-Sagi D.;
RT "Identification of a novel Rac1-interacting protein involved in membrane
RT ruffling.";
RL EMBO J. 15:3778-3786(1996).
RN [7]
RP INTERACTION WITH ARL1.
RX PubMed=11303027; DOI=10.1074/jbc.m102359200;
RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific
RT and shared effectors: characterizing ARL1-binding proteins.";
RL J. Biol. Chem. 276:22826-22837(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP SUBCELLULAR LOCATION, INTERACTION WITH ARL1 AND ARFIP1, AND SUBUNIT.
RX PubMed=21239483; DOI=10.1074/jbc.m110.201442;
RA Man Z., Kondo Y., Koga H., Umino H., Nakayama K., Shin H.W.;
RT "Arfaptins are localized to the trans-Golgi by interaction with Arl1, but
RT not Arfs.";
RL J. Biol. Chem. 286:11569-11578(2011).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=22981988; DOI=10.1016/j.devcel.2012.07.019;
RA Gehart H., Goginashvili A., Beck R., Morvan J., Erbs E., Formentini I.,
RA De Matteis M.A., Schwab Y., Wieland F.T., Ricci R.;
RT "The BAR domain protein Arfaptin-1 controls secretory granule biogenesis at
RT the trans-Golgi network.";
RL Dev. Cell 23:756-768(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND THR-76, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP FUNCTION, AND INTERACTION WITH IKBKG AND IKBKB.
RX PubMed=26296658; DOI=10.1016/j.cellsig.2015.08.012;
RA You D.J., Park C.R., Furlong M., Koo O., Lee C., Ahn C., Seong J.Y.,
RA Hwang J.I.;
RT "Dimer of arfaptin 2 regulates NF-kappaB signaling by interacting with
RT IKKbeta/NEMO and inhibiting IKKbeta kinase activity.";
RL Cell. Signal. 27:2173-2181(2015).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARL1.
RX PubMed=26507660; DOI=10.1074/jbc.m115.673582;
RA Eiseler T., Wille C., Koehler C., Illing A., Seufferlein T.;
RT "Protein Kinase D2 Assembles a Multiprotein Complex at the Trans-Golgi
RT Network to Regulate Matrix Metalloproteinase Secretion.";
RL J. Biol. Chem. 291:462-477(2016).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31204568; DOI=10.1080/15548627.2019.1632124;
RA Judith D., Tooze S.A.;
RT "ATG9A supplies PtdIns4P to the autophagosome initiation site.";
RL Autophagy 15:1660-1661(2019).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-99.
RX PubMed=30917996; DOI=10.1083/jcb.201901115;
RA Judith D., Jefferies H.B.J., Boeing S., Frith D., Snijders A.P.,
RA Tooze S.A.;
RT "ATG9A shapes the forming autophagosome through Arfaptin 2 and
RT phosphatidylinositol 4-kinase IIIbeta.";
RL J. Cell Biol. 218:1634-1652(2019).
RN [18]
RP FUNCTION.
RX PubMed=33773106; DOI=10.1016/j.molcel.2021.03.001;
RA Nguyen T.N., Padman B.S., Zellner S., Khuu G., Uoselis L., Lam W.K.,
RA Skulsuppaisarn M., Lindblom R.S.J., Watts E.M., Behrends C., Lazarou M.;
RT "ATG4 family proteins drive phagophore growth independently of the
RT LC3/GABARAP lipidation system.";
RL Mol. Cell 81:2013-2030(2021).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 118-341 IN COMPLEX WITH RAC1.
RX PubMed=11346801; DOI=10.1038/35075620;
RA Tarricone C., Xiao B., Justin N., Walker P.A., Rittinger K., Gamblin S.J.,
RA Smerdon S.J.;
RT "The structural basis of Arfaptin-mediated cross-talk between Rac and Arf
RT signalling pathways.";
RL Nature 411:215-219(2001).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 118-315, INTERACTION WITH ARL1,
RP AND SUBCELLULAR LOCATION.
RX PubMed=22679020; DOI=10.1074/jbc.m112.365783;
RA Nakamura K., Man Z., Xie Y., Hanai A., Makyio H., Kawasaki M., Kato R.,
RA Shin H.W., Nakayama K., Wakatsuki S.;
RT "Structural basis for membrane binding specificity of the
RT Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase.";
RL J. Biol. Chem. 287:25478-25489(2012).
CC -!- FUNCTION: Plays a role in constitutive metalloproteinase (MMP)
CC secretion from the trans Golgi network (PubMed:26507660). May have
CC important functions during vesicle biogenesis at certain cargo
CC subdomains, which could be predominantly utilized by secreted MMPs,
CC such as MMP7 and MMP2 (PubMed:26507660). Also involved in autophagy by
CC regulating the starvation-dependent trafficking of ATG9A vesicles which
CC deliver the phosphatidylinositol 4-kinase beta (PI4KB) to the
CC autophagosome initiation site (PubMed:31204568, PubMed:30917996).
CC Involved in phagophore growth during mitophagy by regulating ATG9A
CC trafficking to mitochondria (PubMed:33773106). In addition, plays a
CC role in NF-kappa-B inhibition by interacting with IKBKB and IKBKG
CC (PubMed:26296658). {ECO:0000269|PubMed:26296658,
CC ECO:0000269|PubMed:26507660, ECO:0000269|PubMed:30917996,
CC ECO:0000269|PubMed:31204568, ECO:0000269|PubMed:33773106}.
CC -!- SUBUNIT: Forms homodimers or heterodimers with ARFIP1
CC (PubMed:21239483). Interacts with RAC1 (PubMed:11346801). Specifically
CC binds to GTP-bound ARF1 and ARF6, but binds to RAC1.GTP and RAC1.GDP
CC with similar affinities. Interacts with ARL1 (PubMed:11303027,
CC PubMed:22679020, PubMed:26507660). Interacts (via N-terminus) with
CC IKBKB and IKBKG; these interactions inhibit activation of NF-kappa-B
CC (PubMed:26296658). {ECO:0000269|PubMed:11303027,
CC ECO:0000269|PubMed:11346801, ECO:0000269|PubMed:21239483,
CC ECO:0000269|PubMed:22679020, ECO:0000269|PubMed:26296658,
CC ECO:0000269|PubMed:26507660}.
CC -!- INTERACTION:
CC P53365; Q6RW13: AGTRAP; NbExp=4; IntAct=EBI-638194, EBI-741181;
CC P53365; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-638194, EBI-11522760;
CC P53365; P62330: ARF6; NbExp=4; IntAct=EBI-638194, EBI-638181;
CC P53365; P53367: ARFIP1; NbExp=3; IntAct=EBI-638194, EBI-2808808;
CC P53365; P53365: ARFIP2; NbExp=10; IntAct=EBI-638194, EBI-638194;
CC P53365; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-638194, EBI-465872;
CC P53365; Q9UFG5: C19orf25; NbExp=3; IntAct=EBI-638194, EBI-741214;
CC P53365; P51861: CDR1; NbExp=3; IntAct=EBI-638194, EBI-2836538;
CC P53365; Q96MT8: CEP63; NbExp=3; IntAct=EBI-638194, EBI-741977;
CC P53365; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-638194, EBI-11522780;
CC P53365; O43739-2: CYTH3; NbExp=3; IntAct=EBI-638194, EBI-11974015;
CC P53365; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-638194, EBI-12831978;
CC P53365; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-638194, EBI-399105;
CC P53365; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-638194, EBI-3943864;
CC P53365; A1L4K1: FSD2; NbExp=3; IntAct=EBI-638194, EBI-5661036;
CC P53365; Q08379: GOLGA2; NbExp=3; IntAct=EBI-638194, EBI-618309;
CC P53365; Q2KHT4-3: GSG1; NbExp=3; IntAct=EBI-638194, EBI-12951679;
CC P53365; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-638194, EBI-2514791;
CC P53365; O14964: HGS; NbExp=3; IntAct=EBI-638194, EBI-740220;
CC P53365; P42858: HTT; NbExp=3; IntAct=EBI-638194, EBI-466029;
CC P53365; Q8WYH8: ING5; NbExp=3; IntAct=EBI-638194, EBI-488533;
CC P53365; Q13352: ITGB3BP; NbExp=4; IntAct=EBI-638194, EBI-712105;
CC P53365; Q13352-5: ITGB3BP; NbExp=3; IntAct=EBI-638194, EBI-10175826;
CC P53365; P19012: KRT15; NbExp=6; IntAct=EBI-638194, EBI-739566;
CC P53365; P08779: KRT16; NbExp=3; IntAct=EBI-638194, EBI-356410;
CC P53365; P13473-2: LAMP2; NbExp=3; IntAct=EBI-638194, EBI-21591415;
CC P53365; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-638194, EBI-739832;
CC P53365; Q969L2: MAL2; NbExp=6; IntAct=EBI-638194, EBI-944295;
CC P53365; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-638194, EBI-740987;
CC P53365; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-638194, EBI-11988931;
CC P53365; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-638194, EBI-11978907;
CC P53365; Q16236: NFE2L2; NbExp=2; IntAct=EBI-638194, EBI-2007911;
CC P53365; Q9H7Z3: NRDE2; NbExp=3; IntAct=EBI-638194, EBI-1042642;
CC P53365; P37198: NUP62; NbExp=3; IntAct=EBI-638194, EBI-347978;
CC P53365; Q96AL5: PBX3; NbExp=3; IntAct=EBI-638194, EBI-741171;
CC P53365; Q96KN3: PKNOX2; NbExp=5; IntAct=EBI-638194, EBI-2692890;
CC P53365; Q04941: PLP2; NbExp=5; IntAct=EBI-638194, EBI-608347;
CC P53365; P30405: PPIF; NbExp=3; IntAct=EBI-638194, EBI-5544229;
CC P53365; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-638194, EBI-5280197;
CC P53365; P63000: RAC1; NbExp=13; IntAct=EBI-638194, EBI-413628;
CC P53365; P15153: RAC2; NbExp=3; IntAct=EBI-638194, EBI-489652;
CC P53365; P60763: RAC3; NbExp=3; IntAct=EBI-638194, EBI-767084;
CC P53365; Q00765: REEP5; NbExp=3; IntAct=EBI-638194, EBI-1549827;
CC P53365; Q04864-2: REL; NbExp=3; IntAct=EBI-638194, EBI-10829018;
CC P53365; Q92730: RND1; NbExp=3; IntAct=EBI-638194, EBI-448618;
CC P53365; O15126: SCAMP1; NbExp=3; IntAct=EBI-638194, EBI-954338;
CC P53365; Q8TAC9: SCAMP5; NbExp=3; IntAct=EBI-638194, EBI-2695784;
CC P53365; O00560: SDCBP; NbExp=3; IntAct=EBI-638194, EBI-727004;
CC P53365; Q9Y371: SH3GLB1; NbExp=6; IntAct=EBI-638194, EBI-2623095;
CC P53365; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-638194, EBI-2872322;
CC P53365; P08247: SYP; NbExp=3; IntAct=EBI-638194, EBI-9071725;
CC P53365; Q8WV15: TMEM255B; NbExp=3; IntAct=EBI-638194, EBI-2870087;
CC P53365; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-638194, EBI-2130429;
CC P53365; P49638: TTPA; NbExp=3; IntAct=EBI-638194, EBI-10210710;
CC P53365; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-638194, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:22981988}.
CC Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:21239483, ECO:0000269|PubMed:22679020,
CC ECO:0000269|PubMed:26507660, ECO:0000269|PubMed:30917996,
CC ECO:0000269|PubMed:31204568}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P53365-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P53365-2; Sequence=VSP_042524;
CC Name=3;
CC IsoId=P53365-3; Sequence=VSP_046913;
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; U52522; AAA97924.1; -; mRNA.
DR EMBL; AK301856; BAG63298.1; -; mRNA.
DR EMBL; AK304512; BAG65318.1; -; mRNA.
DR EMBL; AC084337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68707.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68708.1; -; Genomic_DNA.
DR EMBL; BC000392; AAH00392.1; -; mRNA.
DR EMBL; X97567; CAA66179.1; -; mRNA.
DR CCDS; CCDS55739.1; -. [P53365-2]
DR CCDS; CCDS55740.1; -. [P53365-3]
DR CCDS; CCDS7765.1; -. [P53365-1]
DR PIR; G02516; G02516.
DR RefSeq; NP_001229784.1; NM_001242855.1. [P53365-3]
DR RefSeq; NP_001229785.1; NM_001242856.1. [P53365-2]
DR RefSeq; NP_036534.1; NM_012402.3. [P53365-1]
DR RefSeq; XP_005252897.1; XM_005252840.4.
DR PDB; 1I49; X-ray; 2.80 A; A/B=118-341.
DR PDB; 1I4D; X-ray; 2.50 A; A/B=118-341.
DR PDB; 1I4L; X-ray; 2.70 A; A/B=118-341.
DR PDB; 1I4T; X-ray; 2.60 A; A/B=118-341.
DR PDB; 4DCN; X-ray; 3.01 A; C/D=118-315.
DR PDBsum; 1I49; -.
DR PDBsum; 1I4D; -.
DR PDBsum; 1I4L; -.
DR PDBsum; 1I4T; -.
DR PDBsum; 4DCN; -.
DR AlphaFoldDB; P53365; -.
DR SMR; P53365; -.
DR BioGRID; 117174; 98.
DR CORUM; P53365; -.
DR IntAct; P53365; 81.
DR MINT; P53365; -.
DR STRING; 9606.ENSP00000484121; -.
DR GlyGen; P53365; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P53365; -.
DR PhosphoSitePlus; P53365; -.
DR BioMuta; ARFIP2; -.
DR DMDM; 1703205; -.
DR EPD; P53365; -.
DR jPOST; P53365; -.
DR MassIVE; P53365; -.
DR MaxQB; P53365; -.
DR PaxDb; P53365; -.
DR PeptideAtlas; P53365; -.
DR PRIDE; P53365; -.
DR ProteomicsDB; 56573; -. [P53365-1]
DR ProteomicsDB; 56574; -. [P53365-2]
DR Antibodypedia; 23860; 239 antibodies from 27 providers.
DR DNASU; 23647; -.
DR Ensembl; ENST00000254584.6; ENSP00000254584.2; ENSG00000132254.13. [P53365-1]
DR Ensembl; ENST00000396777.8; ENSP00000379998.3; ENSG00000132254.13. [P53365-1]
DR Ensembl; ENST00000423813.6; ENSP00000398375.2; ENSG00000132254.13. [P53365-3]
DR Ensembl; ENST00000445086.6; ENSP00000391427.2; ENSG00000132254.13. [P53365-2]
DR GeneID; 23647; -.
DR KEGG; hsa:23647; -.
DR MANE-Select; ENST00000396777.8; ENSP00000379998.3; NM_001376558.2; NP_001363487.1.
DR UCSC; uc001mdk.4; human. [P53365-1]
DR CTD; 23647; -.
DR DisGeNET; 23647; -.
DR GeneCards; ARFIP2; -.
DR HGNC; HGNC:17160; ARFIP2.
DR HPA; ENSG00000132254; Low tissue specificity.
DR MIM; 601638; gene.
DR neXtProt; NX_P53365; -.
DR OpenTargets; ENSG00000132254; -.
DR PharmGKB; PA134879398; -.
DR VEuPathDB; HostDB:ENSG00000132254; -.
DR eggNOG; KOG3876; Eukaryota.
DR GeneTree; ENSGT00950000183040; -.
DR HOGENOM; CLU_047975_3_0_1; -.
DR InParanoid; P53365; -.
DR OMA; HTNSTEE; -.
DR PhylomeDB; P53365; -.
DR TreeFam; TF314945; -.
DR PathwayCommons; P53365; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; P53365; -.
DR SIGNOR; P53365; -.
DR BioGRID-ORCS; 23647; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; ARFIP2; human.
DR EvolutionaryTrace; P53365; -.
DR GeneWiki; ARFIP2; -.
DR GenomeRNAi; 23647; -.
DR Pharos; P53365; Tbio.
DR PRO; PR:P53365; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P53365; protein.
DR Bgee; ENSG00000132254; Expressed in olfactory segment of nasal mucosa and 193 other tissues.
DR ExpressionAtlas; P53365; baseline and differential.
DR Genevisible; P53365; HS.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IMP:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:FlyBase.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0140090; F:membrane curvature sensor activity; IDA:FlyBase.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:FlyBase.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; TAS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0030032; P:lamellipodium assembly; TAS:UniProtKB.
DR GO; GO:0000423; P:mitophagy; IMP:UniProtKB.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:UniProtKB.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0031529; P:ruffle organization; TAS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
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 3D-structure; Alternative splicing; Autophagy; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..341
FT /note="Arfaptin-2"
FT /id="PRO_0000064667"
FT DOMAIN 121..321
FT /note="AH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00294"
FT REGION 46..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..105
FT /note="MTDGILGKAATMEIPIHGNGEARQLPEDDGLEQDLQQVMVSGPNLNETSIVS
FT GGYGGSGDGLIPTGSGRHPSHSTTPSGPGDEVARGIAGEKFDIVKKWGINTYK -> MK
FT PALCLVAMGALVMDSSPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042524"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046913"
FT MUTAGEN 99
FT /note="W->A: Abolished ability to regulate ATG9A
FT trafficking."
FT /evidence="ECO:0000269|PubMed:30917996"
FT CONFLICT 225
FT /note="V -> A (in Ref. 2; BAG63298)"
FT /evidence="ECO:0000305"
FT HELIX 124..173
FT /evidence="ECO:0007829|PDB:1I4D"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1I4D"
FT HELIX 179..215
FT /evidence="ECO:0007829|PDB:1I4D"
FT HELIX 217..245
FT /evidence="ECO:0007829|PDB:1I4D"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1I4T"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:4DCN"
FT HELIX 260..316
FT /evidence="ECO:0007829|PDB:1I4D"
SQ SEQUENCE 341 AA; 37856 MW; AB8D224430D8E213 CRC64;
MTDGILGKAA TMEIPIHGNG EARQLPEDDG LEQDLQQVMV SGPNLNETSI VSGGYGGSGD
GLIPTGSGRH PSHSTTPSGP GDEVARGIAG EKFDIVKKWG INTYKCTKQL LSERFGRGSR
TVDLELELQI ELLRETKRKY ESVLQLGRAL TAHLYSLLQT QHALGDAFAD LSQKSPELQE
EFGYNAETQK LLCKNGETLL GAVNFFVSSI NTLVTKTMED TLMTVKQYEA ARLEYDAYRT
DLEELSLGPR DAGTRGRLES AQATFQAHRD KYEKLRGDVA IKLKFLEENK IKVMHKQLLL
FHNAVSAYFA GNQKQLEQTL QQFNIKLRPP GAEKPSWLEE Q
