ID ARFP1_HUMAN Reviewed; 373 AA. AC P53367; B4DS69; Q2M2X4; Q3SYL4; Q9Y2X6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 2. DT 27-MAR-2024, entry version 182. DE RecName: Full=Arfaptin-1 {ECO:0000303|PubMed:9038142}; DE AltName: Full=ADP-ribosylation factor-interacting protein 1 {ECO:0000303|PubMed:9038142}; GN Name=ARFIP1 {ECO:0000303|PubMed:22981988, GN ECO:0000312|HGNC:HGNC:21496}; 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 A), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. 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 [MRNA] (ISOFORM B). RC TISSUE=Liver; RA Premont R.T., Lefkowitz R.J.; RT "Arfaptin-1b, a long splice variant of arfaptin-1."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND 3). RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B). RC TISSUE=Brain, and Uterus; 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 [7] RP INTERACTION WITH ARF1; ARF3; ARF5 AND ARF6. RX PubMed=10413101; DOI=10.1016/s0014-5793(99)00771-1; RA Williger B.-T., Provost J.J., Ho W.-T., Milstine J., Exton J.H.; RT "Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits RT phospholipase D."; RL FEBS Lett. 454:85-89(1999). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-132, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-361, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-5; SER-69 AND SER-79, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 [11] 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-132, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP SUBCELLULAR LOCATION, INTERACTION WITH ARL1 AND ARFIP2, 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 [14] RP FUNCTION, PHOSPHORYLATION AT SER-132, MUTAGENESIS OF SER-132, SUBCELLULAR RP LOCATION, AND INTERACTION WITH ARF1 AND ARL1. 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-28; SER-39 AND RP SER-132, AND 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, AND 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 [18] RP INTERACTION WITH ATG9A. 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). CC -!- FUNCTION: Plays a role in controlling biogenesis of secretory granules CC at the trans-Golgi network (PubMed:22981988). Mechanistically, binds CC ARF-GTP at the neck of a growing secretory granule precursor and forms CC a protective scaffold (PubMed:9038142, PubMed:22981988). Once the CC granule precursor has been completely loaded, active PRKD1 CC phosphorylates ARFIP1 and releases it from ARFs (PubMed:22981988). In CC turn, ARFs induce fission (PubMed:22981988). Through this mechanism, CC ensures proper secretory granule formation at the Golgi of pancreatic CC beta cells (PubMed:22981988). {ECO:0000269|PubMed:22981988, CC ECO:0000269|PubMed:9038142}. CC -!- SUBUNIT: Forms homodimers or heterodimers with ARFIP2 CC (PubMed:21239483). Interacts with non-myristoylated GTP-bound ARF3, but CC not to GDP-bound ARF3 (PubMed:10413101). Interacts with ARF1 CC (PubMed:10413101, PubMed:22981988). Binds with lower affinity to ARF5 CC and with very little affinity to ARF6 (PubMed:10413101). Interacts with CC ARL1 (PubMed:22981988, PubMed:21239483). Interacts with ATG9A CC (PubMed:30917996). {ECO:0000269|PubMed:10413101, CC ECO:0000269|PubMed:21239483, ECO:0000269|PubMed:22981988, CC ECO:0000269|PubMed:30917996}. CC -!- INTERACTION: CC P53367; P51825-3: AFF1; NbExp=3; IntAct=EBI-2808808, EBI-24213872; CC P53367; P84077: ARF1; NbExp=2; IntAct=EBI-2808808, EBI-447171; CC P53367; P53365: ARFIP2; NbExp=3; IntAct=EBI-2808808, EBI-638194; CC P53367; P40616: ARL1; NbExp=2; IntAct=EBI-2808808, EBI-1052746; CC P53367; Q8WZ55: BSND; NbExp=5; IntAct=EBI-2808808, EBI-7996695; CC P53367; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2808808, EBI-11522780; CC P53367; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-2808808, EBI-12878374; CC P53367; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2808808, EBI-3044087; CC P53367; Q14525: KRT33B; NbExp=3; IntAct=EBI-2808808, EBI-1049638; CC P53367; P43360: MAGEA6; NbExp=3; IntAct=EBI-2808808, EBI-1045155; CC P53367; Q15139: PRKD1; NbExp=2; IntAct=EBI-2808808, EBI-1181072; CC P53367; Q9NS64: RPRM; NbExp=3; IntAct=EBI-2808808, EBI-1052363; CC P53367; O15126: SCAMP1; NbExp=3; IntAct=EBI-2808808, EBI-954338; CC P53367; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-2808808, EBI-2854842; CC P53367; Q71RC9: SMIM5; NbExp=3; IntAct=EBI-2808808, EBI-12334905; CC P53367; O60906: SMPD2; NbExp=3; IntAct=EBI-2808808, EBI-12828299; CC P53367; O43761: SYNGR3; NbExp=3; IntAct=EBI-2808808, EBI-11321949; CC P53367; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-2808808, EBI-1044859; CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:22981988, CC ECO:0000269|PubMed:9038142}. Golgi apparatus, trans-Golgi network CC membrane {ECO:0000269|PubMed:21239483, ECO:0000269|PubMed:30917996}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=B; Synonyms=1b; CC IsoId=P53367-1; Sequence=Displayed; CC Name=A; Synonyms=1a; CC IsoId=P53367-2; Sequence=VSP_004088; CC Name=3; CC IsoId=P53367-3; Sequence=VSP_057425; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:9038142). Higher CC levels in liver, pancreas, placenta, skeletal muscle and heart CC (PubMed:9038142). {ECO:0000269|PubMed:9038142}. 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:0000269|PubMed:22981988}. 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; U52521; AAA97923.1; -; mRNA. DR EMBL; AF124489; AAD29390.1; -; mRNA. DR EMBL; AK290472; BAF83161.1; -; mRNA. DR EMBL; AK299600; BAG61531.1; -; mRNA. DR EMBL; AC099339; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC106882; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC113155; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471056; EAX04968.1; -; Genomic_DNA. DR EMBL; CH471056; EAX04969.1; -; Genomic_DNA. DR EMBL; BC103759; AAI03760.1; -; mRNA. DR EMBL; BC105114; AAI05115.1; -; mRNA. DR EMBL; BC105116; AAI05117.1; -; mRNA. DR EMBL; BC143675; AAI43676.1; -; mRNA. DR CCDS; CCDS34080.1; -. [P53367-1] DR CCDS; CCDS3780.1; -. [P53367-2] DR PIR; G02515; G02515. DR RefSeq; NP_001020764.1; NM_001025593.2. [P53367-2] DR RefSeq; NP_001020766.1; NM_001025595.2. [P53367-1] DR RefSeq; NP_001274360.1; NM_001287431.1. [P53367-1] DR RefSeq; NP_001274361.1; NM_001287432.1. [P53367-1] DR RefSeq; NP_001274362.1; NM_001287433.1. [P53367-2] DR RefSeq; NP_055262.1; NM_014447.3. [P53367-2] DR RefSeq; XP_011530171.1; XM_011531869.2. DR RefSeq; XP_011530172.1; XM_011531870.2. DR AlphaFoldDB; P53367; -. DR SMR; P53367; -. DR BioGRID; 118084; 141. DR IntAct; P53367; 35. DR MINT; P53367; -. DR STRING; 9606.ENSP00000296557; -. DR GlyGen; P53367; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P53367; -. DR MetOSite; P53367; -. DR PhosphoSitePlus; P53367; -. DR BioMuta; ARFIP1; -. DR DMDM; 21264399; -. DR EPD; P53367; -. DR jPOST; P53367; -. DR MassIVE; P53367; -. DR MaxQB; P53367; -. DR PaxDb; 9606-ENSP00000395083; -. DR PeptideAtlas; P53367; -. DR ProteomicsDB; 5003; -. DR ProteomicsDB; 56575; -. [P53367-1] DR ProteomicsDB; 56576; -. [P53367-2] DR Pumba; P53367; -. DR Antibodypedia; 3910; 283 antibodies from 31 providers. DR DNASU; 27236; -. DR Ensembl; ENST00000353617.7; ENSP00000296557.4; ENSG00000164144.16. [P53367-1] DR Ensembl; ENST00000356064.3; ENSP00000348360.3; ENSG00000164144.16. [P53367-2] DR Ensembl; ENST00000405727.6; ENSP00000384189.2; ENSG00000164144.16. [P53367-2] DR Ensembl; ENST00000429148.6; ENSP00000396653.2; ENSG00000164144.16. [P53367-3] DR Ensembl; ENST00000451320.6; ENSP00000395083.2; ENSG00000164144.16. [P53367-1] DR GeneID; 27236; -. DR KEGG; hsa:27236; -. DR MANE-Select; ENST00000353617.7; ENSP00000296557.4; NM_001025595.3; NP_001020766.1. DR UCSC; uc003imz.5; human. [P53367-1] DR UCSC; uc011cij.4; human. DR AGR; HGNC:21496; -. DR CTD; 27236; -. DR DisGeNET; 27236; -. DR GeneCards; ARFIP1; -. DR HGNC; HGNC:21496; ARFIP1. DR HPA; ENSG00000164144; Low tissue specificity. DR MIM; 605928; gene. DR neXtProt; NX_P53367; -. DR OpenTargets; ENSG00000164144; -. DR PharmGKB; PA134920621; -. DR VEuPathDB; HostDB:ENSG00000164144; -. DR eggNOG; KOG3876; Eukaryota. DR GeneTree; ENSGT00950000183040; -. DR HOGENOM; CLU_047975_2_0_1; -. DR InParanoid; P53367; -. DR OMA; ESHEHGF; -. DR OrthoDB; 5166950at2759; -. DR PhylomeDB; P53367; -. DR TreeFam; TF314945; -. DR PathwayCommons; P53367; -. DR SignaLink; P53367; -. DR SIGNOR; P53367; -. DR BioGRID-ORCS; 27236; 15 hits in 1145 CRISPR screens. DR ChiTaRS; ARFIP1; human. DR GeneWiki; ARFIP1; -. DR GenomeRNAi; 27236; -. DR Pharos; P53367; Tbio. DR PRO; PR:P53367; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P53367; Protein. DR Bgee; ENSG00000164144; Expressed in secondary oocyte and 199 other cell types or tissues. DR ExpressionAtlas; P53367; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0032588; C:trans-Golgi network membrane; 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:0006886; P:intracellular protein transport; IDA:MGI. DR GO; GO:1905280; P:negative regulation of retrograde transport, endosome to Golgi; IMP:CACAO. 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; IDA:MGI. DR CDD; cd07660; BAR_Arfaptin; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR010504; AH_dom. DR InterPro; IPR030798; Arfaptin_fam. DR PANTHER; PTHR12141:SF4; ARFAPTIN-1; 1. DR PANTHER; PTHR12141; ARFAPTIN-RELATED; 1. DR Pfam; PF06456; Arfaptin; 1. DR SMART; SM01015; Arfaptin; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR PROSITE; PS50870; AH; 1. DR Genevisible; P53367; HS. 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:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378" FT CHAIN 2..373 FT /note="Arfaptin-1" FT /id="PRO_0000064665" 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:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 28 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 69 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 79 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22981988, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 361 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT VAR_SEQ 32..211 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057425" FT VAR_SEQ 69..100 FT /note="Missing (in isoform A)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9038142" FT /id="VSP_004088" FT MUTAGEN 132 FT /note="S->A: Complete loss of phosphorylation by PRKD1." FT /evidence="ECO:0000269|PubMed:22981988" SQ SEQUENCE 373 AA; 41738 MW; 7A315D0E67DECDBF CRC64; MAQESPKNSA AEIPVTSNGE VDDSREHSFN RDLKHSLPSG LGLSETQITS HGFDNTKEGV IEAGAFQGSP APPLPSVMSP SRVAASRLAQ QGSDLIVPAG GQRTQTKSGP VILADEIKNP AMEKLELVRK WSLNTYKCTR QIISEKLGRG SRTVDLELEA QIDILRDNKK KYENILKLAQ TLSTQLFQMV HTQRQLGDAF ADLSLKSLEL HEEFGYNADT QKLLAKNGET LLGAINFFIA SVNTLVNKTI EDTLMTVKQY ESARIEYDAY RTDLEELNLG PRDANTLPKI EQSQHLFQAH KEKYDKMRND VSVKLKFLEE NKVKVLHNQL VLFHNAIAAY FAGNQKQLEQ TLKQFHIKLK TPGVDAPSWL EEQ //