ARFP1_HUMAN
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 03-AUG-2022, entry version 173.
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, 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). Mechanisitically, 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}.
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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. [P53367-1]
DR RefSeq; XP_011530172.1; XM_011531870.2. [P53367-1]
DR AlphaFoldDB; P53367; -.
DR SMR; P53367; -.
DR BioGRID; 118084; 125.
DR IntAct; P53367; 34.
DR MINT; P53367; -.
DR STRING; 9606.ENSP00000395083; -.
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; P53367; -.
DR PeptideAtlas; P53367; -.
DR PRIDE; P53367; -.
DR ProteomicsDB; 5003; -.
DR ProteomicsDB; 56575; -. [P53367-1]
DR ProteomicsDB; 56576; -. [P53367-2]
DR Antibodypedia; 3910; 256 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 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; HLFQVHK; -.
DR PhylomeDB; P53367; -.
DR TreeFam; TF314945; -.
DR PathwayCommons; P53367; -.
DR SignaLink; P53367; -.
DR SIGNOR; P53367; -.
DR BioGRID-ORCS; 27236; 13 hits in 1069 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 197 other tissues.
DR ExpressionAtlas; P53367; baseline and differential.
DR Genevisible; P53367; HS.
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 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; 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
