AGFG1_HUMAN
ID AGFG1_HUMAN Reviewed; 562 AA.
AC P52594; B3KUL1; E9PHX7; Q15277; Q4VAS0; Q4VAS1; Q4VAS3; Q53QT8; Q53R11;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Arf-GAP domain and FG repeat-containing protein 1;
DE AltName: Full=HIV-1 Rev-binding protein;
DE AltName: Full=Nucleoporin-like protein RIP;
DE AltName: Full=Rev-interacting protein;
DE AltName: Full=Rev/Rex activation domain-binding protein;
GN Name=AGFG1; Synonyms=HRB, RAB, RIP;
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 [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
RP INTERACTION WITH HIV-1 REV AND HTLV-1 REX, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=7634337; DOI=10.1016/0092-8674(95)90437-9;
RA Bogerd H.P., Fridell R.A., Madore S., Cullen B.R.;
RT "Identification of a novel cellular cofactor for the Rev/Rex class of
RT retroviral regulatory proteins.";
RL Cell 82:485-494(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HIV-1 REV.
RC TISSUE=Placenta;
RX PubMed=7637788; DOI=10.1038/376530a0;
RA Fritz C.C., Zapp M.L., Green M.R.;
RT "A human nucleoporin-like protein that specifically interacts with HIV
RT Rev.";
RL Nature 376:530-533(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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 MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Testis;
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 SUBCELLULAR LOCATION, INTERACTION WITH EPS15, AND FUNCTION.
RX PubMed=10613896; DOI=10.1083/jcb.147.7.1379;
RA Doria M., Salcini A.E., Colombo E., Parslow T.G., Pelicci P.G.,
RA Di Fiore P.P.;
RT "The eps15 homology (EH) domain-based interaction between eps15 and hrb
RT connects the molecular machinery of endocytosis to that of nucleocytosolic
RT transport.";
RL J. Cell Biol. 147:1379-1384(1999).
RN [7]
RP FUNCTION.
RX PubMed=14701878; DOI=10.1101/gad.1149704;
RA Sanchez-Velar N., Udofia E.B., Yu Z., Zapp M.L.;
RT "hRIP, a cellular cofactor for Rev function, promotes release of HIV RNAs
RT from the perinuclear region.";
RL Genes Dev. 18:23-34(2004).
RN [8]
RP FUNCTION.
RX PubMed=15749819; DOI=10.1073/pnas.0408889102;
RA Yu Z., Sanchez-Velar N., Catrina I.E., Kittler E.L., Udofia E.B.,
RA Zapp M.L.;
RT "The cellular HIV-1 Rev cofactor hRIP is required for viral replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4027-4032(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP 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 [17]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; THR-177; SER-181 AND
RP SER-362, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP 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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP STRUCTURE BY NMR OF 14-134.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ARFGAP domain of human RIP.";
RL Submitted (DEC-2006) to the PDB data bank.
CC -!- FUNCTION: Required for vesicle docking or fusion during acrosome
CC biogenesis (By similarity). May play a role in RNA trafficking or
CC localization. In case of infection by HIV-1, acts as a cofactor for
CC viral Rev and promotes movement of Rev-responsive element-containing
CC RNAs from the nuclear periphery to the cytoplasm. This step is
CC essential for HIV-1 replication. {ECO:0000250,
CC ECO:0000269|PubMed:10613896, ECO:0000269|PubMed:14701878,
CC ECO:0000269|PubMed:15749819}.
CC -!- SUBUNIT: Interacts with EPS15R and EPS15. Interacts with FCHO1.
CC {ECO:0000269|PubMed:10613896, ECO:0000269|PubMed:22484487,
CC ECO:0000269|PubMed:7634337, ECO:0000269|PubMed:7637788}.
CC -!- INTERACTION:
CC P52594; P63010: AP2B1; NbExp=2; IntAct=EBI-996560, EBI-432924;
CC P52594; P42566: EPS15; NbExp=3; IntAct=EBI-996560, EBI-396684;
CC P52594; Q9P242: NYAP2; NbExp=3; IntAct=EBI-996560, EBI-10269689;
CC P52594; P56282: POLE2; NbExp=3; IntAct=EBI-996560, EBI-713847;
CC P52594; Q93009: USP7; NbExp=2; IntAct=EBI-996560, EBI-302474;
CC P52594; P51809: VAMP7; NbExp=7; IntAct=EBI-996560, EBI-1052205;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10613896,
CC ECO:0000269|PubMed:7634337}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:10613896}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P52594-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52594-2; Sequence=VSP_017600;
CC Name=3;
CC IsoId=P52594-3; Sequence=VSP_017601;
CC Name=4;
CC IsoId=P52594-4; Sequence=VSP_046186, VSP_017601;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:7634337}.
CC -!- DOMAIN: Contains FG repeats. The FG repeat region is required for
CC acting as a cofactor of HIV-1 Rev.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG53473.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing within exon 1.; Evidence={ECO:0000305};
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DR EMBL; L42025; AAC37580.1; -; Genomic_DNA.
DR EMBL; X89478; CAA61667.1; -; mRNA.
DR EMBL; AK097451; BAG53473.1; ALT_SEQ; mRNA.
DR EMBL; AC105286; AAX93270.1; -; Genomic_DNA.
DR EMBL; AC097662; AAY24254.1; -; Genomic_DNA.
DR EMBL; BC030592; AAH30592.1; -; mRNA.
DR EMBL; BC096272; AAH96272.1; -; mRNA.
DR EMBL; BC096273; AAH96273.1; -; mRNA.
DR EMBL; BC096274; AAH96274.1; -; mRNA.
DR EMBL; BC096275; AAH96275.1; -; mRNA.
DR CCDS; CCDS2467.1; -. [P52594-1]
DR CCDS; CCDS46533.1; -. [P52594-4]
DR CCDS; CCDS46534.1; -. [P52594-3]
DR CCDS; CCDS46535.1; -. [P52594-2]
DR PIR; A57088; A57088.
DR RefSeq; NP_001128659.1; NM_001135187.1. [P52594-4]
DR RefSeq; NP_001128660.1; NM_001135188.1. [P52594-3]
DR RefSeq; NP_001128661.1; NM_001135189.1. [P52594-2]
DR RefSeq; NP_004495.2; NM_004504.4. [P52594-1]
DR PDB; 2D9L; NMR; -; A=14-134.
DR PDB; 2OLM; X-ray; 1.48 A; A=4-141.
DR PDB; 2VX8; X-ray; 2.20 A; A/B/C/D=136-175.
DR PDBsum; 2D9L; -.
DR PDBsum; 2OLM; -.
DR PDBsum; 2VX8; -.
DR AlphaFoldDB; P52594; -.
DR SMR; P52594; -.
DR BioGRID; 109503; 86.
DR DIP; DIP-35546N; -.
DR ELM; P52594; -.
DR IntAct; P52594; 19.
DR MINT; P52594; -.
DR STRING; 9606.ENSP00000387282; -.
DR GlyGen; P52594; 36 sites, 2 O-linked glycans (36 sites).
DR iPTMnet; P52594; -.
DR PhosphoSitePlus; P52594; -.
DR BioMuta; AGFG1; -.
DR DMDM; 26007019; -.
DR EPD; P52594; -.
DR jPOST; P52594; -.
DR MassIVE; P52594; -.
DR MaxQB; P52594; -.
DR PaxDb; P52594; -.
DR PeptideAtlas; P52594; -.
DR PRIDE; P52594; -.
DR ProteomicsDB; 20621; -.
DR ProteomicsDB; 56494; -. [P52594-1]
DR ProteomicsDB; 56495; -. [P52594-2]
DR ProteomicsDB; 56496; -. [P52594-3]
DR Antibodypedia; 1598; 225 antibodies from 30 providers.
DR DNASU; 3267; -.
DR Ensembl; ENST00000310078.13; ENSP00000312059.7; ENSG00000173744.18. [P52594-1]
DR Ensembl; ENST00000373671.7; ENSP00000362775.3; ENSG00000173744.18. [P52594-2]
DR Ensembl; ENST00000409171.5; ENSP00000387218.1; ENSG00000173744.18. [P52594-3]
DR Ensembl; ENST00000409979.6; ENSP00000387282.2; ENSG00000173744.18. [P52594-4]
DR GeneID; 3267; -.
DR KEGG; hsa:3267; -.
DR MANE-Select; ENST00000310078.13; ENSP00000312059.7; NM_004504.5; NP_004495.2.
DR UCSC; uc002vpc.3; human. [P52594-1]
DR CTD; 3267; -.
DR DisGeNET; 3267; -.
DR GeneCards; AGFG1; -.
DR HGNC; HGNC:5175; AGFG1.
DR HPA; ENSG00000173744; Low tissue specificity.
DR MIM; 600862; gene.
DR neXtProt; NX_P52594; -.
DR OpenTargets; ENSG00000173744; -.
DR PharmGKB; PA29449; -.
DR VEuPathDB; HostDB:ENSG00000173744; -.
DR eggNOG; KOG0702; Eukaryota.
DR GeneTree; ENSGT00940000155511; -.
DR InParanoid; P52594; -.
DR OMA; WRSKHDP; -.
DR PhylomeDB; P52594; -.
DR TreeFam; TF325357; -.
DR PathwayCommons; P52594; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P52594; -.
DR BioGRID-ORCS; 3267; 20 hits in 1088 CRISPR screens.
DR ChiTaRS; AGFG1; human.
DR EvolutionaryTrace; P52594; -.
DR GeneWiki; HRB_(gene); -.
DR GenomeRNAi; 3267; -.
DR Pharos; P52594; Tbio.
DR PRO; PR:P52594; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P52594; protein.
DR Bgee; ENSG00000173744; Expressed in sperm and 204 other tissues.
DR ExpressionAtlas; P52594; baseline and differential.
DR Genevisible; P52594; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0001675; P:acrosome assembly; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; TAS:ProtInc.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IBA:GO_Central.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasmic vesicle;
KW Developmental protein; Differentiation; DNA-binding; Glycoprotein;
KW Metal-binding; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Spermatogenesis; Transport; Zinc; Zinc-finger.
FT CHAIN 1..562
FT /note="Arf-GAP domain and FG repeat-containing protein 1"
FT /id="PRO_0000204904"
FT DOMAIN 11..135
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 29..52
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 145..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 367
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 232..271
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017600"
FT VAR_SEQ 272
FT /note="G -> AFRMLSSSCSFGEFTSAFPLQATHS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046186"
FT VAR_SEQ 513..514
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017601"
FT CONFLICT 25
FT /note="H -> R (in Ref. 2; CAA61667)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="A -> R (in Ref. 2; CAA61667)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="F -> S (in Ref. 3; BAG53473)"
FT /evidence="ECO:0000305"
FT HELIX 4..21
FT /evidence="ECO:0007829|PDB:2OLM"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:2OLM"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2OLM"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2OLM"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:2OLM"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2OLM"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:2OLM"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2OLM"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2OLM"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2OLM"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:2OLM"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:2OLM"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2OLM"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2OLM"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:2OLM"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:2OLM"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2VX8"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:2VX8"
SQ SEQUENCE 562 AA; 58260 MW; 9A2242217F53B4D9 CRC64;
MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN
PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK
YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGDSAPT LHLNKGTPSQ
SPVVGRSQGQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANADF
ANFDAFGQSS GSSNFGGFPT ASHSPFQPQT TGGSAASVNA NFAHFDNFPK SSSADFGTFN
TSQSHQTASA VSKVSTNKAG LQTADKYAAL ANLDNIFSAG QGGDQGSGFG TTGKAPVGSV
VSVPSQSSAS SDKYAALAEL DSVFSSAATS SNAYTSTSNA SSNVFGTVPV VASAQTQPAS
SSVPAPFGAT PSTNPFVAAA GPSVASSTNP FQTNARGATA ATFGTASMSM PTGFGTPAPY
SLPTSFSGSF QQPAFPAQAA FPQQTAFSQQ PNGAGFAAFG QTKPVVTPFG QVAAAGVSSN
PFMTGAPTGQ FPTGSSSTNP FL
