AGFG1_MOUSE
ID AGFG1_MOUSE Reviewed; 561 AA.
AC Q8K2K6; O70448; Q8BQL5; Q8CDK9;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Arf-GAP domain and FG repeat-containing protein 1;
DE AltName: Full=HIV-1 Rev-binding protein homolog;
DE AltName: Full=Nucleoporin-like protein RIP;
GN Name=Agfg1; Synonyms=Hrb, Rip;
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] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Head, and Testis;
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] (ISOFORM 1).
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 INTERACTION WITH EPS15R.
RX PubMed=9446614; DOI=10.1074/jbc.273.5.3003;
RA Coda L., Salcini A.E., Confalonieri S., Pelicci G., Sorkina T., Sorkin A.,
RA Pelicci P.G., Di Fiore P.P.;
RT "Eps15R is a tyrosine kinase substrate with characteristics of a docking
RT protein possibly involved in coated pits-mediated internalization.";
RL J. Biol. Chem. 273:3003-3012(1998).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH
RP EPS15, AND DISRUPTION PHENOTYPE.
RX PubMed=11711676; DOI=10.1126/science.1063665;
RA Kang-Decker N., Mantchev G.T., Juneja S.C., McNiven M.A.,
RA van Deursen J.M.A.;
RT "Lack of acrosome formation in Hrb-deficient mice.";
RL Science 294:1531-1533(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Required for vesicle docking or fusion during acrosome
CC biogenesis. May play a role in RNA trafficking or localization.
CC {ECO:0000269|PubMed:11711676}.
CC -!- SUBUNIT: Interacts with FCHO1 (By similarity). Interacts with EPS15R
CC and EPS15. {ECO:0000250, ECO:0000269|PubMed:11711676,
CC ECO:0000269|PubMed:9446614}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52594}.
CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:P52594}. Note=Associated
CC with the cytosolic surface of proacrosomic vesicles of early round
CC spermatids. {ECO:0000269|PubMed:11711676}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=Q8K2K6-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8K2K6-1; Sequence=VSP_017602;
CC Name=2;
CC IsoId=Q8K2K6-2; Sequence=VSP_010664;
CC Name=3;
CC IsoId=Q8K2K6-3; Sequence=VSP_010665;
CC -!- DEVELOPMENTAL STAGE: Highly expressed during spermiogenesis.
CC {ECO:0000269|PubMed:11711676}.
CC -!- DOMAIN: Contains FG repeats.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice have a normal life-span and show no apparent
CC abnormalities. Females display normal fertility but males are infertile
CC due to a lack of acrosome in their spermatozoa.
CC {ECO:0000269|PubMed:11711676}.
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DR EMBL; AK049400; BAC33736.1; -; mRNA.
DR EMBL; AK029917; BAC26675.1; -; mRNA.
DR EMBL; AK048326; BAC33303.1; -; mRNA.
DR EMBL; AF057287; AAC97477.1; -; mRNA.
DR EMBL; BC031154; AAH31154.1; -; mRNA.
DR CCDS; CCDS15100.1; -. [Q8K2K6-1]
DR CCDS; CCDS78634.1; -. [Q8K2K6-3]
DR CCDS; CCDS87854.1; -. [Q8K2K6-4]
DR RefSeq; NP_001297642.1; NM_001310713.1. [Q8K2K6-3]
DR RefSeq; NP_034602.1; NM_010472.3. [Q8K2K6-1]
DR RefSeq; XP_006496496.1; XM_006496433.3.
DR AlphaFoldDB; Q8K2K6; -.
DR BioGRID; 200417; 14.
DR ELM; Q8K2K6; -.
DR STRING; 10090.ENSMUSP00000140785; -.
DR GlyGen; Q8K2K6; 1 site.
DR iPTMnet; Q8K2K6; -.
DR PhosphoSitePlus; Q8K2K6; -.
DR EPD; Q8K2K6; -.
DR jPOST; Q8K2K6; -.
DR MaxQB; Q8K2K6; -.
DR PaxDb; Q8K2K6; -.
DR PeptideAtlas; Q8K2K6; -.
DR PRIDE; Q8K2K6; -.
DR ProteomicsDB; 285562; -. [Q8K2K6-4]
DR ProteomicsDB; 285563; -. [Q8K2K6-1]
DR ProteomicsDB; 285564; -. [Q8K2K6-2]
DR ProteomicsDB; 285565; -. [Q8K2K6-3]
DR Antibodypedia; 1598; 225 antibodies from 30 providers.
DR DNASU; 15463; -.
DR Ensembl; ENSMUST00000063380; ENSMUSP00000070250; ENSMUSG00000026159. [Q8K2K6-2]
DR Ensembl; ENSMUST00000113444; ENSMUSP00000109071; ENSMUSG00000026159. [Q8K2K6-3]
DR Ensembl; ENSMUST00000186302; ENSMUSP00000140785; ENSMUSG00000026159. [Q8K2K6-4]
DR Ensembl; ENSMUST00000189220; ENSMUSP00000140170; ENSMUSG00000026159. [Q8K2K6-1]
DR GeneID; 15463; -.
DR KEGG; mmu:15463; -.
DR UCSC; uc007bse.1; mouse. [Q8K2K6-1]
DR UCSC; uc007bsf.1; mouse. [Q8K2K6-2]
DR UCSC; uc007bsg.1; mouse. [Q8K2K6-3]
DR CTD; 3267; -.
DR MGI; MGI:1333754; Agfg1.
DR VEuPathDB; HostDB:ENSMUSG00000026159; -.
DR eggNOG; KOG0702; Eukaryota.
DR GeneTree; ENSGT00940000155511; -.
DR HOGENOM; CLU_027801_1_0_1; -.
DR InParanoid; Q8K2K6; -.
DR OMA; WRSKHDP; -.
DR OrthoDB; 1226524at2759; -.
DR PhylomeDB; Q8K2K6; -.
DR TreeFam; TF325357; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 15463; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Agfg1; mouse.
DR PRO; PR:Q8K2K6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8K2K6; protein.
DR Bgee; ENSMUSG00000026159; Expressed in placenta labyrinth and 258 other tissues.
DR ExpressionAtlas; Q8K2K6; baseline and differential.
DR Genevisible; Q8K2K6; MM.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0001675; P:acrosome assembly; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IMP:MGI.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IMP:MGI.
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 Alternative splicing; Cytoplasmic vesicle; Developmental protein;
KW Differentiation; DNA-binding; Glycoprotein; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Spermatogenesis; Transport;
KW Zinc; Zinc-finger.
FT CHAIN 1..561
FT /note="Arf-GAP domain and FG repeat-containing protein 1"
FT /id="PRO_0000204905"
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 170..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52594"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52594"
FT CARBOHYD 367
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 342..362
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010664"
FT VAR_SEQ 428..458
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010665"
FT VAR_SEQ 513..514
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017602"
FT CONFLICT 2..4
FT /note="AAS -> GGR (in Ref. 1; BAC33736)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="Q -> P (in Ref. 1; BAC33736)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="Q -> H (in Ref. 1; BAC33736)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="T -> R (in Ref. 1; BAC33736)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="R -> K (in Ref. 1; BAC33736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 58043 MW; B612D82F0051ECFF CRC64;
MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN
PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK
YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGESAPA LHLNKGTPSQ
SPVVGRSQGQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANADF
ANFDAFGQSS GSSNFGGFPT ASHSSFQPQT TGGSAGSVNA NFAHFDNFPK SSSADFGTFS
TSQSHQTAST VSKVSTNKAG LQTADKYAAL ANLDNIFSAG QGGDQGSGFG TTGKAPVGSV
VSVPSHSSAS SDKYAALAEL DSVFSSAATS SNAYTPTSNA SSSVFGTVPV GASAQTQPAS
SGPAPFGATP STNPFVAATG PSAASSTNPF QTNARGATAA TFGTASMSMP AGFGTPAQYS
LPTSFSGSFQ QPAFPAQAAF PQQTAFSQQP NGAGFATFGQ TKPVVTPFGQ VAAAGVSSNP
FMTGAPTGQL PTGSSSTNPF L
