AGFG1_RAT
ID AGFG1_RAT Reviewed; 561 AA.
AC Q4KLH5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=Agfg1-ps1, Hrb, Rip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PROTEIN SEQUENCE OF 355-373, GLYCOSYLATION AT SER-367, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=15340146; DOI=10.1073/pnas.0403471101;
RA Khidekel N., Ficarro S.B., Peters E.C., Hsieh-Wilson L.C.;
RT "Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-
RT modified proteins from the brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13132-13137(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Required for vesicle docking or fusion during acrosome
CC biogenesis. May play a role in RNA trafficking or localization (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EPS15R and EPS15. Interacts with FCHO1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52594}.
CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:P52594}.
CC -!- DOMAIN: Contains FG repeats.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:15340146}.
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DR EMBL; BC099202; AAH99202.1; -; mRNA.
DR RefSeq; NP_001129068.1; NM_001135596.1.
DR AlphaFoldDB; Q4KLH5; -.
DR IntAct; Q4KLH5; 2.
DR STRING; 10116.ENSRNOP00000021309; -.
DR GlyGen; Q4KLH5; 1 site.
DR iPTMnet; Q4KLH5; -.
DR PhosphoSitePlus; Q4KLH5; -.
DR jPOST; Q4KLH5; -.
DR PaxDb; Q4KLH5; -.
DR PRIDE; Q4KLH5; -.
DR GeneID; 363266; -.
DR KEGG; rno:363266; -.
DR CTD; 3267; -.
DR RGD; 1560041; Agfg1.
DR eggNOG; KOG0702; Eukaryota.
DR InParanoid; Q4KLH5; -.
DR OrthoDB; 1226524at2759; -.
DR PhylomeDB; Q4KLH5; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q4KLH5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISO:RGD.
DR GO; GO:0007289; P:spermatid nucleus differentiation; ISO:RGD.
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 Cytoplasmic vesicle; Developmental protein; Differentiation;
KW Direct protein sequencing; DNA-binding; Glycoprotein; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Spermatogenesis;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..561
FT /note="Arf-GAP domain and FG repeat-containing protein 1"
FT /id="PRO_0000227908"
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 171..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..451
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:0000250|UniProtKB:P52594"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52594"
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:0000269|PubMed:15340146"
SQ SEQUENCE 561 AA; 58170 MW; 28F272F60F518061 CRC64;
MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN
PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK
YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGESAPA LHLNKGTPTQ
SPVVGRSQGQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANAEF
ANFDAFGQSS GSSNFGGFPT ASHSPFQPQT TGGSAGSVNA NFAHFDNFPK SSSADFGSFS
TSQSHQTAST VSKVSTNKAG LQTADKYAAL ANLDNIFSAG QGGDQGSGFG TTGKAPVGSV
VSVPSHSSAS SDKYAALAEL DSVFSSAATS NNAYTSTSNA SSSVFGTVPV GASPQTQPAS
SGPAPFGATP STNPFVAATG PSAASSTNPF QTNARGATAA TFGTASMSMP AGFGTPAQYS
LPTSFSGSFQ QPPFPAQAAF PQQTAFSQQP NGAGFATFGQ TKPVVTPFGQ VAAAGVSSNP
FMTGAPTGQF PTGSSSTNPF L
