ID   AGFG1_BOVIN             Reviewed;         562 AA.
AC   Q2TA45;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 113.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Rumen reticulum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
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; BC111120; AAI11121.1; -; mRNA.
DR   RefSeq; NP_001033260.1; NM_001038171.2.
DR   AlphaFoldDB; Q2TA45; -.
DR   STRING; 9913.ENSBTAP00000028427; -.
DR   iPTMnet; Q2TA45; -.
DR   PaxDb; Q2TA45; -.
DR   PeptideAtlas; Q2TA45; -.
DR   PRIDE; Q2TA45; -.
DR   GeneID; 536149; -.
DR   KEGG; bta:536149; -.
DR   CTD; 3267; -.
DR   eggNOG; KOG0702; Eukaryota.
DR   HOGENOM; CLU_027801_1_0_1; -.
DR   InParanoid; Q2TA45; -.
DR   OrthoDB; 1226524at2759; -.
DR   TreeFam; TF325357; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Developmental protein; Differentiation; DNA-binding;
KW   Glycoprotein; Metal-binding; 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_0000227907"
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          168..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..194
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:0000250"
SQ   SEQUENCE   562 AA;  58134 MW;  6F9432B51C98DD53 CRC64;
     MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN
     PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK
     YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGDSAPA LHLNKGTPSQ
     SPVVGRSQAQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANADF
     ANFDAFGQSS GSSNFGGFPT ASHSSFQPQT TGGSAGSVNA NFAHFDNFPK SSSADFGTFN
     TSQSHQTASA VSKVSANKAG LQTTDKYAAL ANLDNIFSAG QGGDQGSGFG TTGKAPVGSV
     VSVPSQSSAS SDKYAALAEL DSVFSSAATS SNAYTSTSNA SSNVFGTVPV GASAQTQPAS
     SSVPAPFGAT PSTNPFVAAA GPSVASSTNP FQTNARGATA ATFGTASMSM PAGFGTPAPY
     SLPTSFSGSF QQPAFPAQAA FPQQTAFSQQ PNGAGFAAFG QTKPVVTPFG QVGAAGVSSN
     PFMTGAPTGQ FPTGSSSTNP FL