ID   RAGP1_XENLA             Reviewed;         580 AA.
AC   O13066;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Ran GTPase-activating protein 1;
DE            Short=RanGAP1;
GN   Name=rangap1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH
RP   RANBP2 AND UBE2I.
RC   TISSUE=Oocyte;
RX   PubMed=9108047; DOI=10.1073/pnas.94.8.3736;
RA   Saitoh H., Pu R., Cavenagh M., Dasso M.;
RT   "RanBP2 associates with Ubc9p and a modified form of RanGAP1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3736-3741(1997).
CC   -!- FUNCTION: GTPase activator for RAN, converting it to the GDP-bound
CC       state (PubMed:9108047). Converts cytoplasmic GTP-bound RAN to GDP-bound
CC       RAN, which is required for RAN-mediated nuclear import and export (By
CC       similarity). {ECO:0000250|UniProtKB:P46060,
CC       ECO:0000269|PubMed:9108047}.
CC   -!- SUBUNIT: Homodimer (By similarity). Identified in a complex with RANBP2
CC       and the ubiquitin-conjugating enzyme E2 (UBE2I) (PubMed:9108047).
CC       {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:9108047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46060}.
CC       Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P46060}. Nucleus envelope
CC       {ECO:0000250|UniProtKB:P46060}. Chromosome, centromere, kinetochore
CC       {ECO:0000250|UniProtKB:P46060}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250|UniProtKB:P46060}. Note=Cytoplasmic during interphase.
CC       Detected at the nuclear envelope during interphase. Targeted to the
CC       nuclear pores after sumoylation. During mitosis, associates with
CC       mitotic spindles, but is essentially not detected at the spindle poles.
CC       Mitotic location also requires sumoylation.
CC       {ECO:0000250|UniProtKB:P46060}.
CC   -!- PTM: May be sumoylated. {ECO:0000305|PubMed:9108047}.
CC   -!- SIMILARITY: Belongs to the RNA1 family. {ECO:0000305}.
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DR   EMBL; U88155; AAB62321.1; -; mRNA.
DR   AlphaFoldDB; O13066; -.
DR   SMR; O13066; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.25.40.200; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR009109; Ran_GTPase_activating_1_C.
DR   InterPro; IPR036720; RanGAP1_C_sf.
DR   Pfam; PF13516; LRR_6; 3.
DR   Pfam; PF07834; RanGAP1_C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF69099; SSF69099; 1.
PE   1: Evidence at protein level;
KW   Centromere; Chromosome; Cytoplasm; Cytoskeleton; GTPase activation;
KW   Kinetochore; Leucine-rich repeat; Nucleus; Reference proteome; Repeat;
KW   Ubl conjugation.
FT   CHAIN           1..580
FT                   /note="Ran GTPase-activating protein 1"
FT                   /id="PRO_0000056739"
FT   REPEAT          48..71
FT                   /note="LRR 1"
FT   REPEAT          111..134
FT                   /note="LRR 2"
FT   REPEAT          141..168
FT                   /note="LRR 3"
FT   REPEAT          207..230
FT                   /note="LRR 4"
FT   REPEAT          235..258
FT                   /note="LRR 5"
FT   REPEAT          292..315
FT                   /note="LRR 6"
FT   REPEAT          320..343
FT                   /note="LRR 7"
FT   REGION          356..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..398
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  62908 MW;  BE1ED7693E8FFE3E CRC64;
     MAAEDIAQLA DCLAKANVGD GELSFKGKTL KLNTAQDAEE VIREIEEYEG LQALRLEGNT
     VGVEAAKAIA EVLQRKPDLK RCHWSDMFTG RLRPEIPTAL RSLGDALITA GAQLTELDLS
     DNAFGPDGVR GFEALLKSPT CFTLQELKLN NCGMGIGGGK ILAAALTECH KKSSAHGKPL
     ALKVFIAGRN RLENDGATAL SEAFRLIGTL EEVHMPQNGI NHAGITALAE SFKANSLLKV
     INLNDNTFTE KGGVAMAEAL KTLRQVEVIN FGDCLVRSKG AQAIASALKE GLHKLKDLNL
     SYCEIKADAA VSLAESVEDK SDLEKLDLNG NCLGEEGCEQ VQEILESINM ANILGSLSDD
     EDEDDDDDDE DDDDDEDDEN DDEEVEEEEE EVEEEEGGDN ENKEKSKEIP CLSGSAPASP
     PKLPVDASTF LSFPSPEKLV RMGPRRSAMI AQQVNVADTE KVVQAFIQVS SVYREDGEIK
     AAVEETIDGL MKEAFENRGF QANVFITSLL VQMGLLKSED KMKTIPHLNG PLLTLNHMVQ
     QNYFPKSLAS TLLAFISKPN GVLENNASAR HTLLCNLHNL