ID F1MAA5_RAT Unreviewed; 584 AA.
AC F1MAA5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=RAN GTPase activating protein 1 {ECO:0000313|Ensembl:ENSRNOP00000050029.5};
GN Name=Rangap1 {ECO:0000313|Ensembl:ENSRNOP00000050029.5,
GN ECO:0000313|RGD:1310380};
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 {ECO:0000313|Ensembl:ENSRNOP00000050029.5, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000050029.5, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000050029.5,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
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).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000050029.5}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000050029.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; F1MAA5; -.
DR STRING; 10116.ENSRNOP00000050029; -.
DR PaxDb; 10116-ENSRNOP00000050029; -.
DR PeptideAtlas; F1MAA5; -.
DR Ensembl; ENSRNOT00000052098.6; ENSRNOP00000050029.5; ENSRNOG00000031789.6.
DR AGR; RGD:1310380; -.
DR RGD; 1310380; Rangap1.
DR eggNOG; KOG1909; Eukaryota.
DR GeneTree; ENSGT00440000039203; -.
DR HOGENOM; CLU_028747_2_0_1; -.
DR InParanoid; F1MAA5; -.
DR OrthoDB; 3025421at2759; -.
DR TreeFam; TF318283; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-RNO-9793242; SUMOylation of nuclear envelope proteins.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000031789; Expressed in testis and 19 other cell types or tissues.
DR ExpressionAtlas; F1MAA5; baseline and differential.
DR GO; GO:1904115; C:axon cytoplasm; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:1990723; C:cytoplasmic periphery of the nuclear pore complex; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0072686; C:mitotic spindle; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005643; C:nuclear pore; IDA:RGD.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0106068; C:SUMO ligase complex; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IDA:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IDA:RGD.
DR GO; GO:1904117; P:cellular response to vasopressin; IEP:RGD.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; ISO:RGD.
DR GO; GO:0051168; P:nuclear export; ISO:RGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; ISO:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00116; LRR_RI; 1.
DR Gene3D; 1.25.40.200; Ran-GTPase activating protein 1, C-terminal domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR009109; Ran_GTPase_activating_1_C.
DR InterPro; IPR027038; RanGap.
DR InterPro; IPR036720; RanGAP1_C_sf.
DR PANTHER; PTHR24113; RAN GTPASE-ACTIVATING PROTEIN 1; 1.
DR PANTHER; PTHR24113:SF5; RAN GTPASE-ACTIVATING PROTEIN 1; 1.
DR Pfam; PF13516; LRR_6; 3.
DR Pfam; PF07834; RanGAP1_C; 1.
DR SMART; SM00368; LRR_RI; 8.
DR SUPFAM; SSF69099; Ran-GTPase activating protein 1 (RanGAP1), C-terminal domain; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
PE 1: Evidence at protein level;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 408..581
FT /note="Ran-GTPase activating protein 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07834"
FT REGION 354..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..397
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 62898 MW; 0BC998916294861B CRC64;
MASEDIAKLA ETLAKTQVAG GQLSFKGKGL KLNTAAKDVI KEIEEFDGLE ALRLEGNTVG
VEAARVIAKA LEKKSKLKRC HWSDMFTGRL RSEIPPALIS LGEGLITAGA QLVELDLSDN
AFGPDGVRGF EALLKSPACF TLQELKLNNC GMGIGGGKIL AAALTECHRK SSAQGKPLTL
KVFVAGRNRL ENDGATALAE AFGIIGTLEE VHMPQNGINH PGVTALAQAF AINPLLRVIN
LNDNTFTEKG GVAMAETLKT LRQVEVINFG DCLVRSKGAV AIADAVRGGL PKLKELNLSF
CEIKRDAALV VAEAVADKAE LEKLDLNGNA LGEEGCEQLQ EVLDSFNMAK VLASLSDDEG
EDEDEDEEGE DDEDEEDEEE EEEEEEEEEE EEEEPQQRGS GEEPATPSRK ILDPNSGEPA
PVLSSPPPTD LSTFLSFPSP EKLLRLGPKV SVLIVQQTDT SDPEKVVSAF LKVASVFRDE
ASVKTAVLDA IDALMKKAFS SSSFNSNTFL TRLLIHMGLL KSEDKIKAIP SLHGPLMVLN
HVVQQDYFPK TLAPLLLAFV TKPNGALESC SFARHSLLQT LYSI
//
