ID F1LXQ7_RAT Unreviewed; 1955 AA.
AC F1LXQ7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 3.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Rho GTPase activating protein 21 {ECO:0000313|Ensembl:ENSRNOP00000060787.3};
GN Name=Arhgap21 {ECO:0000313|Ensembl:ENSRNOP00000060787.3,
GN ECO:0000313|RGD:1311028};
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:ENSRNOP00000060787.3, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000060787.3, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060787.3,
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:16641100}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3] {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 [4] {ECO:0000313|Ensembl:ENSRNOP00000060787.3}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000060787.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic
CC vesicle membrane {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00004284}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004395}.
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DR AlphaFoldDB; F1LXQ7; -.
DR SMR; F1LXQ7; -.
DR STRING; 10116.ENSRNOP00000060787; -.
DR iPTMnet; F1LXQ7; -.
DR PhosphoSitePlus; F1LXQ7; -.
DR PaxDb; 10116-ENSRNOP00000060787; -.
DR Ensembl; ENSRNOT00000068156.4; ENSRNOP00000060787.3; ENSRNOG00000008659.8.
DR AGR; RGD:1311028; -.
DR RGD; 1311028; Arhgap21.
DR eggNOG; KOG4407; Eukaryota.
DR GeneTree; ENSGT00940000155406; -.
DR HOGENOM; CLU_001776_0_0_1; -.
DR InParanoid; F1LXQ7; -.
DR TreeFam; TF329345; -.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000008659; Expressed in cerebellum and 19 other cell types or tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0051683; P:establishment of Golgi localization; ISO:RGD.
DR GO; GO:0051645; P:Golgi localization; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0051684; P:maintenance of Golgi location; ISO:RGD.
DR GO; GO:0072384; P:organelle transport along microtubule; ISO:RGD.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01253; PH_ARHGAP21-like; 1.
DR CDD; cd04395; RhoGAP_ARHGAP21; 1.
DR Gene3D; 1.20.5.220; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23175; PDZ DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23175:SF16; RHO GTPASE-ACTIVATING PROTEIN 21; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1LXQ7};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 57..166
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 937..1046
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1153..1345
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 33..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1854..1955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1859..1907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1914..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1955 AA; 216376 MW; 91B221F777223D4A CRC64;
MAQFRLLDCM MNHNWSLLCN LYCAWSGQVS KNKDGKEQGE PVSPSEDESF SWPGPKTVML
KRTSQGFGFT LRHFIVYPPE SAIQFSYKDE ENGNRGGKQR NRLEPMDTIF VKQVKEGGPA
FEAGLCTGDR IIKVNGESVI GKTYSQVIAL IQNSDTTLEL SVMPKDEDIL QVLQFTKDVT
ALAYSQDAYL KGNGAYSGNA RDIPEPPPVC YPWLPATPSA TAQPVEVSPP DSLLNKQQTS
TPVLTQPGRA YRMEIQVPPS PTDVAKSNTA VCVCSESVRT VIVPSEKVVD LLANRNSPSG
PAHRTEEVRY GVSDQASAKA AARTTPPPSA PTARLSHQTI GSRSLEPSGI LLKSGNYSGH
SEGISSSRSQ AVDSPPVSVN HYSANSHQHI DWKNYKTYKE YIDNRRLHIG CRTIQERLDS
LRAASQSAAD YNQVVPARTA LQVRRRSTSH DRVPQSIQIR QRSVSQERLE DSVLMKYCPR
SASQGALTSP PVSFSNHRTR SWDYIEGQSE ATATVNSESQ TPDSNGERKQ TYKWSGFTEQ
DDRRGIHERP RQQEMHKPFR GSNLTVAPVV NSDNRRLGGR GVGPVSQFKK IPPDLRPPHS
NRNFPTTSGM SLPRGIAQDR SPLVKVRSNS LKALPPPVPK PSFSQHSLAS TKDQRPVNHL
HQHGLLSQQT RGRPESTFPH LELQTDVSPS LPGTSAKTSP QLSENLGTSD LDLHASPRNG
DVDSQEADVQ PSDVPDNKES VILREKPQPG RQTPQPLRHQ SYILAVNDQE TGSDPTCWLP
NDARREVHIK RMEERKASCT SPPGDSLASI PFIDEPTSPS IDHEVAHIPA SAVISASTSQ
VPSIATVPPS LTTSAPLIRR QLSHDQESVG PPSLDGQHTS KTERSKSYDE GLDDYREDAK
LSFKHVSSLK GIKIADSQKS SEDSGSRKDS SSEVFSDAAK EGWLQFRPLV TDKGKRVGGS
IRPWKQMYVV LRGHSLYLYK DRREQTTPSE EEQPISVNAC LIDISYSETK RRNVFRLTTS
DCECLFQAED RDDMLAWIKT IQESSNLNEE DTGVTNRDLI SRRIKEYNSL LSKTEQLPKT
PRQSLSIRQT LLGAKSEPKT QSPHSPKEES ERKLLSKDDT SPPKDKGTWR RGIPSIVRKT
FEKKPAATGT FGVRLDDCPP AHTNRYIPLI VDICCKLVEE RGLEYTGIYR VPGNNAAISS
MQEELNKGMA DIDIQDDKWR DLNVISSLLK SFFRKLPEPL FTNDKYADFI EANRKEDPLD
RLRTLKRLIH DLPEHHFETL KFLSAHLKTV AENSEKNKME PRNLAIVFGP TLVRTSEDNM
THMVTHMPDQ YKIVETLIQH HDWFFTEEGA EEPLTAVQEE NTVDSQPVPN IDHLLTNIGR
TGVLPGDVSD SATSDSTKSK GSWGSGKDQY SRELLVSSIF AAASRKRKKP KEKAQPSSSE
DELDSVFFKK ENMEPSHSEI KEESKRESET PGRKQRVVVA KDSNTKKDTG TTKEEKKMPS
DEPSPPHSSK RNRSPTLSCR LAMLKESPRS LLTQKPHCEE TGSDSGTLSS QASLARSSTK
KSTSPETRHT EFLSNAGTIT SDYSTTSSTT YLTSLDSSRL SPEVQSVAES KGDEADDERS
ELVSEGRPVE TDSESEFPVF PSALTSGQFR GKLQEVARSS RRNSEGSEAS CTEGSLTPSL
DSRRQQFSSH RLIECDTLSR KKSARFKSDS GSPGDTRTEK ETPALAKMFD VMKKGKSTGS
LLTPSRSESE KQEATWKTKI ADRLKLRPRA PADDMFGVGN QKPTAETAKR KNIKRRHTLG
GHRDATEISV LSFWKAQEQS ADKESELSAV NRLKPKCSAQ DLSISDWLAR ERIRSSASDL
SRSEGCEPQA ESPSVLGTPT STHTPPPSQQ PEARAAASTS ASTSQPPLST PPQSPDQING
DSFQNTSQNA SSAANAHPHK LSESPNTKTE SPPCL
//
