ID D4AAI2_RAT Unreviewed; 1117 AA. AC D4AAI2; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 2. DT 27-MAR-2024, entry version 107. DE SubName: Full=Rho GTPase activating protein 45 {ECO:0000313|Ensembl:ENSRNOP00000057381.3}; GN Name=Arhgap45 {ECO:0000313|Ensembl:ENSRNOP00000057381.3, GN ECO:0000313|RGD:1308662}; 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:ENSRNOP00000057381.3, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000057381.3, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000057381.3, 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: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:ENSRNOP00000057381.3} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000057381.3}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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 AlphaFoldDB; D4AAI2; -. DR STRING; 10116.ENSRNOP00000057381; -. DR iPTMnet; D4AAI2; -. DR PhosphoSitePlus; D4AAI2; -. DR PaxDb; 10116-ENSRNOP00000057381; -. DR PeptideAtlas; D4AAI2; -. DR Ensembl; ENSRNOT00000060648.4; ENSRNOP00000057381.3; ENSRNOG00000013220.8. DR UCSC; RGD:1308662; rat. DR AGR; RGD:1308662; -. DR RGD; 1308662; Arhgap45. DR VEuPathDB; HostDB:ENSRNOG00000013220; -. DR eggNOG; KOG1453; Eukaryota. DR GeneTree; ENSGT00950000183110; -. DR HOGENOM; CLU_006236_0_1_1; -. DR InParanoid; D4AAI2; -. DR OrthoDB; 5395569at2759; -. DR TreeFam; TF351450; -. DR Reactome; R-RNO-6798695; Neutrophil degranulation. DR Reactome; R-RNO-8980692; RHOA GTPase cycle. DR Reactome; R-RNO-9013148; CDC42 GTPase cycle. DR Reactome; R-RNO-9013149; RAC1 GTPase cycle. DR Proteomes; UP000002494; Chromosome 7. DR Bgee; ENSRNOG00000013220; Expressed in thymus and 19 other cell types or tissues. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd20816; C1_GMIP-like; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR031160; F_BAR. DR InterPro; IPR001060; FCH_dom. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR PANTHER; PTHR15228:SF18; RHO GTPASE-ACTIVATING PROTEIN 45; 1. DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00055; FCH; 1. DR SMART; SM00324; RhoGAP; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR PROSITE; PS51741; F_BAR; 1. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 269..539 FT /note="F-BAR" FT /evidence="ECO:0000259|PROSITE:PS51741" FT DOMAIN 700..745 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 759..972 FT /note="Rho-GAP" FT /evidence="ECO:0000259|PROSITE:PS50238" FT REGION 1..109 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 423..458 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 572..623 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1004..1034 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1051..1117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 381..408 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 16..36 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 45..67 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 443..458 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1076..1098 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1117 AA; 123149 MW; 46BD3E5CF7022D81 CRC64; MFSRKKRELM KTPSISKKNR AGSPNPQSSS GELPRKDCTE TPSLEPPAMS LSTVAKGTGT LKRPTSLSRH ASAAGFPLSG TATRTLGRGY RSPLSAASPA ELPTEGPFPD GVEDISTLLA DVARFAEGLE KLKEFVLRDA DLLEARRPLA HECLGEALRV MRQVISKYPL LNTVETLTAA GTLIAKVKAF HYECNNESDK REFEKALETI AVSFSCTVSE FLLGEVDSST LLAVPPGDPS QLVENLYGSG SEGPPHSVED CEEGCLPPEE VDMLLQRCEG GVDAALQYAK DMARYMKDLI GYLEKRTTLE MEFAKGLQKV VHNCRQNVTH APHMPLLSIY SLALEQDLEF GHGMVQAVGT LQTQTFMQPL TLRRLEHERR RKEIKESWHR AQRKLQEAEA NLRKAKQGYK QRCEDHDKAR LQVAKAEEEQ QGTGPGAGTA ASKALDKRRR LEEEAKNKAE EAMATYRTCV ADAKTQKQEL EDTKVTALRQ IQEVIRQSDQ TIKSATISYY QLMHMQTAPL PVNFQMLCES SKLYDPGQQY ASHVRQLQRG EEPDVRYDFE PYVSTNAWSP IMRTRKGSFN PGDASGPEAA GSPPEEGGTS EGAPNKDHRG GRGHQVHKSW PISISDTEVS LDVSSGDLKK FDRTSSSGTM SSNEELVDQE AGLVASAFDS ADLNGMDPEL PVAMPSGPFR HVGLSKAART HRLRKLRTPA KCRECNSYVY FQGAECEECC LACHKKCLET LAIQCGHKKL QGRLQLFGQD FSQAAHSTPD GVPFIIKKCV CEIERRALHT KGIYRVNGVK TRVEKLCQAF ENGKELVELS QASPHDISNV LKLYLRQLPE PLISFRFYHE LVGLAKDSLK AEAEAKAASR GRQDGSESEA ATLAMVGRLR ELMRDLPAEN RATLLYLLRH LRRIVEMEQD NKMTPGNLGI VFGPTLLRPR PTDATVSLSS LVDYPHQARV IETLIVHYGL VFEEEPEEAA GSQEGASAQC AQLETAEGIV FPQQEEADDG NRESQVASND SDSELEEASD LLSSSDASAL HRLSFLEQTE AGLEEGPQSH SGSEEQLESE DAAPGHQLCS FNTNQSNNTT QASLPTMRLR DGQITGGSGR KRQPQFV //