ARAP2_MOUSE
ID ARAP2_MOUSE Reviewed; 1703 AA.
AC Q8BZ05; Q80TX2; Q8C3T2; Q8VEL6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2;
DE AltName: Full=Centaurin-delta-1;
DE Short=Cnt-d1;
GN Name=Arap2; Synonyms=Centd1, Gm148, Kiaa0580;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1070 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Fetal lung, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 759-1703 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1530-1703 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1627, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-
CC activating protein that modulates actin cytoskeleton remodeling by
CC regulating ARF and RHO family members. Is activated by
CC phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can
CC be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2)
CC binding, albeit with lower efficiency (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZ05-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZ05-2; Sequence=VSP_014996, VSP_014997;
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DR EMBL; AK037027; BAC29675.1; -; mRNA.
DR EMBL; AK084988; BAC39331.1; -; mRNA.
DR EMBL; AK122316; BAC65598.1; -; mRNA.
DR EMBL; BC018234; AAH18234.1; -; mRNA.
DR CCDS; CCDS51506.1; -. [Q8BZ05-1]
DR AlphaFoldDB; Q8BZ05; -.
DR SMR; Q8BZ05; -.
DR STRING; 10090.ENSMUSP00000075924; -.
DR iPTMnet; Q8BZ05; -.
DR PhosphoSitePlus; Q8BZ05; -.
DR EPD; Q8BZ05; -.
DR MaxQB; Q8BZ05; -.
DR PaxDb; Q8BZ05; -.
DR PRIDE; Q8BZ05; -.
DR ProteomicsDB; 283195; -. [Q8BZ05-1]
DR ProteomicsDB; 283196; -. [Q8BZ05-2]
DR UCSC; uc008xlz.2; mouse. [Q8BZ05-2]
DR MGI; MGI:2684416; Arap2.
DR eggNOG; KOG1117; Eukaryota.
DR InParanoid; Q8BZ05; -.
DR PhylomeDB; Q8BZ05; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR ChiTaRS; Arap2; mouse.
DR PRO; PR:Q8BZ05; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BZ05; protein.
DR GO; GO:0005737; C:cytoplasm; 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:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04385; RhoGAP_ARAP; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 5.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037858; RhoGAP_ARAP.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 4.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 5.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 4.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTPase activation; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1703
FT /note="Arf-GAP with Rho-GAP domain, ANK repeat and PH
FT domain-containing protein 2"
FT /id="PRO_0000074213"
FT DOMAIN 6..70
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 480..572
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 585..677
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 674..809
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 899..1001
FT /note="PH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1012..1110
FT /note="PH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1114..1295
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 1324..1418
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 1428..1531
FT /note="PH 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 698..721
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 84..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..1519
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014996"
FT VAR_SEQ 1531..1575
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014997"
SQ SEQUENCE 1703 AA; 193398 MW; 0D99E59D35E0ABEB CRC64;
MSSVSEVNAD IRDFLMSINL EQYLLHFREF GFYTVRDCTS INDSVLHQIG ISPTGHRRRI
LKQLQMIFSK MQDFPIYANV HKAKNGSTTK EQQHSDPSSS THTGIECSDS ITVHRPGPAP
SEMVTTSTLS EGNCQSPKSH DKLCLSSHDL LCPEEELHQN VDSSKDSLFG GVNVKIDPLI
TKRAVEYTAG EEHTEKGNLT SEDSSKALST NTECLPSGDC PTSGTHSGNG TNGVLESFPP
TPFFQFQGEM VVNELYVPSS PVHGPMRSRS KLVSRPSRSF LLRHRPVPEI PGSTKSIPGS
YFRDRRSNTT SAGKSLTLKN SNEDNSTSIF PYGETFLFQR LESSKKRSIK NEFWPHENTV
KEEAATTRNS ILTQSSIYDN RKEKVSEDKV EDIWIPREDK NNLAQDSASE SEYSTVEECF
QSLRRKNSKA SKSRTQKAFY LDPFNRHSYP LSSTSGNTEP SSTISNAISP YACFYGSSAA
KEKCGWLDKL SPQGKRMFQK RWVKFDGLSI SHYNNDREMY SKGIIPLTAI STVRAQGDNK
FEIVTTQRTF VFRVEKEEER NDWISILLSA LKSPSLASQL QAAVAPEKCG YLELRGYKAK
IFTVLRGNSV WLCKNEQDFK SGLGITIIPM NVANVKQVDR AVKQSFEIIT PYRSFSFTAD
SEREKQEWIE AVQQSIAETL SDYEVAEKIW FNESNRSCAD CKAPDPDWAS INLCVVICKK
CAGQHRSLGP KDCKVRSLKM DASIWSNELI ELFIVIGNKR ANDFWAGNLQ KDEELQVDSP
VEKRKNFITQ KYKEGKFRKT LLASLTKEEL NKALCAAVVK PDVLETMALL FSGADVMCAT
GDPVHSTPYL LAKKAGQSLQ MEFLYHNKFS DFPQYDAHFE GGSSQDAAQS SFLCDFLYQT
AAAASRVSSE KKLLEDTNKK WCVLEGGFLS YYENDRCTTP NGTINISEVI CLAVHKEDFY
LNTGPIFVFE IYLPSERVFL FGAETSQIQR KWTETIAKRF VPFVAENLTE ADYDLIGQLF
YKDCHALDQW RKGWFAMDKS SLCFCLQTQE AQEERMNLRR LQELTISTMV QNGEKVDVLL
LVEKGRTLYI HGHTKLDFTV WHTAIEKAAG TDGNALQDQQ LCKNDVPIIV NSCIAFVTQY
GLGCKYIYQK DGDPLHISEL LESFKKDARS VKLRAGKHQL EDVTGVLKSF LSDIDDALLT
KELYPYWVSA LDTQDEKERT SKYRAFIRSL PGVNRATLAA LIEHLYRVQK CSEINHMNAH
NLAMVFSSCL FQTKGQTSEE VNVIEDLINN YVEIFEVKED QVKQMDIENS FITKWKDTQV
SQAGDLLIEV FVERKEPDCS IIIRISPVME AEELTNDILA IKNIIPMKGD IWATFEVIEN
EELERPLHYT ENVLEQVLQW SSLAEPGSAY LVVKRFLTVD SIKQCREKSI KEGILKLKEE
PSKILSGNKF QDRCVVLRDG HLFIYKDPKS SKHDKMFPLR AMKFYLGVKK KMKPPTSWGL
TVYSEKHHWH LCCDSLQAQM EWMASIFIAQ HENDIWPPAG KERKRSITKN PKIGGLPLIP
IQHERNATQA RKNIETARAE LERLRLSEKH DPRDFTDSSL KDRASLIAHC LEHKDEKLRN
RARKHRSFNC LEDTEAEGPH GLPKAYKGPK TLKKTEERNS KATLDADPKL PSKVIEELSV
VLQRSRPLHK ELPDEQTLQK EVK
