ACAP2_MOUSE
ID ACAP2_MOUSE Reviewed; 770 AA.
AC Q6ZQK5; Q3UHL4; Q811F3; Q9CTS8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2;
DE AltName: Full=Centaurin-beta-2;
DE Short=Cnt-b2;
GN Name=Acap2; Synonyms=Centb2, Kiaa0041 {ECO:0000312|EMBL:BAC97851.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAC97851.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC97851.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE27843.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE27843.1};
RC TISSUE=Urinary bladder {ECO:0000312|EMBL:BAB32141.3};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAH46455.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 405-770.
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH46455.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH46455.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-734, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; SER-387; SER-573 AND
RP SER-576, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [7]
RP INTERACTION WITH RAB35 AND MICALL1.
RX PubMed=23572513; DOI=10.1242/jcs.117846;
RA Kobayashi H., Fukuda M.;
RT "Rab35 establishes the EHD1-association site by coordinating two distinct
RT effectors during neurite outgrowth.";
RL J. Cell Sci. 126:2424-2435(2013).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6
CC (ARF6). {ECO:0000250|UniProtKB:Q15057}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) and phosphatidic acid.
CC {ECO:0000250|UniProtKB:Q15057}.
CC -!- SUBUNIT: Interacts with RAB35 (GTP-bound form); the interaction is
CC direct and probably recruits ACAP2 to membranes. Interacts with
CC MICALL1; the interaction is indirect through RAB35.
CC {ECO:0000269|PubMed:23572513}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:14621295};
CC IsoId=Q6ZQK5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q6ZQK5-2; Sequence=VSP_052554;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97851.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129041; BAC97851.1; ALT_INIT; mRNA.
DR EMBL; AK020591; BAB32141.3; -; mRNA.
DR EMBL; AK147319; BAE27843.1; -; mRNA.
DR EMBL; BC046455; AAH46455.1; -; mRNA.
DR CCDS; CCDS49823.1; -. [Q6ZQK5-1]
DR RefSeq; NP_084414.1; NM_030138.2. [Q6ZQK5-1]
DR AlphaFoldDB; Q6ZQK5; -.
DR SMR; Q6ZQK5; -.
DR BioGRID; 219526; 1.
DR STRING; 10090.ENSMUSP00000061501; -.
DR iPTMnet; Q6ZQK5; -.
DR PhosphoSitePlus; Q6ZQK5; -.
DR EPD; Q6ZQK5; -.
DR jPOST; Q6ZQK5; -.
DR MaxQB; Q6ZQK5; -.
DR PaxDb; Q6ZQK5; -.
DR PeptideAtlas; Q6ZQK5; -.
DR PRIDE; Q6ZQK5; -.
DR ProteomicsDB; 285834; -. [Q6ZQK5-1]
DR ProteomicsDB; 285835; -. [Q6ZQK5-2]
DR Antibodypedia; 19460; 219 antibodies from 36 providers.
DR DNASU; 78618; -.
DR Ensembl; ENSMUST00000058033; ENSMUSP00000061501; ENSMUSG00000049076. [Q6ZQK5-2]
DR Ensembl; ENSMUST00000230614; ENSMUSP00000154983; ENSMUSG00000049076. [Q6ZQK5-1]
DR GeneID; 78618; -.
DR KEGG; mmu:78618; -.
DR UCSC; uc007yxb.1; mouse. [Q6ZQK5-1]
DR UCSC; uc007yxc.1; mouse. [Q6ZQK5-2]
DR CTD; 23527; -.
DR MGI; MGI:1925868; Acap2.
DR VEuPathDB; HostDB:ENSMUSG00000049076; -.
DR eggNOG; KOG0521; Eukaryota.
DR GeneTree; ENSGT00940000156389; -.
DR HOGENOM; CLU_012513_0_1_1; -.
DR InParanoid; Q6ZQK5; -.
DR OMA; GSVMSCE; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q6ZQK5; -.
DR TreeFam; TF318315; -.
DR BioGRID-ORCS; 78618; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Acap2; mouse.
DR PRO; PR:Q6ZQK5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6ZQK5; protein.
DR Bgee; ENSMUSG00000049076; Expressed in stroma of bone marrow and 225 other tissues.
DR ExpressionAtlas; Q6ZQK5; baseline and differential.
DR Genevisible; Q6ZQK5; MM.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0030029; P:actin filament-based process; ISO:MGI.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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 PANTHER; PTHR23180; PTHR23180; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Coiled coil; Endosome; GTPase activation;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..770
FT /note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
FT containing protein 2"
FT /id="PRO_0000306385"
FT DOMAIN 1..226
FT /note="BAR"
FT /evidence="ECO:0000255"
FT DOMAIN 266..361
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 399..520
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 632..661
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 665..694
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 698..727
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT ZN_FING 414..437
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 371..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 734
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
FT VAR_SEQ 78..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052554"
FT CONFLICT 526
FT /note="E -> K (in Ref. 3; AAH46455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 770 AA; 87211 MW; 8882864BB7D248F2 CRC64;
MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM
NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF
KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEAANILT ATRKCFRHIA LDYVLQINVL
QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ
KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
KFKDSPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NTSCCDCGLA
DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE
AKLEKMGVKK PQPGQRQEKE AYIRAKYVER KFVDKYSALL SPSEQEKRII SKSCEDQRLS
HARASVHTPV KSNDSGIQQC SEDGRESLPS TVSANSLYEP EGERQESSVF LDSKHLNPGL
QLYRASYEKN LPKMAEALAH GADVNWANSD ENQATPLIQA VLGGSLVTCE FLLQNGANVN
QRDVQGRGPL HHATVLGHTG QVCLFLKRGA NQHATDEEGK DPLSIAVEAA NADIVTLLRL
ARMNEEMRES EGLYGQPGDE TYQDIFRDFS QMASNNPEKL NRFQQDSQKF