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   24-JAN-2024, entry version 147.
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,
RC   Pancreas, 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; 2.
DR   STRING; 10090.ENSMUSP00000154983; -.
DR   GlyGen; Q6ZQK5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6ZQK5; -.
DR   PhosphoSitePlus; Q6ZQK5; -.
DR   EPD; Q6ZQK5; -.
DR   jPOST; Q6ZQK5; -.
DR   MaxQB; Q6ZQK5; -.
DR   PaxDb; 10090-ENSMUSP00000061501; -.
DR   PeptideAtlas; Q6ZQK5; -.
DR   ProteomicsDB; 285834; -. [Q6ZQK5-1]
DR   ProteomicsDB; 285835; -. [Q6ZQK5-2]
DR   Pumba; Q6ZQK5; -.
DR   Antibodypedia; 19460; 238 antibodies from 36 providers.
DR   DNASU; 78618; -.
DR   Ensembl; ENSMUST00000058033.9; ENSMUSP00000061501.9; ENSMUSG00000049076.13. [Q6ZQK5-2]
DR   Ensembl; ENSMUST00000230614.2; ENSMUSP00000154983.2; ENSMUSG00000049076.13. [Q6ZQK5-1]
DR   GeneID; 78618; -.
DR   KEGG; mmu:78618; -.
DR   UCSC; uc007yxb.1; mouse. [Q6ZQK5-1]
DR   UCSC; uc007yxc.1; mouse. [Q6ZQK5-2]
DR   AGR; MGI:1925868; -.
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; DWEPEIL; -.
DR   OrthoDB; 1449795at2759; -.
DR   PhylomeDB; Q6ZQK5; -.
DR   TreeFam; TF318315; -.
DR   BioGRID-ORCS; 78618; 3 hits in 79 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 228 other cell types or tissues.
DR   ExpressionAtlas; Q6ZQK5; baseline and differential.
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   CDD; cd08851; ArfGap_ACAP2; 1.
DR   CDD; cd07638; BAR_ACAP2; 1.
DR   CDD; cd13250; PH_ACAP; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR004148; BAR_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR23180:SF241; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF16746; BAR_3; 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; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 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.
DR   Genevisible; Q6ZQK5; MM.
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
//