ACAP1_MOUSE
ID ACAP1_MOUSE Reviewed; 740 AA.
AC Q8K2H4; Q3U441; Q571H6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1;
DE AltName: Full=Centaurin-beta-1;
DE Short=Cnt-b1;
GN Name=Acap1; Synonyms=Centb1, Kiaa0050 {ECO:0000312|EMBL:BAD90138.1};
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:0000312|EMBL:BAE32594.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD {ECO:0000312|EMBL:BAE32594.1}; TISSUE=Dendritic cell;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAH31462.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH31462.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH31462.1};
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] {ECO:0000305, ECO:0000312|EMBL:CAI35146.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 583-740.
RC TISSUE=Natural killer cell {ECO:0000312|EMBL:BAD90138.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Kitamura H., Nagase T.,
RA Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CLTC AND SLC2A4, AND MUTAGENESIS OF ARG-448.
RX PubMed=17664335; DOI=10.1083/jcb.200608033;
RA Li J., Peters P.J., Bai M., Dai J., Bos E., Kirchhausen T., Kandror K.V.,
RA Hsu V.W.;
RT "An ACAP1-containing clathrin coat complex for endocytic recycling.";
RL J. Cell Biol. 178:453-464(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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: GTPase-activating protein (GAP) for ADP ribosylation factor 6
CC (ARF6) required for clathrin-dependent export of proteins from
CC recycling endosomes to trans-Golgi network and cell surface. Required
CC for regulated export of ITGB1 from recycling endosomes to the cell
CC surface and ITGB1-dependent cell migration (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:17664335}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) and phosphatidic acid.
CC {ECO:0000250|UniProtKB:Q15027}.
CC -!- SUBUNIT: Banana-shaped homodimer laterally assembling into tetramers,
CC the tetramers further pack helically onto the membrane. Interacts with
CC GTP-bound ARF6. Interacts with third cytoplasmic loop of SLC2A4/GLUT4.
CC Interacts with CLTC. Interacts with GULP1. Forms a complex with GDP-
CC bound ARF6 and GULP1. Interacts with ITGB1; required for ITGB1
CC recycling. {ECO:0000250|UniProtKB:Q15027, ECO:0000269|PubMed:17664335}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- DOMAIN: PH domain binds phospholipids including phosphatidic acid,
CC phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate
CC (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate
CC ACAP1-binding to PIP2 or PIP3 containing membranes. Only one PH domain
CC of one ACAP1 dimer inserts into the membrane, while the other PH domain
CC acts primaryly to interact with adjacent ACAP1 dimers (By similarity).
CC {ECO:0000250|UniProtKB:Q15027}.
CC -!- DOMAIN: The BAR domain mediates homodimerization, it can neither bind
CC membrane nor impart curvature, but instead requires the neighboring PH
CC domain to achieve these functions (By similarity).
CC {ECO:0000250|UniProtKB:Q15027}.
CC -!- MISCELLANEOUS: Cells overexpressing Acap1 show accumulation of an
CC electron dense coat containing Acap1 and Cltc on internal membranes as
CC well as accumulation of Tfrc in pericentriolar recycling endosomes.
CC Adipocytes with reduced level of Acap1 or Cltc fail to transport
CC SLC2A4/GLUT4 from recycling endosomes to the cell surface upon insulin
CC stimulation.
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DR EMBL; AK154449; BAE32594.1; -; mRNA.
DR EMBL; AL596185; CAI35146.1; -; Genomic_DNA.
DR EMBL; AL845465; CAI35146.1; JOINED; Genomic_DNA.
DR EMBL; AL845465; CAM13886.1; -; Genomic_DNA.
DR EMBL; AL596185; CAM13886.1; JOINED; Genomic_DNA.
DR EMBL; BC031462; AAH31462.1; -; mRNA.
DR EMBL; AK220213; BAD90138.1; -; mRNA.
DR CCDS; CCDS24919.1; -.
DR RefSeq; NP_722483.2; NM_153788.3.
DR AlphaFoldDB; Q8K2H4; -.
DR SMR; Q8K2H4; -.
DR IntAct; Q8K2H4; 1.
DR STRING; 10090.ENSMUSP00000001631; -.
DR iPTMnet; Q8K2H4; -.
DR PhosphoSitePlus; Q8K2H4; -.
DR EPD; Q8K2H4; -.
DR MaxQB; Q8K2H4; -.
DR PaxDb; Q8K2H4; -.
DR PRIDE; Q8K2H4; -.
DR ProteomicsDB; 285833; -.
DR Antibodypedia; 24069; 249 antibodies from 34 providers.
DR DNASU; 216859; -.
DR Ensembl; ENSMUST00000001631; ENSMUSP00000001631; ENSMUSG00000001588.
DR GeneID; 216859; -.
DR KEGG; mmu:216859; -.
DR UCSC; uc007jsf.1; mouse.
DR CTD; 9744; -.
DR MGI; MGI:2388270; Acap1.
DR VEuPathDB; HostDB:ENSMUSG00000001588; -.
DR eggNOG; KOG0521; Eukaryota.
DR GeneTree; ENSGT00940000160289; -.
DR InParanoid; Q8K2H4; -.
DR OMA; QATYFQQ; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q8K2H4; -.
DR TreeFam; TF318315; -.
DR BioGRID-ORCS; 216859; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8K2H4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K2H4; protein.
DR Bgee; ENSMUSG00000001588; Expressed in granulocyte and 73 other tissues.
DR Genevisible; Q8K2H4; MM.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
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; 1.
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 ANK repeat; Endosome; Lipid degradation; Lipid metabolism; Membrane;
KW Metal-binding; Nitration; Reference proteome; Repeat; Transducer; Zinc;
KW Zinc-finger.
FT CHAIN 1..740
FT /note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
FT containing protein 1"
FT /id="PRO_0000306384"
FT DOMAIN 1..226
FT /note="BAR"
FT /evidence="ECO:0000255"
FT DOMAIN 265..360
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 405..527
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 606..635
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 639..668
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 672..702
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT ZN_FING 420..443
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 1..382
FT /note="Required for formation of endosomal tubules when
FT overexpressed with PIP5K1C"
FT /evidence="ECO:0000250|UniProtKB:Q15027"
FT REGION 405..740
FT /note="Required for interaction with GULP1"
FT /evidence="ECO:0000250|UniProtKB:Q15027"
FT REGION 525..566
FT /note="Prevents interaction with ITGB1 when S-554 is not
FT phosphorylated"
FT /evidence="ECO:0000250"
FT REGION 525..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 485
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15027"
FT MUTAGEN 448
FT /note="R->Q: Loss of catalytic activity. No loss of
FT accumulation of coat proteins on internal membranes upon
FT overexpression of Acap1."
FT /evidence="ECO:0000269|PubMed:17664335"
FT CONFLICT 522
FT /note="K -> R (in Ref. 1; BAE32594)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="S -> H (in Ref. 4; BAD90138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 740 AA; 81704 MW; 798A87CBCC5F8513 CRC64;
MTVKLDFEEC LKDSPRFRAS IELVETEVSE LETRLEKLLK LGSCLLESGQ HYLAAGRAFV
VGICDLARLG PPEPMMAECL EKFTVSLNHK LDSHAELLDA TQHTLQQQIQ TLVKEGLRGF
REARRDFWRG AENLEAALTH NAEVPRRRVQ EAEEAGTALR TARAGYRSRA LDYALQVNVI
EDKRKFDIME FVLRLVEAQA TYFQQGHEEL NRLAQYRKEL GTQLHNLVLN SARQKRDMEQ
RHVLLKQKEL GGEEPEPSLK EGPSGLVMEG HLFKRASNAF KTWSRRWFTI QNNQLVYQKK
YKDPVTVVVD DLRLCTVKLC PDSERRFCFE VVSTSKSCFL QADSERLLQL WVSAVQSSIA
SAFSQAHLEN SPRGPGQVSG YHAPGSAATL ACGGAARGRE SGGVGQVAAQ VQSVDGNAQC
CDCREPAPEW ASINLGVTLC IQCSGIHRSL GVHFSKVRSL TLDSWEPELV KLMCELGNVI
INQIYEARVE AMAVKKPGPS CSRQEKEAWI HAKYVEKKFL TKLPEIRGRR GGRGPPRGHP
PVPPKPPIRP HSGIVRSKSE CPSDDMGSLH PGALLFQAAG HPPSLPTMAD ALAHGADVNW
VNVGQGNATP LIRATAANSL LACEFLLQNG ANVNQADSAG RGPLHHATIL GHTGLACLFL
KRGADLGARD TEGRDPLTIA METTNADIVT LLRLAKMREA EAAQGQAGDE TYLDIFRDFS
LMASDDPEKL SRRSHDLHTL
