Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1

Gene

Acap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration (By similarity).By similarity1 Publication

Enzyme regulationi

GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri420 – 44324C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
Alternative name(s):
Centaurin-beta-1
Short name:
Cnt-b1
Gene namesi
Name:Acap1
Synonyms:Centb1, Kiaa0050Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2388270. Acap1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi448 – 4481R → Q: Loss of catalytic activity. No loss of accumulation of coat proteins on internal membranes upon overexpression of Acap1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1PRO_0000306384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei485 – 4851Nitrated tyrosineBy similarity

Keywords - PTMi

Nitration

Proteomic databases

EPDiQ8K2H4.
MaxQBiQ8K2H4.
PaxDbiQ8K2H4.
PRIDEiQ8K2H4.

PTM databases

iPTMnetiQ8K2H4.
PhosphoSiteiQ8K2H4.

Expressioni

Gene expression databases

BgeeiQ8K2H4.
CleanExiMM_CENTB1.
ExpressionAtlasiQ8K2H4. baseline and differential.
GenevisibleiQ8K2H4. MM.

Interactioni

Subunit structurei

Banana-shaped homodimer laterally assembling into tetramers, the tetramers further pack helically onto the membrane. Interacts with GTP-bound ARF6. Interacts with third cytoplasmic loop of SLC2A4/GLUT4. Interacts with CLTC. Interacts with GULP1. Forms a complex with GDP-bound ARF6 and GULP1. Interacts with ITGB1; required for ITGB1 recycling.By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001631.

Structurei

3D structure databases

ProteinModelPortaliQ8K2H4.
SMRiQ8K2H4. Positions 1-364, 405-723.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 226226BARSequence analysisAdd
BLAST
Domaini265 – 36096PHPROSITE-ProRule annotationAdd
BLAST
Domaini405 – 527123Arf-GAPPROSITE-ProRule annotationAdd
BLAST
Repeati606 – 63530ANK 1Sequence analysisAdd
BLAST
Repeati639 – 66830ANK 2Sequence analysisAdd
BLAST
Repeati672 – 70231ANK 3Sequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 382382Required for formation of endosomal tubules when overexpressed with PIP5K1CBy similarityAdd
BLAST
Regioni405 – 740336Required for interaction with GULP1By similarityAdd
BLAST
Regioni525 – 56642Prevents interaction with ITGB1 when S-554 is not phosphorylatedBy similarityAdd
BLAST

Domaini

PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate ACAP1-binding to PIP2 or PIP3 containing membranes. Only one PH domain of one ACAP1 dimer inserts into the membrane, while the other PH domain acts primaryly to interact with adjacent ACAP1 dimers (By similarity).By similarity
The BAR domain mediates homodimerization, it can neither bind membrane nor impart curvature, but instead requires the neighboring PH domain to achieve these functions (By similarity).By similarity

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation
Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
Contains 1 BAR domain.Sequence analysis
Contains 1 PH domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri420 – 44324C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0521. Eukaryota.
COG5347. LUCA.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000220815.
HOVERGENiHBG050889.
InParanoidiQ8K2H4.
KOiK12489.
OMAiFERRSEC.
OrthoDBiEOG7PVWNT.
PhylomeDBiQ8K2H4.
TreeFamiTF318315.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K2H4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVKLDFEEC LKDSPRFRAS IELVETEVSE LETRLEKLLK LGSCLLESGQ
60 70 80 90 100
HYLAAGRAFV VGICDLARLG PPEPMMAECL EKFTVSLNHK LDSHAELLDA
110 120 130 140 150
TQHTLQQQIQ TLVKEGLRGF REARRDFWRG AENLEAALTH NAEVPRRRVQ
160 170 180 190 200
EAEEAGTALR TARAGYRSRA LDYALQVNVI EDKRKFDIME FVLRLVEAQA
210 220 230 240 250
TYFQQGHEEL NRLAQYRKEL GTQLHNLVLN SARQKRDMEQ RHVLLKQKEL
260 270 280 290 300
GGEEPEPSLK EGPSGLVMEG HLFKRASNAF KTWSRRWFTI QNNQLVYQKK
310 320 330 340 350
YKDPVTVVVD DLRLCTVKLC PDSERRFCFE VVSTSKSCFL QADSERLLQL
360 370 380 390 400
WVSAVQSSIA SAFSQAHLEN SPRGPGQVSG YHAPGSAATL ACGGAARGRE
410 420 430 440 450
SGGVGQVAAQ VQSVDGNAQC CDCREPAPEW ASINLGVTLC IQCSGIHRSL
460 470 480 490 500
GVHFSKVRSL TLDSWEPELV KLMCELGNVI INQIYEARVE AMAVKKPGPS
510 520 530 540 550
CSRQEKEAWI HAKYVEKKFL TKLPEIRGRR GGRGPPRGHP PVPPKPPIRP
560 570 580 590 600
HSGIVRSKSE CPSDDMGSLH PGALLFQAAG HPPSLPTMAD ALAHGADVNW
610 620 630 640 650
VNVGQGNATP LIRATAANSL LACEFLLQNG ANVNQADSAG RGPLHHATIL
660 670 680 690 700
GHTGLACLFL KRGADLGARD TEGRDPLTIA METTNADIVT LLRLAKMREA
710 720 730 740
EAAQGQAGDE TYLDIFRDFS LMASDDPEKL SRRSHDLHTL
Length:740
Mass (Da):81,704
Last modified:October 1, 2002 - v1
Checksum:i798A87CBCC5F8513
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti522 – 5221K → R in BAE32594 (PubMed:16141072).Curated
Sequence conflicti584 – 5841S → H in BAD90138 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154449 mRNA. Translation: BAE32594.1.
AL596185, AL845465 Genomic DNA. Translation: CAI35146.1.
AL845465, AL596185 Genomic DNA. Translation: CAM13886.1.
BC031462 mRNA. Translation: AAH31462.1.
AK220213 mRNA. Translation: BAD90138.1.
CCDSiCCDS24919.1.
RefSeqiNP_722483.2. NM_153788.3.
UniGeneiMm.288671.

Genome annotation databases

EnsembliENSMUST00000001631; ENSMUSP00000001631; ENSMUSG00000001588.
GeneIDi216859.
KEGGimmu:216859.
UCSCiuc007jsf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154449 mRNA. Translation: BAE32594.1.
AL596185, AL845465 Genomic DNA. Translation: CAI35146.1.
AL845465, AL596185 Genomic DNA. Translation: CAM13886.1.
BC031462 mRNA. Translation: AAH31462.1.
AK220213 mRNA. Translation: BAD90138.1.
CCDSiCCDS24919.1.
RefSeqiNP_722483.2. NM_153788.3.
UniGeneiMm.288671.

3D structure databases

ProteinModelPortaliQ8K2H4.
SMRiQ8K2H4. Positions 1-364, 405-723.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001631.

PTM databases

iPTMnetiQ8K2H4.
PhosphoSiteiQ8K2H4.

Proteomic databases

EPDiQ8K2H4.
MaxQBiQ8K2H4.
PaxDbiQ8K2H4.
PRIDEiQ8K2H4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001631; ENSMUSP00000001631; ENSMUSG00000001588.
GeneIDi216859.
KEGGimmu:216859.
UCSCiuc007jsf.1. mouse.

Organism-specific databases

CTDi9744.
MGIiMGI:2388270. Acap1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0521. Eukaryota.
COG5347. LUCA.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000220815.
HOVERGENiHBG050889.
InParanoidiQ8K2H4.
KOiK12489.
OMAiFERRSEC.
OrthoDBiEOG7PVWNT.
PhylomeDBiQ8K2H4.
TreeFamiTF318315.

Miscellaneous databases

PROiQ8K2H4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K2H4.
CleanExiMM_CENTB1.
ExpressionAtlasiQ8K2H4. baseline and differential.
GenevisibleiQ8K2H4. MM.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NODImported.
    Tissue: Dendritic cell.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech IIImported.
    Tissue: Mammary glandImported.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Kitamura H., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 583-740.
    Tissue: Natural killer cellImported.
  5. "An ACAP1-containing clathrin coat complex for endocytic recycling."
    Li J., Peters P.J., Bai M., Dai J., Bos E., Kirchhausen T., Kandror K.V., Hsu V.W.
    J. Cell Biol. 178:453-464(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLTC AND SLC2A4, MUTAGENESIS OF ARG-448.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiACAP1_MOUSE
AccessioniPrimary (citable) accession number: Q8K2H4
Secondary accession number(s): Q3U441, Q571H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Cells overexpressing Acap1 show accumulation of an electron dense coat containing Acap1 and Cltc on internal membranes as well as accumulation of Tfrc in pericentriolar recycling endosomes. Adipocytes with reduced level of Acap1 or Cltc fail to transport SLC2A4/GLUT4 from recycling endosomes to the cell surface upon insulin stimulation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.