ACAP1_BOVIN
ID ACAP1_BOVIN Reviewed; 745 AA.
AC A5PK26;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI42329.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI42329.1};
RC TISSUE=Thymus {ECO:0000312|EMBL:AAI42329.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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 (By similarity). {ECO:0000250|UniProtKB:Q15027}.
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 -!- PTM: Phosphorylation at Ser-555 by PKB is required for interaction with
CC ITGB1, export of ITGB1 from recycling endosomes to the cell surface and
CC ITGB1-dependent cell migration. {ECO:0000250|UniProtKB:Q15027}.
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DR EMBL; BC142328; AAI42329.1; -; mRNA.
DR RefSeq; NP_001096704.1; NM_001103234.1.
DR AlphaFoldDB; A5PK26; -.
DR SMR; A5PK26; -.
DR STRING; 9913.ENSBTAP00000034967; -.
DR PaxDb; A5PK26; -.
DR PRIDE; A5PK26; -.
DR GeneID; 508582; -.
DR KEGG; bta:508582; -.
DR CTD; 9744; -.
DR eggNOG; KOG0521; Eukaryota.
DR InParanoid; A5PK26; -.
DR OrthoDB; 751525at2759; -.
DR Proteomes; UP000009136; Unplaced.
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: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; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Endosome; Membrane; Metal-binding; Nitration; Phosphoprotein;
KW Reference proteome; Repeat; Transducer; Zinc; Zinc-finger.
FT CHAIN 1..745
FT /note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
FT containing protein 1"
FT /id="PRO_0000306383"
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 607..640
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 644..673
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 677..707
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..745
FT /note="Required for interaction with GULP1"
FT /evidence="ECO:0000250|UniProtKB:Q15027"
FT REGION 525..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..567
FT /note="Prevents interaction with ITGB1 when S-554 is not
FT phosphorylated"
FT /evidence="ECO:0000250"
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 MOD_RES 555
FT /note="Phosphoserine; by PKB"
FT /evidence="ECO:0000250|UniProtKB:Q15027"
SQ SEQUENCE 745 AA; 82129 MW; 715DDB3F83D823A8 CRC64;
MTVKLDFEEC LKDSPRFRAS VELVEAEVSE LETRLEKLLK LGNGLLESGR HYLAASRAFI
VGICDLAHLG PPEPMMAECL DKFTQSLSHK LDSHAELLDA TQHTLQRQIQ TLVKEGLRSF
REAGRDFWRG AESLEAALTH NAEVPRRRAQ EAEEAGAALK VARAGYRGRA LDYALQINVI
EDKRKFDIME FVLRLVEAQA THFQQGHEEL SQLAQYRKEL GGQLHQLVLN SAREKRDMEQ
RHVLLKQKEL GGEEPEPSLK EGPGGLVMEG HLFKRASNAF KTWSRRWFTI QSNQLVYQKR
YKDPVTVVVD DLRLCTVKLC PDSERRFCFE VVSPSKSCLL QSDSERLMQL WVSAVQSSIA
TAFSQARLDD SPRGLGQGSG HLAISSAATL GPGGLTRGRE PGGVGHVAAQ VQSVDGNAQC
CDCREPAPEW ASINLGVTLC IQCSGIHRSL GVHFSKVRSL TLDSWEPELV KLMCELGNVV
INQIYEARVE AMAVKKPGPS CSRQEKEAWI HAKYVEKKFL TKLPEIRGRR GGRGPPRGHP
PVPPKPGLIR PKPGSFRSKP EPPSEDLQSL HPGALLFRAA GHPPSLPTMA DALAHGADVN
WVNGGQENAT PLIQATAAVR VLNSLLACEF LLQNGANVNQ VDNQGRGPLH HATILGHTGL
ACLFLKRGAD LGVRDSEGRD PLTIAVETAN ADIVTLLRLA KMREADAAQG QAGDETYLDI
FRDFSLMASD DPEKLSRRSH DLHTL
