ACAP2_CHICK
ID ACAP2_CHICK Reviewed; 781 AA.
AC Q5ZK62;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
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; ORFNames=RCJMB04_12p24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|EMBL:CAG31881.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG31881.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG31881.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
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DR EMBL; AJ720222; CAG31881.1; -; mRNA.
DR RefSeq; NP_001006548.1; NM_001006548.1.
DR AlphaFoldDB; Q5ZK62; -.
DR SMR; Q5ZK62; -.
DR BioGRID; 685213; 1.
DR STRING; 9031.ENSGALP00000011389; -.
DR PaxDb; Q5ZK62; -.
DR PRIDE; Q5ZK62; -.
DR Ensembl; ENSGALT00000011404; ENSGALP00000011390; ENSGALG00000007040.
DR GeneID; 424895; -.
DR KEGG; gga:424895; -.
DR CTD; 23527; -.
DR VEuPathDB; HostDB:geneid_424895; -.
DR eggNOG; KOG0521; Eukaryota.
DR GeneTree; ENSGT00940000156389; -.
DR HOGENOM; CLU_012513_0_1_1; -.
DR InParanoid; Q5ZK62; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q5ZK62; -.
DR TreeFam; TF318315; -.
DR PRO; PR:Q5ZK62; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000007040; Expressed in colon and 12 other tissues.
DR ExpressionAtlas; Q5ZK62; baseline and differential.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW ANK repeat; Coiled coil; Endosome; GTPase activation; Membrane;
KW Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..781
FT /note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
FT containing protein 2"
FT /id="PRO_0000306388"
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..521
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 642..671
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 675..704
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 708..737
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 365..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 88454 MW; C0B1285AB9E762BC CRC64;
MKVTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCLANKQFM
NGIRDLAQYS CKDALVETNL TKFSDTLQEM INYHNILFDQ TQRSIKAQLQ TFVKEDIKKF
KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEATNILT ATRKCFRHIA LDYVLQINVL
QSKRRSEILK SMLSFMYAHL TFFHQGYDLF SELGPYMKDL GAQLDQLAVD AAKEKRDMEQ
KHSTIQQKDY SGDDTKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
ATAYREKGDE SEKQEKKSSP STGSLESGSE TKEKLLKGES ALQRVQCIPG NAACCDCGLA
DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDSWE PELLKLMCEL GNDVINRIYE
AKLEKMGVKK PQPGSQRQEK EMYIKAKYVE RKFVEKQPAA AVSPLESRTK VLPQSQEEKR
HSAPEKSFLA IEQGAASPRV RSSDSGIQQS VDDSREHLAS TISANSLYEP EGEKQESSVF
YDSRQLNPGL HLYRAAFEKN LPDMAEALAH GAEVNWVNME ENKATPLIQA VRGGSLVTCE
FLLQNGANVN IRDMKGRGPL HHATVLGHTG QVCLFLKRGA NQHATDEDGK DPLSIAVEAA
NADIVTLLRL ARMNEEMRES EGLYGQPGDE IYQDIFRDFS QMASNNPEKL NRFQQSDSQK
P
