ACAP2_RABIT
ID ACAP2_RABIT Reviewed; 778 AA.
AC Q6IVG4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
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;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1] {ECO:0000312|EMBL:AAT11274.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney {ECO:0000269|PubMed:16039000};
RX PubMed=16039000; DOI=10.1016/j.virusres.2005.06.003;
RA Bradley R.R., Terajima M.;
RT "Vaccinia virus K1L protein mediates host-range function in RK-13 cells via
RT ankyrin repeat and may interact with a cellular GTPase-activating
RT protein.";
RL Virus Res. 114:104-112(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 -!- 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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
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DR EMBL; AY620244; AAT11274.1; -; mRNA.
DR RefSeq; NP_001075643.1; NM_001082174.1.
DR AlphaFoldDB; Q6IVG4; -.
DR SMR; Q6IVG4; -.
DR STRING; 9986.ENSOCUP00000001546; -.
DR PRIDE; Q6IVG4; -.
DR GeneID; 100008949; -.
DR KEGG; ocu:100008949; -.
DR CTD; 23527; -.
DR eggNOG; KOG0521; Eukaryota.
DR InParanoid; Q6IVG4; -.
DR OrthoDB; 751525at2759; -.
DR Proteomes; UP000001811; Unplaced.
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; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..778
FT /note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
FT containing protein 2"
FT /id="PRO_0000306386"
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 640..669
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 673..702
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 706..735
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 518..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQK5"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQK5"
FT MOD_RES 742
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15057"
SQ SEQUENCE 778 AA; 87901 MW; 9ECA111F71E99A74 CRC64;
MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCLANKQFM
NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF
KDAKKQFEKV SEEKENALAK NAQVQRNKQH EVEEATNILT ATRKCFRHIA LDYVLQINVL
QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ
KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCVPG NASCCDCGLA
DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE
ANVEKMGIKK PQPGQRQEKE AYIKAKYVER KFVDKYSVSS SPPEQEKKVV SKDSEEKRLS
IPKLGPGDQV RTSIQSSVKS NDSGIQQSSD DGRESLPSTV SANSLYEPEG ERQDSSVFLD
SKHLNPGLQL YRASYEKNLP KMAEALAHGA DVNWANSEEN KATPLIQAVL GGSLVTCEFL
LQNGANVNQR DVQGRGPLHH ATVLGHTGQV CLFLKRGANQ HATDEEGKDP LSIAVEAANA
DIVTLLRLAR MNEEMRESEG LYGQPGDETY QDIFRDFSQM ASNNPEKLNR FQQDSQKF
